GDNF family receptor alpha-2 is a glycosylphosphatidylinosito l (GPI)-linked cell surface receptor. It is part of the GDNF receptor family. Glial cell line-derived neurotrophic factor (GDNF) and neurturin (NTN) are two structurally related, potent neurotrophic factors that play key roles in the control of neuron survival and differentiation. GFRA2 mediates the NRTN-induced autophosphorylation and activation of the RET receptor. It also able to mediate GDNF signaling through the RET tyrosine kinase receptor. It acts preferentially as a receptor for NTN compared to its other family member, GDNF family receptor alpha 1.
Members of the glial cell line-derived neurotrophic factor (GDNF) family, including GDNF and Neurturin, play key roles in the control of vertebrate neuronal survivial and differentiation. GDNF is a glycosylated, disulfide-bonded homodimer that is distantly related to the TGF superfamily of growth factors. Three receptors for these factors, GFRα-1, GFRα-2, and GFRα-3 have been identified. The receptors do not contain transmembrane domains and are attached to the cell membrane by glycosyl-phosphoinositol linkage. Both GFRα-1 and GFRα-2 have been shown to mediate the GDNF-dependent and Neurturin-dependent phosphorylation and activation of the tyrosine kinase Ret. GFR-3 is expressed only during development. GFRα-2 binds Neurturin and mediates activation of RET receptor tyrosine kinase by both Neurturin and GDNF.
Gamma-Glutamylaminecyclotransferase is an enzyme that converts gamma-glutamylamines to free amines and 5-oxoproline which belongs to the gamma-glutamylcyclotransferase family. It shows high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and contributes to degradation of proteins cross-linked by transglutaminases. It degrades the cross-link between a lysine and a glutamic acid residue from two proteins that have been cross-linked by transglutaminases. This protein adopts the newly identified cyclotransferase fold, observed in Gamma-Glutamylcyclotransferase, an enzyme with activity toward gamma-glutamyl-alpha-amino acids.
Human Υ-Glutamylcyclotransferase belongs to the Transferases family, specifically the Aminoacyltransferase. Gamma-Glutamylcyclotransferase catalyzes the formation of 5-Pxoproline from Gamma-Glutamyl Dipeptides. It plays an important role in Glutathione Homeostasis. Gamma-Glutamylcyclotransferase induces the release of Cytochrome C from the mitochondria resulting in the induction of apoptosis.
Geranylgeranyl pyrophosphate synthase (GGPS1) is a member of the FPP/GGPP synthase family. GGPS1 is highly expressed in testis, heart and skeletal muscle. GGPS1 is localized in the cytoplasm and has geranylgeranyl diphosphate (GGPP) synthase activity. It catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins. Other transcriptional splice variants have been found.
Growth hormone (GH); also known as somatotropin; is a member of a family of growth factors. It plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. GH includes prolactin; placental lactogens; proliferins; and somatolactin. It is synthesized primarily by somatotropes in the anterior pituitary and is stored in secretory granules. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
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