Type I macrophage scavenger receptor contains α-helical and collagen-like coiled coils

Nature ◽  
1990 ◽  
Vol 343 (6258) ◽  
pp. 531-535 ◽  
Author(s):  
Tatsuhiko Kodama ◽  
Mason Freeman ◽  
Lucia Rohrer ◽  
James Zabrecky ◽  
Paul Matsudaira ◽  
...  
2013 ◽  
Vol 9 (1) ◽  
pp. 47-50
Author(s):  
Dhruba Acharya

CD36 was described nearly 30 years ago as “glycoprotein IV” the fourth major band of 88KD observed on SDS-PAGE of platelet membrane (1). It is present on many mammalian cell types: microvascular endothelium; professional phagocytes including macrophages, dendritic cells, microglia and retinal pigment-epithellium; erythroid precursors; hepatocytes; adipocytes; cardiac and skeletal myocytes; and specialized epithelia of the breast, kidney and gut (2). As a pattern recognition receptor, CD36 binds a diverse set of ligands, including oxidized low-density lipoprotein (oxLDL)(5), anionic phospholipids (4), long-chain fatty acids, thrombospondin-1, fibrillar -amyloid, and the membrane of cells undergoing apoptosis (3, 5, 6). CD36 has been implicated in a wide variety of normal and pathologic biological functions, including angiogenesis, atherosclerosis, phagocytosis, inflammation, lipid metabolism, and removal of apoptotic cells (3, 5). In 1993, Endemann et al. first identified CD36 as a potential oxLDL receptor (7).Unlike macrophage scavenger receptor A type I and II, CD36 binds LDL that has been exposed to minimally oxidizing condition. The observation that CD36 was an oxLDL receptor was the catalyst for many to prove the role of CD36 in atherosclerosis. DOI: http://dx.doi.org/10.3126/njh.v9i1.8349 Nepalese Heart Journal Vol.9(1) 2012 pp.47-50


Author(s):  
Long Yang ◽  
Tingting Geng ◽  
Guang Yang ◽  
Jinzhu Ma ◽  
Leilei Wang ◽  
...  

AbstractMacrophage scavenger receptor 1 (MSR1) mediates the endocytosis of modified low-density lipoproteins and plays an important antiviral role. However, the molecular mechanism underlying MSR1 antiviral actions remains elusive. Herein, we report that MSR1 activates autophagy to restrict infection of Chikungunya virus (CHIKV), an arthritogenic alphavirus that causes acute and chronic crippling arthralgia. Msr1 expression was rapidly upregulated after CHIKV infection in mice. Msr1 knockout mice had elevated viral loads and increased susceptibility to CHIKV arthritis along with a normal type I IFN response. Induction of LC3 lipidation by CHIKV, a marker of autophagy, was reduced in Msr1-/- cells. Mechanistically, MSR1 interacted with ATG12 through its cytoplasmic tail and this interaction was enhanced by CHIKV nsP1 protein. MSR1 repressed CHIKV replication through ATG5-ATG12-ATG16L1 and this was dependent on the FIP200-and-WIPI2-binding domain, but not the WD40 domain of ATG16L1. Our results elucidate an antiviral role for MSR1 involving the autophagic function of ATG5-ATG12-ATG16L1.


2010 ◽  
Vol 1 (2) ◽  
pp. 174-187 ◽  
Author(s):  
Jason W. K. Goh ◽  
Yen Seah Tan ◽  
Alister W. Dodds ◽  
Kenneth B. M. Reid ◽  
Jinhua Lu

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Long Yang ◽  
Tingting Geng ◽  
Guang Yang ◽  
Jinzhu Ma ◽  
Leilei Wang ◽  
...  

Abstract Macrophage scavenger receptor 1 (MSR1) mediates the endocytosis of modified low-density lipoproteins and plays an important antiviral role. However, the molecular mechanism underlying MSR1 antiviral actions remains elusive. We report that MSR1 activates autophagy to restrict infection of Chikungunya virus (CHIKV), an arthritogenic alphavirus that causes acute and chronic crippling arthralgia. Msr1 expression was rapidly upregulated after CHIKV infection in mice. Msr1 knockout mice had elevated viral loads and increased susceptibility to CHIKV arthritis along with a normal type I IFN response. Induction of LC3 lipidation by CHIKV, a marker of autophagy, was reduced in Msr1−/− cells. Mechanistically, MSR1 interacted with ATG12 through its cytoplasmic tail and this interaction was enhanced by CHIKV nsP1 protein. MSR1 repressed CHIKV replication through ATG5-ATG12-ATG16L1 and this was dependent on the FIP200-and-WIPI2-binding domain, but not the WD40 domain of ATG16L1. Our results elucidate an antiviral role for MSR1 involving the autophagic function of ATG5-ATG12-ATG16L1.


Circulation ◽  
2004 ◽  
Vol 110 (22) ◽  
pp. 3472-3479 ◽  
Author(s):  
Jihong Han ◽  
Michael Parsons ◽  
Xiaoye Zhou ◽  
Andrew C. Nicholson ◽  
Antonio M. Gotto ◽  
...  

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