The four human glycoprotein hormones chorionic gonadotropin (CG), luteinizing hormone (LH), follicle stimulating hormone (FSH), and thyroid stimulating hormone (TSH) are dimers consisting of alpha and beta subunits that are associated noncovalently. The alpha subunits of these hormones are identical, however, their beta chains are unique and confer biological specificity. The protein encoded by this gene is the alpha subunit and belongs to the glycoprotein hormones alpha chain family. Two transcript variants encoding different isoforms have been found for this gene.
CGB7 (chorionic gonadotropin, beta polypeptide 7) belongs to the glycoprotein hormones subunit beta family. Glycoprotein hormones are heterodimers consisting of a common alpha subunit and an unique beta subunit which confers biological specificity. CGB7 gene is a member of the glycoprotein hormone beta chain family and encodes the beta 7 subunit of chorionic gonadotropin (CG). CG is produced by the trophoblastic cells of the placenta and stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy. The beta subunit of CG is encoded by 6 genes which are arranged in tandem and inverted pairs on chromosome 19q13.3 and contiguous with the luteinizing hormone beta subunit gene. CGB7 is used as adjunctive therapy in the treatment of obesity. CGB7 also stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy.
Cell Growth Regulator with EF Hand Domain Protein 1 (CGREF1) is a secreted calcium ion binding protein. CGREF1 contains two EF-hand domains and both EF-hands are required for function. Human CGREF1 is synthesized as a 301 amino acid precursor that contains a 19 amino acid signal sequence, and a 282 amino acid mature chain. CGREF1 is probably digested extracellularly by an unknown serine protease generating extremely hydrophobic bioactive peptides. CGREF1 mediates cell-cell adhesion in a calcium-dependent manner. In addition, CGREF1 is able to inhibit growth in several cell lines.
Chromogranin A (CgA), also known as pituitary secretory protein I (SP-I), is a member of the granin family of regulated secretory proteins. CgA shares several protein characteristics common to the granin family: acidic isoelectric point, the capacity to bind calcium ions, the ability to form aggregates and multiple dibasic cleavage sites. Mature human CgA is 439 amino acids (aa) and contains 10 dibasic, proteolytic cleavage sites, capable of yielding several smaller peptides, each displaying a unique function. Mature human CgA shares 63% aa sequence identity with mouse and rat CgA. CgA is expressed exclusively in the secretory dense core granules of most normal and neoplastic neuroendocrine cells. Increased levels of CgA have been detected inpatients with neuroendocrine tumors as well as non-neuroendocrine tumors, hence CgA is an important serological marker for tumor diagnosis and monitoring tumorprogression/regression. It has been demonstrated in mouse model that full-length CgA containing its C-terminal region can impair angiogenesis and tumor growth. In addition, CgA can bind to Secretogranin III to regulate the biogenesis of secretory granules.
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