Tumor necrosis factor receptor superfamily member 3; also known as Lymphotoxin-beta receptor;Tumor necrosis factor C receptor;Tumor necrosis factor receptor 2-related protein;Tumor necrosis factor receptor type III;LTBR;TNFCR; TNFR3 and TNFRSF3; is a member of the tumor necrosis factor (TNF) family of receptors. LTBR is a single-pass type I membrane protein and contains four TNFR-Cys repeats. It is expressed on the surface of most cell types; but not on T and B lymphocytes. LTBR and its ligand play a role in the development and organization of lymphoid tissue and transformed cells. Activation of LTBR can trigger apoptosis. In addition; LTBR can lead to the release of the cytokine interleukin 8.
Leukotriene C4 synthase, also known as LTC4 synthase, Leukotriene-C(4) synthase, and LTC4S, is a multi-pass membrane protein which belongs to theMAPEG family. LTC4S is detected in lung, platelets and the myelogenous leukemia cell line KG-1 (at protein level). LTC4S activity is present in eosinophils, basophils, mast cells, certain phagocytic mononuclear cells, endothelial cells, vascular smooth muscle cells and platelets. LTC4S is essential for the production of cysteinyl leukotrienes (Cys-LT), critical mediators in asthma. Mutagenic analysis of the conjugation function of human LTC4S has identified R51 and Y93 as critical for acid and base catalysis of LTA4 and reduced glutathione, respectively. A comparison across species for proteins that possess LTC4S activity reveals conservation of both of these residues, whereas R51 is absent in the FLAP molecules. Thus, within the glutathione S-transferase superfamily of genes, alignment of specific residues allows the separation of LTC4S family members from their most structurally similar counterparts, the FLAP molecules. Defects in LTC4S are the cause of leukotriene C4 synthase deficiency (LTC4 synthase deficiency). LTC4 synthase deficiency is a fatal neurometabolic developmental disorder. It is associated with muscular hypotonia, psychomotor retardation, failure to thrive, and microcephaly.
Lactotransferrin is a member of the transferrin family that transfer iron to the cells and control the level of free iron in the blood and external secretions. Lactotransferrin is a secreted protein and contains two transferrin-like domains. Lactotransferrin can be cleaved into the following four chains: Kaliocin-1, Lactoferroxin-A, Lactoferroxin-B, and Lactoferroxin-C. Lactoferroxin A, Lactoferroxin B, and Lactoferroxin C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while Lactoferroxin B and Lactoferroxin C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors. LTF has antimicrobial activity (bacteriocide, fungicide) and is part of the innate defense, mainly at mucoses.
This gene is a member of the transferrin family of genes and its protein product is found in the secondary granules of neutrophils. The protein is a major iron-binding protein in milk and body secretions with an antimicrobial activity, making it an important component of the non-specific immune system. The protein demonstrates a broad spectrum of properties, including regulation of iron homeostasis, host defense against a broad range of microbial infections, anti-inflammatory activity, regulation of cellular growth and differentiation and protection against cancer development and metastasis. Antimicrobial, antiviral, antifungal and antiparasitic activity has been found for this protein and its peptides. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Lumican is a 40 kD secreted protein which belongs to the small leucine-rich repeat proteoglycans (SLRPs) and the class II subfamily. Human Lumican is synthesized as a 338 amino acid precursor then cut the 18 aa signal sequence. The mature Human Lumican contains 12 leucine-rich repeats (LRRs), 4 potential sites of N-linked glycosylation, and a C- terminal with two conserved cyst-eines. Lumican can be existed in extracellular matrix of human articular cartilage. Lumican participates in the maintenance of tissue homeostasis and regulates cellular functions in vivo, such as cell proliferation, adhesion, migration, and differentiation. The overexpression of lumican has been correlated to colorectal tumor, breast, neuroendocrine, and pancreatic cancers.
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