anti-Scavenger Receptor Class B, Member 2 (SCARB2) Anticorps

Zebrafish Scavenger Receptor Class B, Member 2 (SCARB2) interaction partners

1. This work describes a novel function for the Scarb2 receptor as an essential glycoprotein for notochord development.

Human Scavenger Receptor Class B, Member 2 (SCARB2) interaction partners

1. Here, we report the EV71-SCARB2 complex structure determined at 3.4 A resolution using cryo-electron microscopy. This reveals that SCARB2 binds EV71 on the southern rim of the canyon, rather than across the canyon, as predicted.

2. SCARB2 polymorphisms (rs6824953 and rs11097262) were associated with susceptibility to EV71 infection (OR 1.60, 95% CI 1.07-2.39; and OR 1.64, 95% CI 1.09-2.47, respectively).

3. Glycosylation, ubiquitination and palmitoylation are involved in regulating CD36 stability, while phosphorylation at extracellular sites affect the rate of fatty acid uptake. In addition, CD36 modification by O-linked N-acetylglucosamine may regulate the translocation of CD36 from endosomes to the cell surface.

4. Crystal structure of a LIMP-2 luminal domain dimer with bound cholesterol and phosphatidylcholine is described. Binding of these lipids alters LIMP-2 from functioning as a glucocerebrosidase-binding monomer toward a dimeric state that preferentially binds anionic phosphatidylserine over neutral phosphatidylcholine.

5. The binding of a monoclonal antibody to the apical region of SCARB2 blocks EV71 infection.

6. The findings identify SR-BII as a functional SAA receptor that mediates SAA uptake and contributes to its proinflammatory signaling via the MAPK-mediated signaling pathways.

7. In this paper we provide an updated overview of the clinical and genetic features of SCARB2-related PME and on the functions of the LIMP2 protein [review]

8. neutrophils are able to drive a macrophage activation that would regulate the increase in LIMP-2 expression during the early phase of Cer-induced acute pancreatitis

9. Findings suggested that STX1B rs4889603, FAM47E rs6812193 and SCARB2 rs6825004 do not confer a significant risk for Parkinson's disease

10. LIMPII was increased greater than twofold in urinary microvesicles obtained from patients with idiopathic membranous nephropathy compared to microvesicles of patients with idiopathic focal segmental glomerulosclerosis and normal controls.

11. hSR-BII, and to a lesser extent hSR-BI, significantly increase LPS-induced inflammation and contribute to LPS-induced tissue injury in the liver and kidney, two major organs susceptible to LPS toxicity.

12. Although hrGCase cellular uptake is independent of LIMP-2, its trafficking to the lysosomes is mediated by this receptor.

13. SNCA and SCARB2 loci are also associated with dementia with Lewy bodies, after a study-wise Bonferroni correction, although these have a different association profile than the associations reported for the same loci in Parkinson's.

14. a novel mutation in SCARB2 as a cause of progressive myoclonus epilepsy in China

15. SCARB2 regulates TLR9-dependent IFN-I production of plasmacytoid dendritic cells

16. Disease-causing cathepsin-F mutants fail to cleave LIMP-2. Our findings provide evidence that LIMP-2 represents an in vivo substrate of cathepsin-F with relevance for understanding the pathophysiology of type-B-Kufs-disease.

17. Data indicate that scavenger receptor SCARB2 triggers uncoating of human enterovirus 71 (EV71) under low pH conditions.

18. SCARB2 and PSGL-1 in human gastrointestinal tract, lung, and brain tissues correlated with the distribution of pathological changes seen in EV71 infection.

19. In LIMP-2-deficient brains a significant reduction in GC activity led to lipid storage, disturbed autophagic/lysosomal function, and alpha-synuclein accumulation.

20. The LIMP-2/SCARB2 binding sequences for enterovirus 71 and GCase are not similar, indicating that LIMP-2/SCARB2 may have multiple or overlapping binding sites with differing specificities.

Mouse (Murine) Scavenger Receptor Class B, Member 2 (SCARB2) interaction partners

1. LIMP-2 facilitates transport of phospholipids into murine fibroblasts, with a strong substrate preference for phosphatidylserine.

2. The findings identify SR-BII as a functional SAA receptor that mediates SAA uptake and contributes to its proinflammatory signaling via the MAPK-mediated signaling pathways.

3. AP-3-dependent LB targeting is facilitated by protein/protein interaction between LIMP-2/SCARB2 and PRDX6 in vitro and in vivo

4. Heterologous expression of the luminal domain of LIMP-2 in wild-type cells.

5. In LIMP-2-deficient brains a significant reduction in GC activity led to lipid storage, disturbed autophagic/lysosomal function, and alpha-synuclein accumulation.

6. absence of Limp-2 reduces inflammation in experimental crescentic glomerulonephritis with decreased macrophage and T-cell infiltration in the kidney.

7. Limp-2 deficiency leads to a minor increase in circulating renin. Limp-2, however, is not required for acute or chronic stimulation of renin release.

8. The SR-BII is involved in cholesterol ester uptake for steroidogenesis and spermatogenesis in the testis.

9. The residues between 144 and 151 are critical for SCARB2 binding to VP1 of EV71 and seven residues from the human receptor could convert murine SCARB2, an otherwise inefficient receptor, to an efficient receptor for EV71 viral infection.

10. The data suggest that tubular proteinuria in Limp-2(-/-) mice is due to failure of endosomes containing reabsorbed proteins to fuse with lysosomes in the proximal tubule of the kidney. Failure of proteolysis is a novel mechanism for tubular proteinuria.

11. The coiled-coil structure of LIMP-2 is required for its interaction with beta-glucocerebrosidase.

12. CD36 is not essential for MHC class I cross-presentation of cell-associated antigen by CD8 alpha+ dendritic cells.

13. CD36 is differentially expressed by CD8+ splenic dendritic cells but is not required for cross-presentation in vivo.

14. Overexpression of LGP85 causes an enlargement of early endosomes and late endosomes/lysosomes. LGP85 may participate in reorganizing the endosomal/lysosomal compartments.

15. SR-A and CD36 are responsible for the preponderance of modified LDL uptake in macrophages and that other scavenger receptors do not compensate for their absence

16. LIMP-2/LGP85 deficiency causes ureteric pelvic junction obstruction, deafness and peripheral neuropathy in mice

17. Our findings suggest an important role for LIMP2 in the control of the localization and the level of apically expressed membrane proteins such as KCNQ1, KCNE1 and megalin in the stria vascularis.

18. Peritoneal macrophages isolated from SR-BI/BII-knockout mice demonstrated a 30% decrease in bacterial uptake when compared with macrophages from normal mice.

19. Lysosomal integral membrane protein 2 is a novel component of the cardiac intercalated disc and vital for load-induced cardiac myocyte hypertrophy.

20. These data support a role for LIMP-2 as the mannose-6-phosphate-independent trafficking receptor for beta-glucocerebrosidase.