Glutamate carboxypeptidase 2, also known as FOLH1, PSMA, belongs to the M28B subfamily and the peptidase M28 family. It is highly expressed in prostate epithelium and can be detected in urinary bladder, kidney, testis, ovary, fallopian tube, breast, adrenal gland, liver, esophagus, stomach, small intestine, colon and brain (at protein level). PSMA is used as a diagnostic and prognostic indicator of prostate cancer, and as a possible marker for various neurological disorders such as schizophrenia, Alzheimer disease and Huntington disease. It has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity and has a preference for tri-alpha-glutamate peptides. PSMA involves in prostate tumor progression and also exhibits a dipeptidyl-peptidase IV type activity. In vitro, PSMA cleaves Gly-Pro-AMC. PSMA is stable at pH greater than 6.5.
Phosphoserine phosphatase (PSPH) belongs to a subfamily of the phosphotransferases. PSPH is the rate-limiting enzyme in l-serine biosynthesis. It has previously been found that Phosphoserine phosphatase (PSPH) plays a role in epidermal homeostasis. Phosphoserine phosphatase (PSP) catalyzes the hydrolysis of phosphoserine to serine. Phosphoserine phosphatase (PSPH) expression has been examined in human-mouse somatic cell hybrids retaining different combination of human chromosomes. Phosphoserine phosphatase (PSPH) is expressed throughout the proliferative layer of the epidermis and hair follicles in rodent and human skin and is highly induced in SCC. In keratinocytes; Phosphoserine phosphatase (PSPH) is a cytoplasmic protein that primarily localizes to endosomes and is present primarily as a homodimer. Knock down of Phosphoserine phosphatase (PSPH) dramatically diminished SCC cell proliferation and cyclin D1 levels in the presence of exogenous of l-serine production suggesting a non-canonical role for Phosphoserine phosphatase (PSPH) in epithelial carcinogenesis. Phosphoserine phosphatase (PSPH) is highly induced in proliferative normal keratinocytes and in skin tumors. Phosphoserine phosphatase (PSPH) appears to be critical for the proliferation of SCC cells; however; this phenomenon may not involve the phosphoserine metabolic pathway.
Phosphoserine phosphatase (PSP) is an enzyme that belongs to the serB family. PSPH catalyzes magnesium-dependent hydrolysis of L-phosphoserine and is also involved in an exchange reaction between L-serine and L-phosphoserine. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. Deficiency of this protein is thought to be linked to Williams syndrome. A disorder that results in pre- and postnatal growth retardation; moderate psychomotor retardation and facial features suggestive of Williams syndrome.
Acts as a receptor for sonic hedgehog (SHH), indian hedgehog (IHH) and desert hedgehog (DHH). Associates with the smoothened protein (SMO) to transduce the hedgehog's proteins signal. Seems to have a tumor suppressor function, as inactivation of this protein is probably a necessary, if not sufficient step for tumorigenesis.
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