Abstract
A Role for Human SPα as a Pattern Recognition Receptor
Highlights
A vast number of structurally diverse cell surface or soluble glycoproteins have been defined as scavenger receptors (SR) [3]
The present report shows that Sp␣, a soluble molecule secreted by macrophages, is involved in the recognition of pathogen-associated molecular patterns, namely LPS and lipoteichoic acid (LTA)
The scavenger receptor cysteine-rich (SRCR) domain was first reported on the mouse type I class A macrophage scavenger receptor
Summary
A vast number of structurally diverse cell surface or soluble glycoproteins have been defined as scavenger receptors (SR) [3] Their common feature is that they are involved in the recognition and endocytosis of polyanionic molecules, such as oxidized or acetylated low density lipoproteins. The SRCR domains of group B proteins mostly contain 8 cysteine residues and are encoded by a single exon. Human Sp␣ (hSp␣) is an SRCR-SF group B protein for which limited functional information is available. It is a soluble 38-kDa glycoprotein composed of three SRCR domains, and it is expressed by macrophages present in lymphoid tissues (spleen, lymph node, thymus, bone marrow, and fetal liver). Sp␣ may play a role in the homeostasis of IgM, because it has been found present in IgM but not IgG or IgA fractions from human serum [20]
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