PSG2 is a secreted protein that in humans is encoded by the PSG2 gene. It is a member of the human pregnancy-specific glycoproteins (PSGs) family. These proteins are synthesized in large amounts by placental trophoblasts and released into the maternal circulation during pregnancy. PSG2 consist of a single N domain, with structural similarity to the immunoglobulin variable domains, followed by a variable number of immunoglobulin constant-like A and/or B domains. It has an arg-gly-asp (RGD) motif, which has been shown to function as an adhesion recognition signal for several integrins, in the N-terminal domain.
Pregnancy-specific beta-1-glycoprotein 3 is also known as Carcinoembryonic Antigen SG5,Pregnancy-Specific Glycoprotein 3 ,PS-Beta-G-3, PSBG-3.It belongs to the immunoglobulin superfamily. CEA family.It synthesized in large amounts by placental trophoblasts and released into the maternal circulation during pregnancy. Molecular cloning and analysis of several PSG genes has indicated that the PSGs form a subgroup of the carcinoembryonic antigen (CEA) gene family, Members of the CEA family consist of a single N domain, with structural similarity to the immunoglobulin variable domains, followed by a variable number of immunoglobulin constant-like A and/or B domains.
Pregnancy-specific beta-1-glycoprotein 5, is a secreted protein which belongs to the immunoglobulin superfamily, CEA family. It contains 2 Ig-like C2-type (immunoglobulin-like) domains and 1 Ig-like V-type (immunoglobulin-like) domain.
PSG6 is a pregnancy-specific glycoprotein(PSG). PSGs are secreted proteins which are produced by the rodent and primate placenta and play a critical role in pregnancy success. The levels of PSGs are highest during the third trimester of pregnancy, a time marked by the most profound suppression of MS disease attacks. PSGs regulate T-cell function. The regulation of T-cell function during pregnancy is likely the result of significant hormonal changes and may well involve immunoregulatory proteins derived from the placenta. Pregnancy specific glycoproteins (PSGs) are the most abundant placentally derived glycoproteins in the maternal serum. PSG1, PSG6, PSG6N, and PSG11 induce dose-dependent secretion of anti-inflammatory cytokines by human monocytes. Human and murine PSGs exhibit cross-species activity.
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.
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