Glutamate Oxaloacetate Transaminase 1 (GOT1) is a cytoplasmic protein. GOT1 belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. GOT1 is a pyridoxal phosphate-dependent enzyme that exists in cytoplasmic and mitochondrial forms. GOT1 plays a key role in amino acid metabolism and the urea and tricarboxylic acid cycles. GOT1 involves in L-methionine salvage from methylthioadenosine, aspartate catabolic process, cellular response to insulin stimulus, polyamine metabolic process, and glucocorticoid stimulus.
Glutaminyl cyclase, also known as QPCT, can promote the N-terminal cyclization reaction of N-terminal pyroglutamate(pGlu). The pGlu formation from its glutaminyl precursor is required in the maturation of numerous bioactive peptides, while the aberrant formation of pGlu may be related to several pathological processes, such as osteoporosis and amyloidotic diseases. Glutaminyl cyclase's structure reveals an alpha/beta scaffold akin to that of two-zinc exopeptidases but with several insertions and deletions, particularly in the active-site region. Glutaminyl cyclase's amino acid sequence of this enzyme is 86% identical to that of bovine glutaminyl cyclase. It is responsible for the presence of pyroglutamyl residues in many neuroendocrine peptides.
The protein encoded by this gene, glutathione S-transferase (GST) theta 2B (GSTT2B), is a member of a superfamily of proteins that catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. Human GSTs can be divided into five main classes: alpha, mu, pi, theta, and zeta. The theta class includes GSTT1, GSTT2, and GSTT2B. GSTT2 and GSTT2B are nearly identical to each other, and share 55% amino acid identity with GSTT1. All three genes may play a role in human carcinogenesis. The GSTT2B gene is a pseudogene in some populations.
The Glypicans are a small multigene family of GPI-linked proteoglycans that play a key role in growth factor signaling. Human Glypican 1 (GPC1) is synthesized as a 558 amino acid (aa) preproprecursor that contains a 23 aa signal sequence, a 507 aa mature segment, and a 28 aa C-terminal prosegment. There are two potential N-linked and four potential O-linked sites for glycosylation or glycanation. There are potentially two heparan sulfate (HS) modifications on GPC1 that could contribute to a native molecular weight of approximately 200 kDa. Mature human GPC1 shares 91% aa identity with mature mouse GPC1. Cells known to express GPC1 include neurons, smooth and skeletal muscle cells, keratinocytes, osteoblasts, Schwann cells, immature dendritic cells, and tumor, plus tumorassociated vascular endothelial cells. The function of GPC1 is complex and varied. As a proteoglycan, it appears to make use of its HS adduct to impact select growth factor activity. This is accomplished by having juxtramembrane HS attachment sites, and a flexible, GPI-linkage.
Glypican-3/GPC3 is a member of the glypican family. It belongs to the glypican family and is highly expressed in lung, liver, and kidney. It is a heparan sulfate proteoglycan, which is overexpressed in various neoplasms such as hepatocellular carcinoma, malignant melanoma, and testicular yolk sac tumor, and plays an important role in cell growth and differentiation. GPC3 function is tissue dependent. In some tissues, GPC3 acts as a tumor suppressor gene, whereas in others, it acts as an oncofetal protein. GPC3 is a reliable marker for hepatocellular carcinoma. The sensitivity and specificity exceeds both alpha-fetoprotein and hepatocyte-paraffin1. GPC3 immunohistochemistry can aid in the differentiation of testicular germ cell tumors, being expressed in all yolk sac tumors but not in seminomas. GPC3 expression has also been identified in some squamous cell carcinomas of the lung and clear cell carcinomas of the ovary. Glypican-3 is currently regarded as a tumor marker and potential target for immunotherapy.
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