Linker for Activation of T-Cells Family Member 2 (LAT2) is a single-pass type III membrane protein. LAT2 is highly expressed in the spleen, peripheral blood lymphocytes, and germinal centers of lymph nodes. LAT2 is involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. It may also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Coupleing activate of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2.
Latexin; also known as endogenous carboxypeptidase inhibitor; tissue carboxypeptidase inhibitor; TCI; ECI and LXN; is a cytoplasm protein which belongs to theprotease inhibitor I47 (latexin) family. It is highly expressed in heart; prostate; ovary; kidney; pancreas; and colon. Latexin / LXN is the only known endogenous specific inhibitor of zinc-dependent metallocarboxypeptidases (MCPs) present in mammalians so far. Latexin is originally identified as a molecular marker for the regional specification of the neocortex in development in rats. The 222 amino acid latexin in human shows different expression distribution with high levels in heart; prostate; ovary; kidney; pancreas; and colon; but only moderate or low levels in other tissues including brain. Latexin is also expressed at high levels and is inducible in macrophages in concert with other protease inhibitors and potential protease targets; and thus is suggested to play a role in inflammation and innate immunity pathways. Despite of the non-detectable sequence similarity with plant and parasite inhibitors; Latexin is related to a human putative tumor suppressor protein; TIG1. In addition; Latexin is also implicated in Alzheimer's disease.
Layilin, a recently characterized as a 55 kDa transmembrane protein with homology to C-type lectins, is present in numerous cell lines and tissue extracts. As one of the adaptor proteins, talin mediates the interactions between the actin filaments and the cell membrane by binding to integral membrane proteins and to the cytoskeleton. Layilin is a newly identified membrane-binding site for talin in peripheral ruffles of spreading cells, a ten-amino acid motif in the layilin cytoplasmic domain is sufficient for talin binding, and its adjacent LH2-LH3 tandem arrays in the cytoplasmic domain provide docking sites for talin. Layilin binds specifically to hyaluronan (HA) through its extracellular domain, a ubiquitous extracellular matrix component in most animal tissues and body fluids, but not to other tested glycosaminoglycans. The research suggests that layilin may mediate signals from extracellular matrix to the cell cytoskeleton via interaction with different intracellular binding partners and thereby be involved in the modulation of cortical structures in the cell. All the above actions reveal an interesting parallel between layilin and the known HA receptor CD44. In addition, merlin and radixin have been identified as different intracellular binding partners of layilin. Accordingly, it has been suggested that layilin plays roles in a variety of cellular processes, including cell shape, adhesion, motility, and homeostasis, as well as signal transduction. In addition, layilin might play an important role in the process of invasion and lymphatic metastasis of lung carcinoma.
Lipopolysaccharide binding protein (LBP) is a plasma protein, belongs to a member of structurally and functionally related proteins which includes bactericidal permeability-increasing protein (BPI), plasma cholesteryl ester transfer protein (CETP) and phospholipid transfer protein (PLTP). It is involved in the acute-phase immunologic response to gram-negative bacterial infections. In cooperation with BPI. LBP binds LPS and interacts with the CD14 receptor, most likely playing a role in regulating LPS-dependent monocyte responses. Studies suggest that LBP is necessary for the rapid acute-phase response to LPS but not for the clearance of LPS from circulation. Finally, t The LBP gene is found on chromosome 20, directly downstream of the BPI gene.
LC3A, also known as MAP1LC3A, is one of the light chain subunits that function together with both MAP1A and/or MAP1B. MAP1A and MAP1B are microtubule-associated proteins that mediate the physical interactions between microtubules and components of the cytoskeleton. MAP1A and MAP1B each consist of a heavy chain subunit and multiple light chain subunits. As a light chain subunit, MAP1LC3A has an important part in neuronal development and in maintaining the balance between neuronal plasticity and rigidity. MAP1LC3A is expressed as two alternatively spliced isoforms that are expressed in testis, brain, heart, liver, and skeletal muscle but are absent in thymus and peripheral blood leukocytes.
Lipase family. The gene encoding this protein is expressed mainly in brain, liver and testes,followed by secreting into plasma and cerebral spinal fluid. The esterification of cholesterol is required for cholesterol transport. LCAT is a central enzyme in the extracellular metabolism of plasma lipoproteins. Defects in LCAT are the cause of lecithin-cholesterol acyltransferase deficiency (LCATD) and a cause of fish-eye disease (FED).
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