Myoglobin is a 17KDa cytoplasmic oxygen-binding protein encoded by the MB gene and expressed in myocytes of the heart and skeletal muscle. Its name derives from its structural and functional similarity to hemoglobin, the oxygen binding protein found in red blood cells. Functions of myoglobin include oxygen storage and transport, as well as scavenging of NO and reactive oxygen species. Myoglobin also serves as a sensitive marker for muscle injury resulting from cardiac infarction. Myoglobin was the first protein to have its three-dimensional structure determined by X-ray crystallography.
Myozenins may serve as intracellular binding proteins involved in linking Z-disk proteins such as alpha-actinin, gamma-filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis.
Myozenin 2 (MYOZ2) is a 264 amino acid protein that belongs to the myozenin family. MYOZ2 binds to Calcineurin, a phosphatase that is involved in calcium-dependent signal transduction in diverse cell types. MYOZ2 is one of the sarcomeric proteins and plays an important role in myofibrillogenesis and the modulation of calcineurin signaling. It may serve as intracellular binding proteins involved in linking Z line proteins such as alpha-actinin, gamma-filamin, TCAP/telethonin, LDB3/ZASP and plays an important role in the modulation of calcineurin signaling. Defects in MYOZ2 are the cause of familial hypertrophic cardiomyopathy type 16 (CMH16), a hereditary heart disorder.
Pyruvate dehydrogenase kinase, isozyme 1, also known as [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial and PDK1, is a member of the PDK / BCKDK protein kinase family. PDK-1 is expressed predominantly in the heart. It contains onehistidine kinase domain. Pyruvate dehydrogenase kinase (PDK) isoforms are molecular switches that downregulate the pyruvate dehydrogenase complex (PDC) by reversible phosphorylation in mitochondria. An inhibitory effect of lipoic acid on PDKs would result in less phosphorylation of E1 and hence increased PDC activity. At least two isoenzymic forms of pyruvate dehydrogenase kinase ( PDK-1 and PDK-2 ) may be involved in the regulation of enzymatic activity of mammalian pyruvate dehydrogenase complex by phosphorylation. PDK-3 appears to have the highest specific activity among the three isoenzymes. PDK-1 inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism.
N-acetylated-alpha-linked acidic dipeptidase-like protein, also known as NAALADL1, NAALADase L, and Ileal dipeptidylpeptidase, is a Single-pass type I I membrane protein and a member of the peptidase M28 family and M28B subfamily. NAALADase L is mainly expressed in the distal small intestine. It is also expressed in the spleen and testis and Weakly expressed in the brain, locating mainly to the brain stem, amygdala, thalamus and ventral striatum. NAALADase L is a chloride-activated, membrane bound, metallopeptidase that cleaves the endogenous neuropeptide N-acetyl-aspartyl-glutamate (NAAG). NAAG acts as a partial NMDA agonist as well as a full agonist at the presynaptic metabotropic glutamate receptor 3 (mGluR3), where it acts to reduce glutamate release. NAALADase L also exhibits a dipeptidyl-peptidase IV type activity. NAALADase inhibition may be a novel therapeutic approach to reduce or inhibit heightened aggressiveness, and possibly to treat aggressive behavior associated with psychiatric disorders.
Neuronal Acetylcholine Receptor Subunit α-5 (NACHRA5) is a member of the ligand-gated ion channel family. Neuronal AChR is composed of two different type of subunits: α and non-α. When NACHRA5 binds to acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits, leading to the opening of an ion-conducting channel across the plasma membrane. Genetic variations in NACHRA5 have been related to susceptibility to smoking-related behavioral traits and lung cancer, contributing to the smoking quantitative trait locus 3.
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