Carboxypeptidase M (CPM) specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. Carboxypeptidase exert roles in the physiological processes of blood coagulation/fibrinolysis, inflammation, food digestion and pro-hormone and neuropeptide processing. CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins. It is widely distributed in a variety of tissues and cells. CPM is involved in peptide metabolism on both the cell surface and in extracellular fluids. CPM functions not only as a protease but also as a binding partner in cell-surface protein-protein interactions.
Carboxypeptidase M, also known as CPM, is a membrane-bound arginine/lysine carboxypeptidase which is a member of the carboxypeptidases family. These enzymes remove C-terminal amino acids from peptides and proteins and exert roles in the physiological processes of blood coagulation/fibrinolysis, inflammation, food digestion and pro-hormone and neuropeptide processing. Among the carboxypeptidases CPM is of particular importance because of its constitutive expression in an active form at the surface of specialized cells and tissues in the human body. CPM in the brain appears to be membrane-bound via a phosphatidylinositol glycan anchor. CPM is widely distributed in a variety of tissues and cells. The amino acid sequence of CPM indicated that the C-terminal hydrophobic region might be a signal for membrane attachment via a glycosylphosphatidylinositol (GPI) anchor. CPM is involved in peptide metabolism on both the cell surface and in extracellular fluids. CPM functions not only as a protease but also as a binding partner in cell-surface protein-protein interactions.
Cardiotrophin-1, also known as CT-1 and CTF1, is a member of the IL-6 superfamily. It is a sreted cytokine that is expressed in heart, skeletal muscle, prostate and ovary, and to lower levels in lung, kidney, pancreas, thymus, testis and small intestine. The protein exerts its cellular effects by interacting with the glycoprotein 130 (gp130)/leukemia inhibitory factor receptor beta (LIFR) heterodimer. In addition, CT-1 activates phosphatidylinositol 3-kinase (PI-3 kinase) in cardiac myocytes and enhances transcription factor NF-κB DNA -binding activities.
Z-farnesyl diphosphate synthase (FDPS) is an enzyme belonging to the family of transferases; specifically those transferring aryl or alkyl groups other than methyl groups. Z-farnesyl diphosphate synthase (FDPS) functions as key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate; a precurcor for several classes of essential metabolites. FDPS catalyzes the production of geranyl pyrophosphate and farnesyl pyrophosphate from isopentenyl pyrophosphate and dimethylallyl pyrophosphate. The resulting product; farnesyl pyrophosphate; is a key intermediate in cholesterol and sterol biosynthesis; a substrate for protein farnesylation and geranylgeranylation; and a ligand or agonist for certain hormone receptors and growth receptors. Drugs that inhibit this enzyme prevent the post-translational modifications of small GTPases and have been used to treat diseases related to bone resorption. Functions of FDPS may be inactivated by interferon-induced RSAD2. This inactivation may result of disruption of lipid rafts at the plasma membrane; and thus have an antiviral effect since many enveloped viruses need lipid rafts to bud efficiently out of the cell.
In RNAseq data from human islet donors, CARTPT expression levels correlated with insulin, exocytosis genes and key beta-cell transcription factors. Insufficient insulin release and hyperglucagonaemia are culprits in type 2 diabetes. Cocaine- and amphetamine-regulated transcript (CART, encoded by Cartpt) affects islet hormone secretion and beta cell survival in vitro in rats, and Cart (-/-) mice have diminished insulin secretion. Established a potential role for cocaine and amphetamine regulated transcript (CARTPT) in dominant follicle selection in cattle. CARTPT expression is elevated in subordinate versus dominant follicles, and treatment with the mature form of the CARTPT peptide (CART) decreases follicle-stimulating hormone (FSH)-stimulated granulosa cell estradiol production in vitro and follicular fluid estradiol and granulosa cell CYP19A1 mRNA in vivo.
Peripheral plasma membrane protein CASK; also known as calcium/calmodulin-dependent serine protein kinase; CASK and LIN2; is a nucleus; cytoplasm and cell membrane protein which belongs to theMAGUK family. CASK / LIN2 contains oneguanylate kinase-like domain; twoL27 domains; onePDZ (DHR) domain; oneprotein kinase domain and oneSH3 domain. CASK / LIN2 is ubiquitously expressed. Expression of CASK / LIN2 is significantly greater in brain relative to kidney; lung; and liver and in fetal brain and kidney relative to lung and liver. CASK / LIN2 is a multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK / LIN2 contributes to neural development and regulation of gene expression via interaction with the transcription factor TRB1. It binds to cell-surface proteins; including amyloid precursor protein; neurexins and syndecans. CASK / LIN2 may mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1. Defects in CASK are the cause of mental retardation X-linked CASK-related (MRXCASK). Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Defects in CASK are also the cause of FG syndrome type 4 which is an X-linked disorder characterized by mental retardation; relative macrocephaly; hypotonia and constipation.
Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-10,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.
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