Amphoterin-Induced Protein 2 (AMIGO2) is a single-pass type I membrane protein which belongs to the AMIGO family of immunoglobulin superfamily. Mature AMIGO2 contains an Ig-like C2-type (immunoglobulin-like) domain; 6 LRR (leucine-rich) repeats; a LRRCT domain; as well as a LRRNT domain. AMIGO2 is mainly expressed in in breast; ovary; cervix; and uterus; although lower in lung; colon; and rectum. AMIGO2 required for depolarization-dependent survival of cultured cerebellar granule neurons. AMIGO2 may mediate homophilic as well as heterophilic cell-cell interaction with AMIGO1 or AMIGO3. AMIGO2 may contribute to signal transduction through its intracellular domain; and may be required for tumorigenesis of a subset of gastric adenocarcinomas.
Amphiregulin (AREG) is a single-pass membrane protein with 252 amino acids. AREG belongs to the amphiregulin family, which contains 1 EGF-like domain. AREG is expressed in a variety of tissues including ovary, placenta, lung, kidney, stomach, colon, and breast. It is related to Epidermal Growth Factor (EGF) and Transforming Growth Factor Alpha (TGF-alpha). As an EGF-related growth factor, AREG interacts with the EGF/TGF-alpha receptor to promote the growth of normal epithelial cells and inhibits the growth of certain aggressive carcinoma cell lines. AREG may also play a protective role in Bleomycin-Induced Pneumopathy.
AMP-activated protein kinase (AMPK) is a heterotrimeric complex consisting of a catalytic alpha subunit and regulatory beta and gamma subunits. Each subunit exists as alternate isoforms ( alpha 1, alpha 2, beta 1, beta 2, gamma 1, gamma 2, gamma 3), with all 12 combinations able to form complexes. The catalytic alpha subunit of AMPK is activated allosterically by AMP, and by phosphorylation via the AMPK kinases LKB1 and CaMKK beta. AMPK’s role in metabolic regulation has implicated this serine/threonine kinase as a therapeutic target in heart disease, obesity, and diabetes.
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