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Identification and characterization of murine SCARA5, a novel class A scavenger receptor that is expressed by populations of epithelial cells

Identification and characterization of murine SCARA5, a novel class A scavenger receptor that is expressed by populations of epithelial cells
Identification and characterization of murine SCARA5, a novel class A scavenger receptor that is expressed by populations of epithelial cells
Epithelia are positioned at a critical interface to prevent invasion by microorganisms from the environment. Pattern recognition receptors are important components of innate immunity because of their ability to interact with specific microbe-associated structures and initiate immune responses. Several distinct groups of receptors have been recognized. One of these, the scavenger receptors, has been classified into at least eight separate classes. The class A scavenger receptors are characterized by the presence of a collagen-like domain and include macrophage scavenger receptor type A (SR-A1 I/II, SCARA1) and MARCO (SCARA2). These receptors are known to make important contributions to host defense. Here, we identify a novel murine scavenger receptor, SCARA5, which has a structure typical of this class. The cDNA encodes 491 amino acids, which predict a type II protein that contains C-terminal intracellular, transmembrane, extracellular spacer, collagenous, and N-terminal scavenger receptor cysteine rich domains. Expression in Chinese hamster ovary cells confirmed that the receptor assembles as a homotrimer and is expressed at the plasma membrane. SCARA5-transfected cells bound Escherichia coli and Staphylococcus aureus, but not zymosan, in a polyanionic-inhibitable manner. Unlike other class A scavenger receptors, the receptor was unable to endocytose acetylated or oxidized low density lipoprotein. Quantitative RTPCR and in situ hybridization demonstrate SCARA5 has a tissue and cellular distribution unique among class A scavenger receptors. Because of the restriction of SCARA5 transcripts to populations of epithelial cells, we propose that this receptor may play important roles in the innate immune activities of these cells.
0021-9258
11834-11845
Jiang, Yanyan
40057d08-8337-4eb1-b917-4ba81bd9a46e
Oliver, Peter
777ec800-10db-4096-947e-8fdbdd85fb88
Davies, Kay E.
6f681b2f-0689-45e1-ba39-7138e4fac227
Platt, Nick
44ce8cb5-f0dc-4f54-bf2a-feecc48e8305
Jiang, Yanyan
40057d08-8337-4eb1-b917-4ba81bd9a46e
Oliver, Peter
777ec800-10db-4096-947e-8fdbdd85fb88
Davies, Kay E.
6f681b2f-0689-45e1-ba39-7138e4fac227
Platt, Nick
44ce8cb5-f0dc-4f54-bf2a-feecc48e8305

Jiang, Yanyan, Oliver, Peter, Davies, Kay E. and Platt, Nick (2006) Identification and characterization of murine SCARA5, a novel class A scavenger receptor that is expressed by populations of epithelial cells. The Journal of Biological Chemistry, 281 (17), 11834-11845. (doi:10.1074/jbc.M507599200).

Record type: Article

Abstract

Epithelia are positioned at a critical interface to prevent invasion by microorganisms from the environment. Pattern recognition receptors are important components of innate immunity because of their ability to interact with specific microbe-associated structures and initiate immune responses. Several distinct groups of receptors have been recognized. One of these, the scavenger receptors, has been classified into at least eight separate classes. The class A scavenger receptors are characterized by the presence of a collagen-like domain and include macrophage scavenger receptor type A (SR-A1 I/II, SCARA1) and MARCO (SCARA2). These receptors are known to make important contributions to host defense. Here, we identify a novel murine scavenger receptor, SCARA5, which has a structure typical of this class. The cDNA encodes 491 amino acids, which predict a type II protein that contains C-terminal intracellular, transmembrane, extracellular spacer, collagenous, and N-terminal scavenger receptor cysteine rich domains. Expression in Chinese hamster ovary cells confirmed that the receptor assembles as a homotrimer and is expressed at the plasma membrane. SCARA5-transfected cells bound Escherichia coli and Staphylococcus aureus, but not zymosan, in a polyanionic-inhibitable manner. Unlike other class A scavenger receptors, the receptor was unable to endocytose acetylated or oxidized low density lipoprotein. Quantitative RTPCR and in situ hybridization demonstrate SCARA5 has a tissue and cellular distribution unique among class A scavenger receptors. Because of the restriction of SCARA5 transcripts to populations of epithelial cells, we propose that this receptor may play important roles in the innate immune activities of these cells.

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Published date: 2006

Identifiers

Local EPrints ID: 41145
URI: http://eprints.soton.ac.uk/id/eprint/41145
ISSN: 0021-9258
PURE UUID: 1dac6043-3d04-4cb5-8ff8-3f9cc08e720d

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Date deposited: 21 Jul 2006
Last modified: 15 Mar 2024 08:25

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Contributors

Author: Yanyan Jiang
Author: Peter Oliver
Author: Kay E. Davies
Author: Nick Platt

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