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.
Lymphocyte Antigen 6H (LY6H) is a novel member of the LY6 family of glycosylphosphatidylinositol-anchored cell surface glycoproteins. LY6H contains one UPAR/Ly6 domain. Human LY6H is synthesized as a 140 amino acid precursor that contains a 25 amino acid signal sequence, 20 amino acid propeptide that is removed in the mature form, and a 90 amino acid mature chain. LY6H is highly expressed in the brain (cerebral cortex, amygdala, hippocampus and subthalamic nucleus) and in acute human leukemic cell line MOLT-3. It is also found in lower levels in testis, pancreas, small intestine and colon. It has been shown that LY6H may play a role in both the central nervous system and the immune system.
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.
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