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).
Lipocalin-1, also known as Von Ebner gland protein, VEG protein, Tear prealbumin, VEGP, Tear lipocalin and LCN1, is a secreted protein which belongs to thecalycin superfamily and Lipocalin family. Human Lipocalin-1 / VEGP was originally described as a major protein of human tear fluid, which was thought to be tear specific. Lipocalin-1 / VEGP is identical with lingual von Ebner's gland protein, and is also produced in prostate, nasal mucosa and tracheal mucosa. Homologous proteins have been found in rat, pig and probably dog and horse. Lipocalin-1 / VEGP is an unusual lipocalin member, because of its high promiscuity for relative insoluble lipids and binding characteristics that differ from other members. Lipocalin-1 / VEGP acts as the principal lipid binding protein in tear fluid, a more general physiological function has to be proposed due to its wide distribution and properties. Lipocalin-1 / VEGP would be ideally suited for scavenging of lipophilic, potentially harmful substances and thus might act as a general protection factor of epithelia. Lipocalin-1 / LCN1 could play a role in taste reception. It could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Lipocalin-1 / LCN1 can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. It exhibits an extremely wide ligand pocket.
Lymphocyte cytosolic protein 2（LCP2）contains a SAM domain and a SH2 domain. It is highly expressed in spleen, thymus and peripheral blood leukocytes, T-cell and monocytic cell lines, but expressed at lower level in B-cell lines. LCP2 was originally identified as a substrate of the ZAP-70 protein tyrosine kinase following T cell receptor (TCR) ligation in the leukemic T cell line Jurkat. It is phosphorylated after T-cell receptor activation by ZAP70, ITK and TXK, which leads to the up-regulation of Th1 preferred cytokine IL-2 during post-translational modification. Studies using LCP2-deficient T cell lines or mice have provided strong evidence that SLP-76 plays a positive role in promoting T cell development and activation as well as mast cell and platelet function.
L-Lactate Dehydrogenase A Chain (LDHA) is an enzyme that catalyzes the conversion of L-lactate and NAD+ to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA contains an N-terminal coenzyme binding region, a central catalytic site, and at least nine utilized Lys acetylation and two Tyr phosphorylation sites. LDHA belongs to the lactate dehydrogenase family, expressed predominantly in muscle tissue. LDHA mutations have been linked to exertional myoglobinuria.
L-Lactate Dehydrogenase B Chain (LDH-B) is a member of the lactate dehydrogenase family that consists of three members, LDH-A, LDH-B and LDH-C, members of this family function as powerful markers for germ cell tumors. LDH-B is an oxidoreductase that catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. It converts pyruvate to lactate when oxygen is absent or in short supply and it performs the reverse reaction during the Cori cycle in the liver. It is also called Hydroxybutyrate Dehydrogenase (HBD) due to its ability to catalyze the oxidation of hydroxybutyrate.
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