Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV).
This protein is a minor sialoglycoprotein in human erythrocyte membranes. The blood group Gerbich antigens and receptors for Plasmodium falciparum merozoites are most likely located within the extracellular domain. Glycophorin-C plays an important role in regulating the stability of red cells.
Glypicans are a family of HSPGs that are attached to the cell membrane by a glycosyl-phosphatidylinositol anchor. Glypicans are considered to have the ability to modulate the activities of HBGFs. The expression of glypicans is regulated temporally and spatially during development, suggesting they are involved in development and morphogenesis. To date, six glypicans (Glypican 1 to Glypican 6) have been identified in mammals. Glypican 1 (GPC1) is most ubiquitously expressed in adult tissues. GPC1 promotes efficient signaling by HBGFs and plays a critical role in cell growth and differentiation. GPC1 is involved in tumorigenesis and angiogenesis, and is frequently overexpressed in several types of tumors including pancreatic carcinoma, breast cancer and glioma.
Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Members of the glypican-related integral membrane proteoglycan family (GRIPS) contain a core protein anchored to the cytoplasmic membrane via a glycosyl phosphatidylinositol linkage. These proteins may play a role in the control of cell division and growth regulation. The protein encoded by this gene can bind to and inhibit the dipeptidyl peptidase activity of CD26, and it can induce apoptosis in certain cell types. Deletion mutations in this gene are associated with Simpson-Golabi-Behmel syndrome, also known as Simpson dysmorphia syndrome. Alternative splicing results in multiple transcript variants.
Glypican 3 belongs to Glypicans (GPCs), a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) that may play a role in the control of cell division and growth regulation. In mammals, there are six GPCs (GPC1 to GPC6), all of which have a similar core-protein size of approx. 60 kDa and the clustering of glycosaminoglycan attachment site near the C-terminus. They are tethered to the cell surface by GPI linkages, which can be cleaved by endogenous phospholipases, thus releasing the protein. Glypican 3 (GPC3) is highly expressed in many tissues during development and plays an important role in the regulation of embryonic growth. Loss-of-function mutations of GPC3 result in the Simpson-Golabi-Behmel overgrowth syndrome (SGBS), and Gpc-3 null mice display developmental overgrowth. In hepatocellular carcinoma (HCC), the overexpression of glypican 3 has been demonstrated to be a reliable diagnostic indicator.
This gene encodes a sodium- and chloride-dependent glycine neurotransmitter transporter. This integral membrane glycoprotein is responsible for the clearance of extracellular glycine during glycine-mediated neurotransmission. This protein is found in glycinergic axons and maintains a high presynaptic pool of neurotransmitter at glycinergic synapses. Mutations in this gene cause hyperekplexia; a heterogenous neurological disorder characterized by exaggerated startle responses and neonatal apnea. Two transcript variants encoding different isoforms have been found for this gene.
The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids inThe secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Interactions betweenThe Golgi and microtubules are thought to be important forThe reorganization ofThe Golgi after it fragments during mitosis. This gene encodes one ofThe golgins, a family of proteins localized toThe Golgi. This encoded protein has been postulated to play roles inThe stacking of Golgi cisternae and in vesicular transport. Several alternatively spliced transcript variants of this gene have been described, butThe full-length nature of these variants has not been determined.
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