Pregnancy-specific beta-1-glycoprotein 9(PSG9) is a secreted protein and contains 3 Ig-like C2-type (immunoglobulin-like) domains, 1 Ig-like V-type (immunoglobulin-like) domain. It is a member of the PSG family, a group of closely related secreted glycoproteins that are highly expressed in fetal placental syncytiotrophoblast cells. The members of the PSG protein family all have a characteristic N-terminal domain that is homologous to the immunoglobulin variable region. PSGs become detectable in serum during the first two to three weeks of pregnancy and increase as the pregnancy progresses, eventually representing the most abundant fetal protein in the maternal blood at term. PSGs function to stimulate secretion of TH2-type cytokines from monocytes, and they may also modulate the maternal immune system during pregnancy, thereby protecting the semi-allotypic fetus from rejection. PSGs are commonly expressed in trophoblast tumors. Eleven human PSG proteins (PSG1-PSG11) have been described.
PSGL-1 (CD162), is a mucintype glycoprotein that plays a key role in leukocyte adhesion. Human PSGL-1 cDNA encodes 412 amino acids (aa). It expressed on neutrophils, monocytes and most lymphocytes. The mature PSGL-1 (aa 42-412) is expressed as a disulfide-linked homodimer that signals intracellularly and promotes integrin activation. PSGL-1 is found on virtually all leukocytes, dendritic cells, platelets, and some endothelial cells. It is primarily responsible for early events in extravasation, especially rolling adhesion of leukocytes to vascular endothelium. Through high affinity, This SLe(x)-type proteoglycanPGSL-1 calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation.
P-selectin glycoprotein ligand-1 (PSGL-1), also known as SELPLG or CD162, is the high affinitycounter-receptor for P-selectin on expressed on activated endothelial cells and platelets. PSGL-1 is a mucin-type glycoprotein, expressed on leukocytes and platelets as a homodimer of two disulfide-linked subunits of ~120 kD. As cell adhesion molecules, multiple studies have shown that PSGL-1/ P-selectin interaction is required for the normal recruitment of leukocytes during inflammatory reactions, and also participates in hemostatic responses. PSGL-1 protein requires two distinct posttranslational modifications for the Ca2+-dependent recognition by the lectin domain of P-selectin, that is tyrosine sulfation and specific O-linked glycosylation (sialic acid and fucose). PSGL-1 can also bind to other two members of the selectin family, E-selectin (endothelial) and L-selectin (leukocyte), but binds best to P-selectin.
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.
Glutamate carboxypeptidase 2 , also known as Glutamate carboxypeptidase II , Membrane glutamate carboxypeptidase , Prostate-specific membrane antigen , GCPII , PSMA , FOLH1 , and NAALAD1 , is a single-pass type II membrane protein which belongs to thepeptidase M28 family and M28B subfamily. FOLH1 is highly expressed in prostate epithelium. It is detected in urinary bladder , kidney , testis , ovary , fallopian tube , breast , adrenal gland , liver , esophagus , stomach , small intestine , colon , brain (at protein level) , and the capillary endothelium of a variety of tumors. FOLH1 has both folate hydrolase and N-acetylated alpha linked acidic dipeptidase (NAALADase) activity. It has a preference for tri-alpha-glutamate peptides. Genetic variation in FOLH1 may be associated with low folate levels and consequent hyperhomocysteinemia. This condition can result in increased risk of cardiovascular disease , neural tube defects , and cognitive deficits. FOLH1 also shows a promising role in directed imaging and therapy of recurrent or metastatic disease.
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