Lysozyme G-Like Protein 2 (LYG2) is a secreted protein that belongs to the glycosyl hydrolase 23 family. LYG2 contains one SLT domain, one protein domain present in bacterial lytic transglycosylase (SLT) and in eukaryotic lysozymes (GEWL). SLT domain catalyzes the cleavage of the β-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyglucosamine (GlcNAc). LYG2 has hydrolase activity which acting on glycosyl bonds, and possess lysozyme activity.
Lymphotactin is a secreted protein which belongs to the intercrine gamma family. It is also a member of the XC chemokine family. XCL1 is found in spleen with highest level, lower in peripheral leukocytes and very low levels in lung, colon and small intestine. XCL1 plays a role in inflammatory and immunological responses, inducing leukocyte migration and activation. XCL1 induces chemotactic function by binding to a chemokine receptor called XCR1. XCL1 is closely related to another chemokine called XCL2.
Tyrosine-protein kinase Lyn is a member of the Src family of protein tyrosine kinases, which is mainly expressed in hematopoietic cells, in neural tissues liver, and adipose tissue. Tyrosine-protein kinase Lyn has many functions. Lyn kinase may down regulate expression of stem cell growth factor receptor (KIT). Lyn kinase Acts as an effector of EpoR (erythropoietin receptor) in controlling KIT expression and may play a central role in erythroid differentiation during the switch between proliferation and maturation. Lyn kinase also acts as a positive regulator of cell movement while negatively regulating adhesion to stromal cells by inhibiting the ICAM-1-binding activity of beta-2 integrins. Lyn kinase relays suppressing signals from the chemokine receptor CXCR4 to beta-2 integrin LFA-1 in hematopoietic precursors. This kinase is Involved in induction of stress-activated protein kinase (SAPK), but not ERK or p38 MAPK, in response to genotoxic agents. Tyrosine-protein kinase Lyn Required for the initiation of the B-cell response, but also for its down-regulation and termination. It also Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. It has been reported that Lyn kinase plays a role in the inflammatory response to bacterial lipopolysaccharide. Lyn kinase Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells.
Ly6 / PLAUR domain-containing protein 3; also known as GPI-anchored metastasis-associated protein C4.4A homolog; Matrigel-induced gene C4 protein; MIG-C4 and LYPD3; is a cell membrane protein which contains twoUPAR/Ly6 domains. Human LYPD3 contains twoUPAR/Ly6 domains. LYPD3 is expressed in placenta; skin and urothelium. It is found in suprabasal keratinocytes of chronic wounds. Weak expression of LYPD3 is found in esophagus and peripheral blood mononuclear cells. It is found in the majority of primary and metastatic transitional cell carcinomas (TCCs) and as well in breast cancer tissues; but not in adjacent normal tissues. High expression of LYPD3 is found in the tumor component of some noninvasive superficial lesions and in invasive and metastatic urothelial cancers. LYPD3 is up-regulated in migrating keratinocytes during epithelisation of incisional skin wounds. LYPD3 supports cell migration. It may be involved in urothelial cell-matrix interactions. It may also be involved in tumor progression
Ly6/PLAUR domain containing3 (LYPD-3) is a GPI-linked protein. The structure of LYPD-3 is similar to the urokinasetype plasminogen activator receptor (uPAR). LYPD-3 is a 6 -100 kDa molecule with variable cell type-specific N-O-linked glycosylation; mature human LYPD-3 contains two uPAR/Ly6 domains and a Ser/Thr/Pro-rich (STP) region includes a protease sensitive site . The interaction of LYPD-3 with Laminin 1 and 5 on neighboring cells promotes the adhesion; spreading; and migration of tumor cells. LYPD-3 additionally interacts with Galectin-3 and the anterior gradient proteins AG-2 and AG-3. LYPD-3 overexpression in non-small cell lung cancer is predictive of increased mortality.
Acyl-Protein Thioesterase 1 (APT-1) is lysophospholipase that belongs to the AB hydrolase 2 family. Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. APT-1 performs on biological membranes to regulate the multifunctional lysophospholipids. It hydrolyzes lysophosphatidylcholine in both monomeric and micellar forms. It hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS; in addition, it also has depalmitoylating activity and low lysophospholipase activity.
Acyl-Protein Thioesterase 2 is a cytoplasmic protein that belongs to the AB Hydrolase 2 family. LYPLA2 is a lysophospholipase and hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. LYPLA2 has hydrolase activity that converts Palmitoyl-protein to palmitate and protein. LYPLA2 regulates the multifunctional lysophospholipids by acting on biological membranes. LYPLA2 participates in Glycerophospholipid metabolism pathway; fatty acid metabolic process and lipid metabolic process.
lysozyme C is a secreted protein and belongs to the glycosyl hydrolase 22 family. Lysozymes have primarily a bacteriolytic function, damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.
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