The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Cluster of differentiation 36 (CD36), also known as FAT, SCARB3, GP88, glycoprotein IV (gpIV) and glycoprotein IIIb (gpIIIb), is a member of the CD system as well as the class B scavenger receptor family of cell surface proteins. CD36 can be found on the surface of many cell types in vertebrate animals and it consists of 472 amino acids and is extensively glycosylated. It is an integral membrane protein primarily serving as receptors for thrombospondin and collagen and by the erythrocytes infected with the human malaria parasite. The role of CD36 as a cell surface receptor has been extended to that of a signal transduction molecule.
Human Glycoprotein A33 (GPA33) is a single-pass type I membrane protein; belongs to the CTX family of cell adhesion molecular within the immunoglobulin family; can be expressed in normal gastrointestinal epithelium and in 95% of colon cancers. GPA33 consists of one Ig-like C2-type domain and one Ig-like V-type domain. The predicted mature protein includes a single transmembrane domain; a extracellular region and a intracellular tail. Intracellular traffic and recycling to the cell surface appear to play an important role in GPA33 function and to have an influence on its surface density superseding translation regulation. GPA33 has become a promising target of immunologic therapy strategies. GPA33 may also play a important role in cell-cell recognition and signaling.
Glypican-3/GPC3 is a member of the glypican family. It belongs to the glypican family and is highly expressed in lung, liver, and kidney. It is a heparan sulfate proteoglycan, which is overexpressed in various neoplasms such as hepatocellular carcinoma, malignant melanoma, and testicular yolk sac tumor, and plays an important role in cell growth and differentiation. GPC3 function is tissue dependent. In some tissues, GPC3 acts as a tumor suppressor gene, whereas in others, it acts as an oncofetal protein. GPC3 is a reliable marker for hepatocellular carcinoma. The sensitivity and specificity exceeds both alpha-fetoprotein and hepatocyte-paraffin1. GPC3 immunohistochemistry can aid in the differentiation of testicular germ cell tumors, being expressed in all yolk sac tumors but not in seminomas. GPC3 expression has also been identified in some squamous cell carcinomas of the lung and clear cell carcinomas of the ovary. Glypican-3 is currently regarded as a tumor marker and potential target for immunotherapy.
GPD1; also known as glycerolphosphate dehydrogenase 1; is a member of the NAD-dependent glycerol-3-phosphate dehydrogenase family. GPD1 catalyzes the reversible redox conversion ofdihydroxyacetone phosphate (DHAP); thus plays a critical role in carbohydrate and lipid metabolism. It also reduces nicotine adenine dinucleotide (NADH) to glycerol-3-phosphate (G3P) and NAD+. Meanwhile; GPD1 and mitochondrial glycerol-3-phosphate dehydrogenase also form a glycerol phosphate shuttle that facilitates the transfer of reducing equivalents from the cytosol to mitochondria. Mutations in GPD1 gene are a cause of transient infantile hypertriglyceridemia.
Glycerol-3-Phosphate Dehydrogenase [NAD(+)]; Cytoplasmic (GPDH-C) belongs to the NAD-Dependent Glycerol-3-Phosphate Dehydrogenase family. GPDH-C plays a critical role in carbohydrate and lipid metabolism by catalyzing the reversible conversion of Dihydroxyacetone Phosphate (DHAP) and reducing Nicotine Adenine Dinucleotide (NADH) to Glycerol-3-Phosphate (G3P) and NAD+. GPDH-C is inhibited by zinc ions and sulfate. Mutations in this gene are a cause of transient infantile hypertriglyceridemia. GPDH-C is unlike Glyceraldehyde 3-Phosphate Dehydrogenase (GAPDH); they have different substrates.
Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) is a member of the Ly6 family of proteins, binds LPL in the subendothelial spaces and transports it to the capillary lumen. GPIHBP1 is an important regulator of triglyceride metabolism by increasing the efficiency of lydrolysis by LPL and uptake of fatty acids. GPIHBP1 was positively correlated with LPL, and GPIHBP1 is a better marker for body weight decrease than LPL.
Lascia la tua email e seleziona le aree che vuoi seguire per ricevere novita di prodotto, approfondimenti tecnici e promozioni piu pertinenti.
Puoi scegliere le macro-aree Life Science e Diagnostica oppure le singole specializzazioni.
Seleziona uno o piu ambiti di interesse per ricevere comunicazioni piu utili e mirate.
Aggiornamenti su ricerca, strumentazione e applicazioni per il mondo Life Science.
Novita, approfondimenti e promozioni per laboratori diagnostici e flussi operativi.
2025 TEMA Ricerca - All Rights Reserved.
