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This information is current as Cysteine-Rich Superfamily Member of the Scavenger Receptor of Mouse S 5 D-SRCRB : A New Group B Molecular and Functional Characterization
| Content Provider | Semantic Scholar |
|---|---|
| Author | Miró-Julià, Cristina Roselló, Sandra Fink, Dorte Rosenbek Escoda-Ferran, Cristina Padilla, Olga Vázquez-Echeverría, Citlali Espinal-Marin, Paula Serra-Pagés, Carles Holmskov, Uffe Yélamos, José Lozano, Francisco |
| Copyright Year | 2011 |
| Abstract | The scavenger receptor cysteine-rich superfamily (SRCR-SF) members are transmembrane and/or secreted receptors exhibiting one or several repeats of a cysteine-rich protein module of ∼100 aa, named scavenger receptor cysteine-rich (SRCR). Two types of SRCR domains (A or B) have been reported, which differ in the number of coding exons and intradomain cysteines. Although no unifying function has been reported for SRCR-SF members, recognition of pathogen-associated molecular patterns (PAMPs) was recently shown for some of them. In this article, we report the structural and functional characterization of mouse S5D-SRCRB, a new group B member of the SRCR-SF. The s5d-srcrb gene maps at mouse chromosome 7 and encompasses 14 exons extending over 15 kb. The longest cDNA sequence found is 4286 bp in length and encodes a mature protein of 1371 aa, with a predicted M r of 144.6 kDa. Using an episomal mammalian-expression system, a glycosylated soluble recombinant form >200 kDa was obtained and used as immunogen for the generation of specific rat mAbs. Subsequent immunohistochemical and real-time PCR analysis showed significant S5D-SRCRB expression in murine genitourinary and digestive tracts. S5D-SRCRB was shown to bind endog-enous extracellular matrix proteins (laminin and galectin-1), as well as PAMPs present on Gram-positive and Gram-negative bacteria and fungi. PAMP binding by S5D-SRCRB induced microbial aggregation and subsequent inhibition of PAMP-induced cytokine release. These abilities suggest that S5D-SRCRB might play a role in the innate defense and homeostasis of certain specialized epithelial surfaces. T he innate immune system represents the first line of host defense for multicellular organisms to maintain homeo-stasis of the internal environment against foreign pathogens (microorganisms, chemicals), as well as altered self-components (1). To do this, the humoral (i.e., complement) and the cellular (e.g., mucocutaneous barriers, macrophages) arms of the innate immune system are equipped with a set of inborn (germ-line encoded) receptors named pattern recognition receptors (PRRs). These PRRs recognize a relatively small spectrum of highly conserved structures of protein, saccharide, lipid, and nucleic acid nature of endogenous and exogenous origin. Typically, PRRs recognize pathogen-associated molecular patterns (PAMPs), which are conserved components essential for pathogen survival and are not shared by the host. Examples of PAMPs include LPS from Gram-negative bacteria, lipotheicoic acid (LTA) and peptidoglycan (PGN) from Gram-positive bacteria, dsRNA from virus, lipoarabinomannan from mycobacteria, and mannan and b-glucan from fungi. Recognition of PAMPs by PRRs usually initiates an inflammatory cascade that involves recruitment of leukocytes to the site of infection, … |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://core.ac.uk/download/pdf/50673182.pdf |
| Alternate Webpage(s) | http://www.jimmunol.org/content/jimmunol/early/2011/01/07/jimmunol.1000840.full.pdf?with-ds=yes |
| Alternate Webpage(s) | http://www.jimmunol.org/content/jimmunol/early/2011/01/07/jimmunol.1000840.full.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
