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SCARB1

SCARB1, or scavenger receptor class B member 1, is a gene located on chromosome 12q24.31 that encodes the scavenger receptor class B type I (SR-BI), a multifunctional transmembrane glycoprotein essential for lipid metabolism, particularly the selective uptake of cholesteryl esters from high-density lipoprotein (HDL) without endocytosis of the lipoprotein particle itself.^[1]^[2] SR-BI is an 82-84 kDa protein consisting of 409 or 509 amino acid isoforms, featuring two transmembrane domains, short intracellular N- and C-terminal tails, and a large extracellular domain rich in glycosylation sites that facilitates ligand binding and lipid transfer through a hydrophobic tunnel.^[1]^[2] It forms oligomers, which enhance its function, and interacts with adaptor proteins like PDZK1 to stabilize expression, particularly in the liver.^[2] The receptor is highly expressed in the liver, adrenal glands, ovaries, and testes, with lower levels in macrophages, endothelial cells, and adipocytes, where its expression is regulated by transcription factors such as SREBP-1, LXRα, and PPARα, as well as hormones like ACTH and estrogen.^[2]^[1] The primary physiological role of SR-BI is mediating reverse cholesterol transport by facilitating the bidirectional flux of free cholesterol and selective uptake of cholesteryl esters, phospholipids, triglycerides, and lipophilic vitamins (A and D) from HDL, thereby delivering cholesterol to the liver for biliary excretion and to steroidogenic tissues for hormone synthesis.^[2]^[1] In addition to HDL, SR-BI binds modified low-density lipoproteins (LDL), very low-density lipoproteins (VLDL), and lipoprotein(a) [Lp(a)], promoting their clearance and reducing plasma lipid levels, while also enabling cholesterol efflux from macrophages to mitigate foam cell formation in atherosclerosis.^[2] Beyond lipid homeostasis, SR-BI serves as a sensor of plasma membrane cholesterol content, influences cellular signaling pathways (e.g., via PI3K/Akt and eNOS activation), and facilitates entry of pathogens like hepatitis C virus and dengue virus into host cells.^[2] Genetic variants in SCARB1, such as the missense mutations P297S and P376L, are associated with elevated HDL cholesterol levels but paradoxically increased risk of coronary heart disease due to impaired SR-BI function in lipid delivery.^[1]^[3] These polymorphisms also influence responses to dietary fats, postprandial lipemia, and conditions like infertility and cancer progression, underscoring SR-BI's broad impact on metabolic and inflammatory diseases.^[4]^[5]

Gene and Protein Overview

Gene Structure and Location

The SCARB1 gene is located on the long arm of human chromosome 12 at the q24.31 cytogenetic band, spanning genomic positions 124,776,856 to 124,863,864 on the GRCh38.p14 reference assembly, which corresponds to approximately 87 kilobase pairs (kb).^[6] In mice, the orthologous Scarb1 gene resides on chromosome 5 at positions 125,354,151 to 125,418,082 on the GRCm39 assembly, encompassing about 64 kb.^[7] The human SCARB1 gene consists of 13 exons and 12 introns, with the canonical transcript (ENST00000261693.11) encoding the full-length SR-BI protein.^[8] Alternative splicing of the gene produces multiple isoforms, including the predominant SR-BI isoform and the shorter SR-BII isoform, which results from skipping of exon 12 and features a distinct C-terminal domain.^[9] Similarly, the mouse Scarb1 gene shares this 13-exon structure and undergoes comparable alternative splicing to generate SR-BI and SR-BII variants.^[2] A notable common polymorphism in SCARB1 is rs5888 (c.889C>T, p.Pro297Ser) in exon 8, with the minor allele frequency (T) reported at approximately 0.35 in global populations based on gnomAD exome data and ranging from 0.22 in East Asians to 0.46 in Europeans.^[10] This variant has been extensively studied for its potential functional implications, though its direct effects on protein activity remain under investigation in genetic association contexts. The proximal promoter region of SCARB1, spanning about 2.2 kb upstream of the transcription start site, contains sterol regulatory elements (SREs) that bind sterol regulatory element-binding proteins (SREBPs), particularly SREBP-2, to mediate cholesterol-responsive transcriptional activation.^[11] Additional regulatory elements include estrogen response element half-sites in both promoter and intronic regions, which facilitate estrogen-dependent regulation, as well as distal enhancers identified through genomic surveys that influence tissue-specific expression.^[2] These elements collectively ensure dynamic control of SCARB1 transcription in response to lipid homeostasis cues.

Protein Structure and Domains

The scavenger receptor class B type I (SR-BI), encoded by SCARB1, is a 509-amino-acid glycoprotein with an approximate molecular weight of 57 kDa prior to post-translational modifications. It adopts a topology typical of class B scavenger receptors, featuring short intracellular N- and C-terminal domains flanking two transmembrane-spanning helices (residues 82–104 and 431–453, approximately 22 and 23 amino acids long, respectively). These are connected by a large extracellular loop comprising about 408 residues, which forms the primary site for ligand interaction. The N-terminal cytoplasmic domain spans 9 amino acids, while the C-terminal domain extends 44 amino acids, both oriented toward the cytosol.^[2] Key structural domains of SR-BI include the cytoplasmic termini, which mediate intracellular signaling and interactions with adaptor proteins such as PDZK1, and the extensive extracellular domain, which contains cysteine-rich motifs and a hydrophobic tunnel that facilitates selective uptake of lipophilic molecules. The extracellular region exhibits sequence variability across species and isoforms, contributing to ligand specificity for diverse partners like high-density lipoprotein (HDL) and phospholipids. Additionally, the protein includes conserved charged residues (e.g., Glu96, Arg98, Lys117) lining a potential conduit for cholesterol transport within the extracellular loop.^[2]^[12] Post-translational modifications significantly influence SR-BI stability and localization. The protein undergoes N-linked glycosylation at 11 sites, with Asn-108 and Asn-173 being particularly critical; mutations at these positions impair plasma membrane trafficking, reduce protein stability, and diminish lipid transfer efficiency. These glycans, along with disulfide bonds formed by six conserved cysteines in the extracellular domain, enhance structural integrity and protect against degradation. Fatty acylation may also occur, further modulating membrane association.^[2]^[13] SR-BI exists in multiple isoforms generated by alternative splicing, primarily SR-BI (full-length, 509 amino acids) and SR-BII (475 amino acids). The isoforms share identical N-termini, transmembrane domains, and extracellular loops but differ in their C-termini due to splicing exclusion of exon 12 in SR-BII, resulting in a unique 40-amino-acid tail (ending in SAMA) instead of the 44-amino-acid tail of SR-BI (ending in EAKL). This alteration eliminates PDZK1-binding motifs in SR-BII, affecting signaling and localization. Expression ratios vary by tissue; SR-BII typically constitutes 5–40% of total SR-B in human liver (∼13–20%) and steroidogenic tissues like adrenal glands and ovaries, with higher relative abundance in testis.^[2]^[12]

Physiological Functions

Role in Lipid Metabolism

SCARB1, encoding the scavenger receptor class B type I (SR-BI), plays a central role in lipid metabolism by facilitating the selective uptake of cholesteryl esters (CEs) from high-density lipoprotein (HDL) particles into cells without degrading or internalizing the entire lipoprotein particle. This non-endocytic process involves the binding of HDL to the extracellular domain of SR-BI, which forms a hydrophobic channel or tunnel that allows the transfer of CEs directly to the plasma membrane, where they are subsequently internalized by the cell.^[14]^[15] The efficiency of this uptake is proportional to the CE content in HDL and is particularly prominent in tissues such as the liver and steroidogenic organs, where it supports cholesterol delivery for essential physiological functions.^[15] A key aspect of SR-BI's function is its contribution to reverse cholesterol transport (RCT), the pathway that removes excess cholesterol from peripheral tissues and delivers it to the liver for excretion in bile. SR-BI promotes the efflux of free cholesterol from cells, such as macrophages in arterial walls, to lipid-poor apolipoprotein A-I or HDL particles, initiating the transport process. In the liver, SR-BI then mediates the selective uptake of HDL-derived cholesterol, enabling its conversion to bile acids or direct biliary secretion, thereby preventing cholesterol accumulation and reducing the risk of atherosclerosis.^[2] Studies in SR-BI-deficient models demonstrate impaired RCT and elevated plasma HDL cholesterol levels, underscoring its critical role in maintaining cholesterol homeostasis.^[2] Beyond HDL, SR-BI interacts with other lipoproteins, including low-density lipoprotein (LDL), very low-density lipoprotein (VLDL), and lipoprotein(a (Lp(a)), by binding them with varying affinities and facilitating selective lipid uptake. This binding modulates plasma lipoprotein levels; for instance, hepatic overexpression of SR-BI enhances the clearance of LDL and VLDL, lowering their circulating concentrations, while also promoting the uptake of oxidized or acetylated forms of LDL in certain cellular contexts.^[16] For Lp(a), SR-BI serves as a receptor that supports the selective transfer of associated lipids, contributing to its hepatic catabolism and influencing overall plasma Lp(a) dynamics.^[16] These interactions highlight SR-BI's multifunctional nature in lipoprotein metabolism. The expression of SCARB1 is subject to regulatory feedback by intracellular cholesterol levels through the sterol regulatory element-binding protein (SREBP) pathway, ensuring adaptive control of lipid uptake. When cholesterol is depleted, SREBP-1 (and to some extent SREBP-2) translocates to the nucleus and binds to specific sterol regulatory elements in the SCARB1 promoter, upregulating gene transcription to increase SR-BI-mediated uptake. Conversely, high intracellular cholesterol suppresses SREBP processing and activation, leading to downregulation of SCARB1 expression and preventing excessive cholesterol accumulation. This feedback mechanism is evident in liver and steroidogenic tissues, where it fine-tunes cholesterol influx in response to cellular needs.^[2]^[17]

Interactions with Vitamins and Carotenoids

SCARB1, encoding the scavenger receptor class B type I (SR-BI), mediates the selective uptake of lipophilic vitamins, including vitamins A, D, and E, from high-density lipoprotein (HDL) particles. For vitamin A, SR-BI facilitates the cellular uptake of provitamin A carotenoids such as beta-carotene, supporting its conversion to retinol for vision and immune functions. Similarly, SR-BI contributes to the delivery of vitamin D, with deficiencies in SR-BI leading to reduced serum and tissue levels of 25-hydroxyvitamin D3, impacting bone health and calcium homeostasis.^[1]^[18]^[19] SR-BI facilitates the selective uptake of fat-soluble vitamin E, particularly alpha-tocopherol, from high-density lipoprotein (HDL) particles into enterocytes and other cells, thereby enhancing its bioavailability and contributing to cellular protection against oxidative stress.^[20] This process is mediated by SR-BI's interaction with HDL-bound alpha-tocopherol, where inhibitors such as BLT1 block up to 80% of uptake in intestinal models, underscoring SR-BI's critical role in intestinal absorption.^[21] In maternal-embryonic transfer, SR-BI supports vitamin E provision during development, with deficiencies impairing neural tube closure in mouse models.^[22] SR-BI also enables the transport of carotenoids, including lutein, zeaxanthin, and beta-carotene, via selective uptake from HDL and other carriers, with a preference for macular xanthophylls like lutein and zeaxanthin over beta-carotene in overexpression studies.^[23] This function is essential for carotenoid deposition in tissues, notably contributing to pigmentation in birds, where SCARB1 mutations abolish yellow, orange, and red feather coloration by disrupting carotenoid uptake and transport.^[24] In mammals, SR-BI similarly promotes carotenoid absorption in the gut and peripheral tissues, linking it to antioxidant defense and visual health.^[25] The uptake mechanism for both vitamins and carotenoids mirrors SR-BI's non-endocytic selective transfer of HDL-derived lipids, involving a hydrophobic channel in the receptor's extracellular domain that allows direct lipid diffusion into the plasma membrane without lipoprotein internalization.^[26] This pathway exploits SR-BI's lipid-binding affinity, enabling efficient delivery of hydrophobic nutrients while retaining the carrier particle.^[27] In SR-BI knockout models, such as Scarb1^{-/-} mice, vitamin E bioavailability is markedly reduced in tissues like the liver and brain, leading to abnormal alpha-tocopherol metabolism and heightened oxidative stress due to diminished antioxidant enzyme activity.^[28]^[29] Similarly, carotenoid uptake is impaired, resulting in lower tissue levels and compromised antioxidant status, as evidenced by reduced provitamin A carotenoid absorption and pigmentation defects in avian mutants.^[25]^[30] These findings highlight SR-BI's auxiliary role in maintaining nutrient-dependent antioxidant homeostasis.

Expression and Regulation

Tissue and Cellular Distribution

SCARB1 exhibits high expression levels in several key tissues, particularly the liver where it is abundantly present in hepatocytes to facilitate cholesterol handling, as well as in steroidogenic tissues such as the adrenal glands, ovaries, and testes.^[2] In the adrenal glands, expression is prominent in the zona fasciculata-reticularis cells, while in the ovaries, it occurs in granulosa and theca-interstitial cells, supporting cholesterol delivery for hormone synthesis.^[2] Moderate expression is observed in the intestine and macrophages, contributing to lipid processing in these sites.^[2] At the cellular level, the SCARB1 protein localizes primarily to the plasma membrane of polarized cells, where it functions as an integral receptor.^[31] In enterocytes, it shows a specific apical distribution along the brush-border membrane, positioning it for interaction with luminal contents.^[32] Expression of SCARB1 is tightly regulated by various factors, including transcriptional activators and dietary influences. PPAR-alpha agonists, such as fibrates, upregulate SCARB1 promoter activity through PPARα/RXR heterodimers, enhancing hepatic expression.^[33] Estrogen similarly induces upregulation, particularly in steroidogenic tissues, via estrogen receptor-mediated mechanisms that influence splicing and overall levels.^[34] In conditions like type 2 diabetes mellitus and insulin resistance, SCARB1 expression is reduced in hepatic cells, associated with hyperglycemia, while high-fat diets can suppress expression in the liver through altered lipid signaling pathways.^[35] SCARB1 produces two main isoforms, SR-BI and SR-BII, differing in their C-terminal domains due to alternative splicing. SR-BI predominates in steroidogenic tissues like the liver, adrenals, and ovaries, comprising the majority of protein (up to 95% in some sites).^[2] In contrast, SR-BII is less abundant overall and shows relatively higher expression in some non-steroidogenic tissues, though it exhibits lower efficiency in lipid uptake compared to SR-BI.^[36]

Species Distribution and Evolutionary Conservation

The SCARB1 gene, encoding the scavenger receptor class B type 1 (SR-BI), is widely distributed across vertebrate species, with expression identified in mammals, birds, reptiles, amphibians, and various fish, including teleosts like goldfish and amphibians like frogs, as well as cartilaginous fish such as sharks and skates.^[37] In non-mammalian vertebrates, SR-BI is prominently expressed in the liver of species including chickens, frogs, goldfish, sharks, and skates, indicating an early emergence in vertebrate evolution. This broad presence underscores its conserved role in lipid handling across diverse vertebrate lineages. In non-mammalian species, SCARB1 plays specialized physiological roles beyond basic lipid metabolism. For instance, in birds, SCARB1 is essential for carotenoid-based coloration, as demonstrated by a loss-of-function mutation in the canary that impairs yellow feather pigmentation by disrupting carotenoid uptake.^[24] In reptiles, such as the painted turtle (Chrysemys picta), SR-BI expression is upregulated in the ovary during egg development, correlating with increased cholesterol efflux to support vitellogenesis.^[37] Additionally, in Chinese soft-shelled turtle (Pelodiscus sinensis) embryos, SCARB1 exhibits dynamic expression patterns that covary with skin carotenoid content and xanthophore development during pigmentation formation.^[38] At the sequence level, SCARB1 demonstrates high evolutionary conservation among vertebrates, particularly in its extracellular domain, which shares approximately 80-90% amino acid identity across mammalian and non-mammalian species, facilitating conserved functions in cholesterol transport.^[39] Overall sequence identity among vertebrate SCARB1 orthologs ranges from 50% to 99%, reflecting strong selective pressure on core structural elements. In contrast, SCARB1 is absent in invertebrates, though functional homologs like ninaD in Drosophila mediate similar carotenoid transport, suggesting divergence after the vertebrate-invertebrate split.^[40] Evolutionarily, SCARB1 belongs to the CD36 gene family, arising from ancient gene duplication events in an ancestral vertebrate genome that generated the paralogs SCARB1, SCARB2, and CD36, enabling diversification of scavenger receptor functions in lipid and nutrient handling.^[41] This duplication likely occurred prior to the divergence of major vertebrate clades, as evidenced by the presence of family members in both jawed and jawless vertebrates.^[41]

Disease Associations

Cardiovascular and Metabolic Disorders

SCARB1 variants, particularly the rs5888 single nucleotide polymorphism (SNP), have been associated with elevated high-density lipoprotein cholesterol (HDL-C) levels and increased lipoprotein(a [Lp(a)] concentrations, contributing to a distinct lipid phenotype. The T allele of rs5888 is linked to higher HDL-C and larger HDL particle sizes, which may offer protection against atherosclerosis by enhancing reverse cholesterol transport, though it also raises the risk of hyperalphalipoproteinemia, a condition characterized by excessively high HDL-C that paradoxically correlates with increased cardiovascular events in some populations.^[42]^[43]^[44] Additionally, this variant influences Lp(a) metabolism, as SCARB1 facilitates selective uptake of cholesteryl esters from Lp(a), and its dysfunction leads to accumulation of this atherogenic particle.^[44]^[45] Reduced SR-B1 activity, often due to genetic polymorphisms in SCARB1, plays a role in metabolic syndrome by promoting dyslipidemia and insulin resistance. Studies indicate that lower SR-B1 expression disrupts HDL-mediated cholesterol efflux, leading to altered lipid profiles with elevated triglycerides and reduced HDL functionality, which exacerbate insulin resistance in adipose and hepatic tissues.^[46]^[47] In individuals with type 2 diabetes, SCARB1 variants are associated with low HDL-C and heightened insulin resistance, underscoring the receptor's contribution to the metabolic disturbances characteristic of the syndrome.^[35]^[48] Animal models, particularly SCARB1 knockout mice, demonstrate the consequences of SR-B1 deficiency on cardiovascular and metabolic health, exhibiting nearly doubled plasma HDL-C levels and impaired cholesterol efflux from macrophages, which accelerates atherosclerosis despite the hyperalphalipoproteinemia. These mice also show disrupted lipid homeostasis, with increased free cholesterol bioavailability in tissues, contributing to pathological lipid accumulation.^[49]^[50]^[51] Recent studies, including those from 2021 to 2024 in American Heart Association journals, have confirmed SCARB1 variants' role in novel phenotypes involving concurrently high HDL-C and Lp(a), with rare compound heterozygous mutations linked to severe premature coronary artery disease, highlighting the dual-edged impact of SR-B1 dysfunction on lipid-related cardiovascular risks.^[52]^[53] These findings emphasize the need for genotype-specific risk stratification in metabolic disorders.^[54]

Infectious Diseases

SCARB1, also known as scavenger receptor class B type I (SR-BI), serves as a critical co-receptor facilitating the entry of hepatitis C virus (HCV) into hepatocytes. It interacts with HCV glycoproteins E1 and E2, in conjunction with CD81, to enable viral attachment and internalization via clathrin-dependent endocytosis.^[55] Blockade of SCARB1, through antibodies or RNA interference, significantly reduces HCV infection efficiency in cell culture models, highlighting its essential role in viral uptake.^[56] In bacterial infections, SCARB1 promotes the endocytosis of pathogens such as Escherichia coli in epithelial cells, particularly through association with lipid rafts and coordination with Toll-like receptor 4 (TLR4) signaling. This mechanism enhances bacterial internalization and activates downstream inflammatory pathways like NF-κB, aiding host defense during mammary gland infections.^[57] SCARB1's involvement extends to other bacteria by binding lipopolysaccharides (LPS), the endotoxin component of Gram-negative bacterial cell walls, which facilitates LPS uptake and modulates innate immune responses.^[58] SCARB1 also contributes to the entry of additional pathogens, including dengue virus and malaria parasites. For dengue virus, SCARB1 acts as a binding receptor for the nonstructural protein NS1 on hepatic and mosquito cells, potentially promoting viral dissemination.^[59] In malaria, SCARB1 enhances hepatocyte permissiveness to Plasmodium sporozoites, boosting invasion and early liver-stage development across species like P. falciparum and P. berghei. In immune cells such as macrophages, SCARB1 expression supports pathogen clearance by mediating uptake of microbial components and triggering pro-inflammatory signaling. However, this receptor can also enable viral persistence; for instance, in HCV infection, SCARB1 facilitates viral RNA uptake and maintenance in macrophages, altering cholesterol metabolism and impairing antiviral responses.

Cancer and Other Pathologies

Oncogenic Roles

SCARB1, encoding the scavenger receptor class B type 1 (SR-B1), is frequently overexpressed in various malignancies, where it facilitates selective uptake of high-density lipoprotein (HDL)-derived cholesterol to support tumor cell proliferation. In breast cancer, elevated SR-B1 levels enhance cholesterol influx, promoting cell growth and survival by maintaining lipid homeostasis essential for rapid division.^[5] Similarly, in prostate cancer, SR-B1 upregulation drives steroidogenic and nonsteroidogenic cholesterol metabolism, enabling androgen-independent tumor progression and increased proliferative capacity.^[60] In nasopharyngeal carcinoma (NPC), SR-B1 overexpression correlates with advanced disease stages, supplying cholesterol that fuels metabolic demands for uncontrolled growth.^[61] SR-B1 contributes to cancer metastasis, particularly through its incorporation into extracellular vesicles (EVs) secreted by tumor cells. In NPC, SCARB1-enriched EVs are internalized by macrophages, co-regulating M1 and M2 polarization to suppress antitumor immunity and enhance invasive potential; this mechanism was elucidated in a 2023 study showing that SCARB1-EVs upregulate CYP1B1 in M2 macrophages, impairing phagocytosis and promoting tumor dissemination.^[61] SR-B1 activates key oncogenic signaling pathways, notably the PI3K/Akt axis, which supports tumor cell survival and resistance to apoptosis. Overexpression of SR-B1 in response to HDL binding triggers PI3K/Akt phosphorylation, driving proliferation and migration in breast and prostate cancers.^[62] This pathway activation is linked to poor clinical outcomes, with high SR-B1 expression associating with aggressive tumor behavior, lymph node metastasis, and reduced overall survival across multiple cancer types, including breast, prostate, and NPC.^[63] As a biomarker, elevated SR-B1 levels hold diagnostic and prognostic value in several cancers. In ovarian cancer, high SR-B1 expression in tumor cells and ascites fluid indicates advanced disease and immune evasion, serving as a potential marker for metastasis risk.^[62] In lung cancer, SR-B1 overexpression correlates with tumor aggressiveness and poorer prognosis, enabling its use in identifying high-risk patients.^[64]

Emerging Associations

Recent studies have implicated SCARB1 in neurological disorders, particularly through its role in amyloid-beta (Aβ) clearance mechanisms in the brain. SCARB1, expressed on astrocytes and involved in Aβ binding on microglia, contributes to Aβ clearance, with impairment potentially contributing to synaptic dysfunction and neuronal loss in Alzheimer's disease (AD) pathology.^[65] Additionally, genetic variants in SCARB1, such as rs5888, have been linked to dyslipidemia and elevated risk of mild cognitive impairment (MCI) in the elderly, with carriers showing higher plasma total cholesterol and HDL-cholesterol levels that correlate with cognitive decline.^[66] In autoimmune and inflammatory conditions, SCARB1 influences disease progression independent of its primary lipid transport functions. In atherosclerosis, SCARB1 deficiency leads to elevated free cholesterol bioavailability, which drives inflammatory responses in the arterial wall, including increased endothelial dysfunction and leukocyte recruitment beyond mere lipid accumulation.^[50] Similarly, in rheumatoid arthritis (RA), SCARB1 is upregulated in synovial tissue and mediates serum amyloid A (A-SAA)-induced inflammation by promoting cytokine production (IL-6, IL-8) and adhesion molecule expression (ICAM-1, VCAM-1) in fibroblasts and endothelial cells, exacerbating joint inflammation.^[67] SCARB1 also shows emerging ties to carotenoid-related pathologies, notably age-related macular degeneration (AMD). The rs5888 variant in SCARB1 increases susceptibility to AMD by impairing selective uptake of macular carotenoids like lutein and zeaxanthin, which protect against oxidative damage in the retina; heterozygous CT carriers exhibit a 2.9- to 3.6-fold higher risk of advanced or exudative AMD.^[68] In infectious contexts, recent investigations (2023–2025) highlight SCARB1's role in bacterial sepsis, where hepatic SCARB1 facilitates lipopolysaccharide (LPS) clearance and modulates inflammatory responses; its deficiency heightens susceptibility to sepsis-induced mortality by impairing cholesterol efflux, glucocorticoid synthesis, and nitric oxide cytotoxicity protection in models like cecal ligation and puncture.^[69] Updates on lipoprotein(a) [Lp(a)] associations reveal SCARB1 variants elevating both HDL-cholesterol and Lp(a) levels through reduced receptor-mediated clearance, conferring increased cardiovascular risk via pro-atherogenic and prothrombotic effects independent of traditional lipid profiles.^[70] Furthermore, SCARB1 influences inflammation in non-oncologic settings, such as diet-induced obesity, where its deficiency exacerbates inflammatory dyslipidemia and adipocyte hypertrophy.^[71]

Research and Therapeutic Potential

Preclinical Studies

Preclinical studies on SCARB1, encoding the scavenger receptor class B type 1 (SR-B1), have primarily utilized genetic knockout models and cell-based assays to elucidate its roles in lipid metabolism, viral entry, and cellular signaling. In SR-B1-deficient (SR-B1^{-/-}) mice, plasma high-density lipoprotein cholesterol (HDL-C) levels are markedly elevated, accompanied by enlarged, cholesterol-rich HDL particles that impair reverse cholesterol transport.^[72]^[73] These models exhibit female infertility due to dysfunctional HDL and ovarian cholesterol dysregulation, highlighting SR-B1's essential function in steroidogenesis and reproduction.^[74] Additionally, SR-B1^{-/-} mice demonstrate resistance to hepatitis C virus (HCV) infection, as SR-B1 facilitates viral entry into hepatocytes, providing a foundational tool for studying HDL-mediated reverse cholesterol transport and lipoprotein homeostasis.^[75]^[76] Cell-based assays employing small interfering RNA (siRNA) knockdown of SCARB1 have revealed its mechanistic contributions to pathogen entry and oncogenesis. In human hepatoma cells, SR-B1 knockdown significantly impairs HCV entry by disrupting HDL-HCV interactions at the cell surface, confirming SR-B1's role as a co-receptor in viral attachment and internalization.^[77] Similarly, in clear cell renal cell carcinoma (ccRCC) and lung cancer cell lines, siRNA-mediated SR-B1 depletion reduces cell viability, colony formation, migration, and invasion, indicating that SR-B1 supports tumor growth through enhanced cholesterol uptake and lipid-dependent signaling.^[78]^[79] SR-B1 integrates into broader cholesterol homeostasis pathways, including those modulated by statins and efflux mechanisms. It facilitates bidirectional cholesterol flux, promoting free cholesterol efflux to HDL while enabling selective cholesteryl ester uptake, which intersects with statin-induced LDL-C lowering by influencing HDL particle remodeling and reverse transport efficiency.^[52]^[80] SCARB1 polymorphisms have been shown to alter statin responsiveness in preclinical lipid profiling, underscoring its regulatory node in hepatic cholesterol efflux pathways involving ABCA1 and ABCG1 transporters.^[81] Conceptual pathway diagrams illustrate SR-B1's positioning within lipid signaling networks, where it bridges HDL binding to downstream PI3K/Akt activation for cellular cholesterol delivery.^[2] Recent advances from 2023 to 2025 have expanded SR-B1's preclinical relevance to extracellular vesicle (EV)-mediated processes and microbial interactions. In nasopharyngeal carcinoma models, EVs enriched with SR-B1 promote metastasis by co-regulating M1/M2 macrophage polarization, enhancing tumor immune evasion and distant organ colonization.^[61] Bacterial uptake assays in mammary epithelial cells demonstrate that SR-B1 facilitates endocytosis of Escherichia coli, linking it to innate immune responses against Gram-negative pathogens via TLR4 signaling integration.^[57] These findings, derived from CRISPR-edited cell lines and EV isolation techniques, emphasize SR-B1's emerging role in dynamic intercellular communication and infection models.^[82]

Targeted Therapies and Inhibitors

ITX5061, a small-molecule antagonist of SCARB1 (also known as SR-B1), inhibits hepatitis C virus (HCV) entry into hepatocytes by blocking the receptor's interaction with viral particles, thereby preventing infection.^[83] Developed as an entry inhibitor, ITX5061 demonstrated potent antiviral activity in preclinical models with an IC50 of 0.1 nM against HCV pseudoparticles.^[84] In clinical trials, including phase I and II studies for treatment-naive HCV patients and liver transplant recipients, ITX5061 at 150 mg/day was well-tolerated over 28 days, showing modest HCV RNA reductions, particularly in genotype 1 infections, and limited viral evolution in transplant settings.^[85] However, despite safety in preventing post-transplant reinfection, the compound did not advance beyond phase II due to limited efficacy when used alone.^[84] In cancer therapy, SCARB1 overexpression in tumor cells, such as in lung, breast, and nasopharyngeal carcinomas, has been exploited for targeted delivery of small interfering RNA (siRNA) therapeutics. Cholesterol-conjugated siRNAs bind to high-density lipoprotein (HDL), which interacts with SCARB1 to facilitate selective uptake into cancer cells, enabling RNA interference against oncogenic targets like KIF11 in large-cell and small-cell lung cancers.^[86] This approach enhances specificity and reduces off-target effects compared to non-targeted siRNA nanoparticles.^[87] Similarly, antibody-drug conjugates and nanoparticle-based mimics of HDL have been developed to exploit SCARB1 expression on tumor surfaces for delivering cytotoxic payloads, showing promise in preclinical models of triple-negative breast cancer and acute myeloid leukemia by promoting selective internalization and apoptosis.^[88]^[89] For cardiovascular applications, small molecules that enhance SCARB1 expression or stability have been investigated to promote reverse cholesterol transport and mitigate atherosclerosis progression. Novel compounds identified through high-throughput screening stabilize SCARB1 mRNA, increasing receptor levels in hepatic cells and reducing plaque formation in mouse models.^[90] However, challenges arise from SCARB1's multiple isoforms (e.g., full-length vs. splice variants), which exhibit tissue-specific functions, complicating selective modulation without disrupting lipid homeostasis or exacerbating off-target effects like altered HDL metabolism.^[91] Emerging preclinical studies as of 2025 highlight SCARB1 inhibitors targeting nasopharyngeal carcinoma (NPC) metastasis, where receptor-mediated extracellular vesicles drive macrophage polarization and tumor spread. SCARB1 knockdown in NPC-derived EVs has been shown to reduce vesicle uptake by macrophages and suppress M2 polarization, inhibiting metastatic niches in vitro and in xenografts.^[61] Additionally, as of 2025, SCARB1 has been linked to cholesterol metabolism-mediated ferroptosis inhibition, contributing to radioresistance in tumor cells and suggesting modulation as a strategy to enhance cancer therapies.^[92] These strategies build on preclinical validations showing SCARB1 modulation alters tumor ferroptosis resistance via cholesterol pathways.^[92]

References

[1]
SCAVENGER RECEPTOR CLASS B, MEMBER 1; SCARB1 - OMIM
SCARB1 mediates uptake of cholesterol and a variety of lipids, including phospholipids, products of triglycerol hydrolysis, lipophilic vitamins A and D, and ...
[2]
Scavenger receptor B type 1: expression, molecular regulation, and ...
The role of the high-density lipoprotein receptor SR-BI in the lipid metabolism of endocrine and other tissues. Endocr. Rev. 24: 357–387. [DOI] [PubMed] ...
[3]
Genetic Variant of the Scavenger Receptor BI in Humans
the gene encoding SR-BI — is expressed in the liver and steroidogenic tissues, where it mediates the selective uptake of HDL ...
[4]
The SCARB1 gene is associated with lipid response to dietary ... - NIH
It is likely that SCARB1 mediates uptake of lipids from both LDL and HDL, and this uptake is associated with an increase in cholesterol esterification (Stangl ...
[5]
SR-BI: Linking Cholesterol and Lipoprotein Metabolism with Breast ...
The SCARB1 gene encodes the scavenger receptor class B type I (SR-BI), which is an 82-kDa glycoprotein with two transmembrane domains separated by a large ...
[6]
SCARB1 scavenger receptor class B member 1 [ (human)] - NCBI
Sep 9, 2025 · The cell surface receptor SR-BI (scavenger receptor class B member 1), is essential for hepatitis C virus (HCV) entry into hepatocytes.
[7]
Scarb1 scavenger receptor class B, member 1 [ (house mouse)] - NCBI
Sep 24, 2025 · Results confirm that Hdlq1 and Hdlq8 are independent QTL on mouse chromosome 5 and demonstrate that Scarb1 and Acads are the underlying genes.
[8]
Transcript: ENST00000261693.11 (SCARB1-201) - Summary
This transcript has 13 exons, is annotated with 24 domains and features, is associated with 38634 variant alleles and maps to 616 oligo probes. Gene. This ...
[9]
Structure and localization of the human gene encoding SR-BI/CLA-1 ...
SR-BI resides on chromosome 12q24.2-qter, spans approximately 75 kilobase pairs, and contains 13 exons. RNA blot analysis of human tissues reveals an expression ...
[10]
rs5888 RefSNP Report - dbSNP - NCBI
### Summary of rs5888 Variant in SCARB1
[11]
Transcription factor sterol regulatory element binding protein 2 ...
Methods and results: Transient transfections demonstrated that SREBP factors induce Cla-1 promoter activity and that SREBP-2 is a more potent inducer than the ...
[12]
https://www.jlr.org/article/S0022-2275(24)00170-6/fulltext
[13]
Thematic Review Series: Lipid Transfer Proteins Scavenger receptor ...
Thus, SR-B1 can exert atheroprotective actions by impacting HDL metabolism and reverse cholesterol transport, mediating removal of cholesterol from macrophages ...
[14]
Identification of Scavenger Receptor SR-BI as a High Density ...
SR-BI binds HDL with high affinity, is expressed primarily in liver and nonplacental steroidogenic tissues, and mediates selective cholesterol uptake.
[15]
SR-B1: A Unique Multifunctional Receptor for Cholesterol Influx and ...
As a regulator of plasma membrane cholesterol content, SR-B1 promotes the uptake of lipid soluble vitamins as well as viral entry into host cells. These ...
[16]
SR-B1, a Key Receptor Involved in the Progression of ... - PMC - NIH
SR-B1 not only plays a role in the metabolism of HDL but also is involved in the clearance of LDL, VLDL, and Lp(a), proposing an important participation in the ...
[17]
https://doi.org/10.1210/endo.140.12.7220
[18]
Scavenger receptor class B type I (SR-BI) is involved in vitamin E ...
Anti-human SR-BI antibodies and BLT1 (a chemical inhibitor of lipid transport via SR-BI) blocked up to 80% of vitamin E uptake and up to 30 % of apical vitamin ...
[19]
Scavenger receptor class B type I (SR-BI) is involved in vitamin E ...
Anti-human SR-BI antibodies and BLT1 (a chemical inhibitor of lipid transport via SR-BI) blocked up to 80% of vitamin E uptake and up to 30% of apical vitamin E ...
[20]
Deficient Vitamin E Uptake During Development Impairs Neural ...
Jul 12, 2017 · Our results suggest the involvement of SR-BI in the maternal provision of embryonic vitamin E to the mouse embryo during neural tube closure.
[21]
Mechanism for the selective uptake of macular carotenoids ...
Mar 1, 2023 · Overexpression of SR-BI in HEK293 cells results in more lutein and zeaxanthin taken up than β-carotene, and this effect can be eliminated by an ...
[22]
High-density lipoprotein receptor SCARB1 is required for carotenoid ...
May 2, 2017 · Our results indicate that SCARB1 is an essential mediator of the expression of carotenoid-based coloration in birds, and suggest a potential ...
[23]
Provitamin A metabolism and functions in mammalian biology1 - NIH
Studies in cell culture and in knockout mouse models showed that the NinaD-related scavenger receptor class B type 1 (SR-B1) mediates carotenoid absorption into ...
[24]
Pathways and Mechanisms of Cellular Cholesterol Efflux—Insight ...
Similarly, SR-BI mediates selective uptake of CEs into steroid hormone-producing cells. ... Alternatively, the hydrophobic channel formed by SR-BI is needed for ...
[25]
Scavenger receptor class B type I: a multifunctional receptor - 2011
Oct 5, 2011 · Taking into consideration that SR-B1 is involved in vitamin E cellular uptake, the existence of α-tocopherol-mediated negative feedback ...
[26]
α-Tocopherol Metabolism Is Abnormal in Scavenger Receptor Class ...
SR-BI KO mice represent a new model for selective tissue vitamin E deficiency and, thus, may be useful for addressing the potential relevance of α-T, other ...Missing: carotenoid | Show results with:carotenoid
[27]
Increased Oxidative Stress in Scavenger Receptor BI Knockout Mice ...
In the current study we show that disruption of SR-BI, a prominent regulator of HDL metabolism, decreases the activity of the HDL-associated antioxidant enzyme ...
[28]
[PDF] High-density lipoprotein receptor SCARB1 is required for carotenoid ...
The expression of carotenoid coloration in birds involves four distinct physiological steps: uptake in the gut, transport in cir- culatory and lymphatic systems ...
[29]
SCARB1 protein expression summary - The Human Protein Atlas
The protein encoded by this gene is a plasma membrane receptor for high density lipoprotein cholesterol (HDL). The encoded protein mediates cholesterol transfer ...Missing: length | Show results with:length
[30]
Differentiation-dependent expression and localization of the class B ...
The current study used the human Caco-2 cell line and mouse intestine to explore the topology of expression of the class B type I scavenger receptor (SR-BI) ...Missing: SCARB1 | Show results with:SCARB1
[31]
Activation of the rat scavenger receptor class B type I gene by ...
PPARalpha/RXR increased the activity of the SR-BI promoter, an effect that was enhanced by clofibrate. Sequence analysis of the rat SR-BI promoter revealed the ...Missing: agonists | Show results with:agonists
[32]
Effect of estrogen on scavenger receptor BI expression in the rat
In this paper we explored the mechanisms responsible for the differential regulation of SR-BI by estrogen in these two tIssues. Previously it was shown that ...
[33]
Scarb1 Gene Polymorphism in Type 2 Diabetes Mellitus-A Review
Oct 12, 2017 · T2DM patients down-regulates SR-BI mRNA expression. Interestingly,decreased SR-BIexpression resulted in markedly increased plasma LDL ...
[34]
Hepatic and Extrahepatic Scavenger Receptors
SR-BII has a tissue distribution similar to that of SR-BI and also mediates selective lipid uptake from HDL, but SR-BII is ≈4 times less efficient in the ...
[35]
Scavenger Receptor class B type I (SR-BI) - PubMed Central - NIH
Mammalian SR-BI is a 509-amino acid, ∼82 kDa glycoprotein, that contains N- and C-terminal cytoplasmic domains, two-transmembrane domains, as well as a large ...
[36]
Comparative transcriptome and miRNA analysis of skin ...
Dec 5, 2022 · ... Scarb1 expression levels ... Therefore, we speculate that Scarb1 may be related to the development of xanthophores in soft-shelled turtle.
[37]
Zebrafish as outgroup model to study evolution of scavenger ...
Modulation of the extracellular regions by generating SCARB1/CD36 chimeric receptors affects various cholesterol transport functions [34]. Alignment of SCARB1 ...Missing: duplication | Show results with:duplication
[38]
Role Analysis of the scarb1 Gene in the Pigmentation of ... - MDPI
This study investigates the role of scavenger receptor class B type I (scarb1) in the body color of Neocaridina denticulata sinensis (cherry shrimp).
[39]
Comparative Studies of Vertebrate Platelet Glycoprotein 4 (CD36)
These suggested that CD36 originated in an ancestral genome and was subsequently duplicated to form three vertebrate CD36 gene family members, SCARB1, SCARB2 ...
[40]
A synonymous variant in scavenger receptor, class b, type i gene is ...
A synonymous variant within scavenger receptor class B type I gene (SCARB1), exon 8 rs5888, has been associated with altered lipid levels and cardiovascular ...
[41]
Scavenger Receptor Class B Type 1 Gene rs5888 Single Nucleotide ...
Results: The genotypic frequencies of SCARB1 rs5888 SNP were different between CAD patients and controls, the subjects with TT genotype had high risk of CAD ( ...
[42]
SCARB1 Gene Variants Are Associated With the Phenotype of ...
Oct 18, 2016 · Human SCARB1 gene variants are associated with a new lipid phenotype, characterized by high levels of both HDL cholesterol and Lp(a).
[43]
SCARB1 Gene Variants Are Associated With the Phenotype of ...
Human SCARB1 gene variants are associated with a new lipid phenotype, characterized by high levels of both HDL cholesterol and Lp(a).
[44]
Expression Levels and Genetic Polymorphism of Scavenger ... - NIH
6,7 Lack of SRB1 protein can result in an imbalance of cholesterol and dyslipidaemia and eventually lead to insulin resistance.8,9 McCarthy et al. reported that ...
[45]
Polymorphisms of the Scavenger Receptor Class B Member 1 Are ...
The gene encoding SR-BI (SCARB1; alias CD36L1, SRB1, CLA-1, and CLA1) is located on chromosome 12q24.1. The coordinates (123,785,056–123,878,214) are based on ...
[46]
Variants in Scavenger Receptor Class B Type I Gene Are ...
Variants within the scavenger receptor class B type I (SCARB1) receptor gene have been previously associated with lipid levels, especially in women, ...
[47]
High Free Cholesterol Bioavailability Drives the Tissue Pathologies ...
Higher HDL-FC bioavailability among Scarb1 −/− vs. WT mice drives increased FC content of multiple cell sites and is a potential biomarker that is ...
[48]
High Free Cholesterol Bioavailability Drives Tissue Pathologies
Aug 12, 2021 · Whereas feeding a high-fat, high-cholesterol diet to Scarb1−/− mice induces ASCVD, changes in plasma concentrations of atherogenic APOB ...
[49]
Hepatic Scavenger Receptor Class B Type 1 Knockdown Reduces ...
Feb 11, 2021 · In line with our findings, a genetic variant (P297S) of SCARB1, the ... rs5888 polymorphism associates with lower plasma triglyceride ...
[50]
Inherited Variants in SCARB1 Cause Severe Early-Onset Coronary ...
May 12, 2021 · We have identified rare, compound heterozygous variants in SCARB1 that segregate with severe, premature CAD, following patterns of Mendelian inheritance.
[51]
Genetic Architecture and Clinical Outcomes of Combined Lipid ...
Jun 3, 2024 · Simultaneous assessment of multiple lipid derangements revealed nuanced differences in coronary artery disease risk and genetic architectures across ...
[52]
HDL Function and Atherosclerosis: Reactive Dicarbonyls as ...
May 25, 2023 · In addition, human carriers of a number of the Scarb1 gene variants have markedly elevated levels of lipoprotein (a), an atherogenic LDL ...Hdl Rct · Cholesterol Efflux · Hdl Antioxidant Function
[53]
Cell entry of hepatitis C virus requires a set of co-receptors that ...
Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor.
[54]
Scavenger receptor class B type I is a key host factor for hepatitis C ...
Scavenger receptor class B type I (SR-BI) has been shown to bind HCV envelope glycoprotein E2, participate in entry of HCV pseudotype particles, and modulate ...
[55]
Scavenger receptor B1 facilitates the endocytosis of Escherichia coli ...
Jan 5, 2023 · SCARB1 belongs to class B of Scavenger receptors (SRs) that are known to be involved in binding and endocytosis of various pathogens.
[56]
Targeting of scavenger receptor class B type I by synthetic ... - PubMed
Human scavenger receptor class B type I, CLA-1, mediates lipopolysaccharide (LPS) binding and internalization (Vishnyakova, T. G., Bocharov, A. V., Baranova ...
[57]
Dengue Virus NS1 Uses Scavenger Receptor B1 as a ... - PubMed
Mar 9, 2022 · We report that the HDL scavenger receptor B1 (SRB1) in human hepatic cells and a scavenger receptor B1-like in mosquito C6/36 cells act as cell surface binding ...<|control11|><|separator|>
[58]
Upregulation of Scavenger Receptor B1 Is Required for ...
Upregulation of scavenger receptor B1 is required for steroidogenic and nonsteroidogenic cholesterol metabolism in prostate cancer.
[59]
SCARB1 in extracellular vesicles promotes NPC metastasis by co ...
Aug 29, 2023 · Our findings showed that SCARB1-EVs promoted metastasis by co-regulating M1 and M2 macrophage function.<|separator|>
[60]
Targeting the SR-B1 Receptor as a Gateway for Cancer Therapy ...
SR-B1 has been found to be highly expressed in several different types of tumors including breast, ovarian, colorectal, pancreatic cancer (Shahzad et al., 2011) ...
[61]
High scavenger receptor class B type I expression is... - LWW
Moreover, high SR-B1 expression is associated with tumor aggressiveness and poor clinical prognosis in breast cancer and prostate cancer. Additionally, the SR- ...<|separator|>
[62]
Prognostic and clinicopathological significance of SR-B1 in solid ...
Studies have found that SR-B1 is overexpression and cholesterol especially HDL cholesterol level is lower in a variety of malignant tumors such as breast, lung, ...
[63]
Microglial Scavenger Receptors and Their Roles in the ...
SCARA-1 knock-out microglia isolated from these animals showed a 60% decrease in the ability to take up amyloid-β compared with wild-type cells [36]. These ...<|separator|>
[64]
Mechanisms of Aβ Clearance and Degradation by Glial Cells
Scavenger receptor type-A (SR-A), type B1 (SR-B1), CD36 and CD40 are able to ... Evidence for impaired amyloid beta clearance in Alzheimer's disease.
[65]
Relationship between plasma lipid and cognitive function in the ...
Relationship between plasma lipid and cognitive function in the elderly based on individual's diet and ApoE, CD36, SCARB1 genetic polymorphisms. Author links ...
[66]
A Role for the High-Density Lipoprotein Receptor SR-B1 in Synovial ...
SR-B1 is expressed in RA synovial tissue and mediates A-SAA–induced pro-inflammatory pathways, a better understanding of A-SAA–mediated inflammatory pathways ...
[67]
rs5888 Variant of SCARB1 Gene Is a Possible Susceptibility Factor ...
Based on a candidate gene approach, we analyzed SNP rs5888 of the SCARB1 gene, coding for SRBI, which is involved in the lipid and lutein pathways.
[68]
The Role of Scavenger Receptor BI in Sepsis - MDPI
Hepatic SR-BI is crucial for LPS clearance during sepsis, as observed in mice with hepatic SR-BI deficiency (Scarb1I179N mice), experiencing a three-fold ...
[69]
SCARB1 Gene Variants are Associated with the Phenotype of ...
Jun 26, 2025 · Human SCARB1 gene variants are associated with a new lipid phenotype, characterized by high levels of both HDL-C and Lp(a).
[70]
Comprehensive Strategy for Identifying Extracellular Vesicle Surface ...
In diet-induced obesity in mice, SCARB1 deficiency increased inflammatory dyslipidaemia and adipocytes hypertrophy and attenuated hepatic steatosis [74].
[71]
(PDF) Rare variant in scavenger receptor BI raises HDL cholesterol ...
SR-BI-deficient (SR-BI −/− ) mice were characterized by enlarged HDL particles, increased plasma HDL-cholesterol (HDL-C) and free cholesterol (FC) levels, and a ...
[72]
High density lipoprotein cholesterol and proteome in SR-B1 KO mice
Nov 12, 2018 · SR-B1 deficient (SR-B1 KO) mice are prone to atherosclerosis and exhibit abnormally large, cholesterol-rich, dysfunctional HDL.
[73]
Serum opacity factor rescues fertility among female Scarb1 - NIH
Mice deficient in the HDL receptor, encoded by Scarb1, are a model of female infertility linked to dysfunctional HDL. Plasma HDL-FC concentrations among Scarb1− ...
[74]
Lipoprotein Receptors Redundantly Participate in Entry of Hepatitis ...
Scavenger receptor class B type 1 (SR-B1) and low-density lipoprotein receptor (LDLR) are known to be involved in entry of hepatitis C virus (HCV), ...
[75]
Role of Scavenger Receptor Class B Type I in Hepatitis C Virus Entry
Scavenger receptor class B type I (SR-BI) is an essential receptor for hepatitis C virus (HCV) and a cell surface high-density-lipoprotein (HDL) receptor.Missing: knockout | Show results with:knockout
[76]
Identification of Conserved Residues in Hepatitis C Virus Envelope ...
A nontargeting siRNA was transfected in parallel and served as a control. Knockdown efficiency was determined by Western blotting with the help of anti-SRB1, ...Peptide Synthesis And... · Cd81 Inhibition Assay And... · ResultsMissing: tumor | Show results with:tumor<|separator|>
[77]
Up-regulation of SR-BI promotes progression and serves as a ...
Jan 22, 2018 · The inhibition of SR-BI attenuated the tumorous behaviors of ccRCC cells, expression of metastasis and AKT pathway related proteins. The content ...Rna Extraction And Real-Time... · Protein Extraction And... · Transwell Cell Migration And...
[78]
Scavenger receptor class B member 1 promotes lung cancer growth ...
Mar 3, 2025 · Hence, SCARB1 knockdown significantly inhibited A549 cell invasion and migration [Figures 2h-j]. Our experiments show that in A549 lung cancer ...
[79]
Influence of SCARB1 polymorphisms on serum lipids of ...
Although statins are considered efficacious and safe, the LDL cholesterol-lowering response to statin is variable, with many patients failing to achieve ...
[80]
SR-B1, a Key Receptor Involved in the Progression of ... - MDPI
SR-B1 not only plays a role in the metabolism of HDL but also is involved in the clearance of LDL, VLDL, and Lp(a), proposing an important participation in the ...
[81]
High-density lipoprotein attenuates lipopolysaccharide-induced IL ...
Our findings uncover a cellular mechanism by which HDL attenuates LPS-induced pro-inflammatory response via SR-B1-mediated LPS degradation.
[82]
Evaluation of ITX 5061, a Scavenger Receptor B1 Antagonist
Feb 15, 2012 · ITX 5061 is a scavenger receptor B1 antagonist that has entered phase 1 clinical trials in hepatitis C virus (HCV)-infected humans.Missing: II | Show results with:II
[83]
The HDL-transporting scavenger receptor B1 promotes viral ...
Jun 20, 2025 · Inhibiting SR-B1 results in lack of acidification in the endolysosomal compartment and entrapment of SARS-CoV-2 in endosomal-lysosomal vesicles.Missing: sepsis | Show results with:sepsis
[84]
Effect of scavenger receptor class B type I antagonist ITX5061 in ...
ITX5061 is a scavenger receptor class B type I antagonist that blocks HCV entry and infection in vitro. We assessed the safety and efficacy of ITX5061 to limit ...Missing: SCARB1 | Show results with:SCARB1
[85]
Personalized siRNA-Nanoparticle Systemic Therapy using ...
Inhibition of gene expression for these targets effectively suppressed lung cancer cell growth. SCARB1 was highly expressed in a subset of tumors from the lung ...Rnai And Cell Viability... · In Vivo Rnai Study Using... · Expression Of Scarb1 In Lung...
[86]
Targeting SR-BI for Cancer Diagnostics, Imaging and Therapy
Sep 26, 2016 · As summarized in Table 1, several patient tumors and cancer cell lines display upregulated expression of SR-BI relative to healthy tissue, ...
[87]
SR-B1-targeted nanodelivery of anti-cancer agents
Jun 2, 2017 · SR-B1-targeted nanodelivery of anti-cancer agents: a promising new approach to treat triple-negative breast cancer Rebecca Johnson,1 ...
[88]
Targeting scavenger receptor class B type 1 with a bioinspired ...
These studies open a new paradigm and strategy for developing targeted synthetic biologics, such as the HDL NP for SR-B1, and cancer therapy in AML.
[89]
Identification of Novel Compounds Enhancing SR-BI mRNA Stability ...
The positive small molecular compounds obtained in this study might become new drug candidates or lead compounds for the treatment of cardiovascular diseases ...
[90]
Differential roles of Scavenger receptor class B type I
The human SCARB1 gene encoding the SR-BI protein is located at 12q24 on chromosome 12, is ~87 kb in length and comprises 13 exons and 12 introns (3). SR-B1 has ...
[91]
Inhibition of Scarb1 on Endothelial Cells Attenuates Pressure ...
Thus, targeting the FB-EC interaction via SCARB1 could be promising for hypertensive heart failure treatment. Whereas several studies have examined EC-CM or FB- ...
[92]
SCARB1 links cholesterol metabolism-mediated ferroptosis ...
Jan 18, 2025 · SCARB1 acts as a suppressor of ferroptosis in tumor cells. SCARB1 enhances ferroptosis resistance through the upregulation of cholesterol metabolism and CoQ10.