Leukocyte-associated immunoglobulin-like receptor 2 ( LAIR2 ), also known as CD306, is a 131 amino acid protein containing one lg-like C2-type domain. It is expressed as a soluble receptor exhibiting high affinity for various collagen molecules to which it binds in a hydroxyproline-dependent manner. LAIR2 is a member of the immunoglobulin superfamily and was identified by its similarity to LAIR1, an inhibitory receptor present on mononuclear leukocytes. LAIR2 is thought to be secreted and may help modulate mucosal tolerance. As a natural competitor for LAIR1, soluble LAIR2 prevents binding of human LAIR1 to collagens and LAIR1 cross-linking, thereby regulating its inhibitory potential. Accordingly, LAIR2 is suggested to perform an immunoregulatory function.
Leukocyte-Associated Immunoglobulin-Like Receptor 2 (LAIR2) is a secreted, 131 amino acid protein that contains one Ig-like C2 type domain, making it a member of the Ig superfamily. When compared to LAIR-1, its transmembrane counterpart, it shares 83% amino acid identity across the signal sequence and extracellular domains, although one is secreted and one is membrane-bound, the two LAIR proteins are thought to have arisen from a common gene ancestor and appear to share similar adhesion profiles. This suggests that LAIR-2 may compete with LAIR-1 for ligand binding. A 114 amino acid alternate splice form of LAIR-2 is truncated at the C terminus, but retains the entire Ig domain. The expression profile of these splice forms, and the presence of orthologs in other species, have not been reported.
Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
Lysosome-Associated Membrane Glycoprotein 1 (LAMP1) is a single-pass type I membrane protein belonging to the LAMP family. LAMP1 is expressed largely in the endosome-lysosome membranes of cells.It shuttles between lysosomes; endosomes; and the plasma membrane. LAMP1 functions to present carbohydrate ligands to selectins and it has also been implicated in tumor cell metastasis. It has been proposed LAMP1 can be used as a therapeutic agent for certain cancers; as well as a marker for lysosomal storage disorders and degranulation on lymphocytes such as CD8+ and NK cells. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells(PBMC) to vascular endothelium; therefore they are possibly involved in the adhesion of PBMCs to the site of inflammation.
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