Human Myelin-Associated Glycoprotein,also known as MAG, Siglec-4,is a cell membrane glycoprotein that is a member of the SIGLEC family of proteins.MAG contains 4 Ig-like C2-type domains and 1 Ig-like V-type domain.MAG functions as an adhesion molecule during neural development. MAG is believed to be involved in myelination during nerve regeneration. it is a adhesion molecule in postnatal neural development that mediates sialic-acid dependent cell-cell interactions between neuronal and myelinating cells and Preferentially binds to alpha-2,3-linked sialic acid. Soluble MAG, which is released from myelin in large quantities, has been identified in normal human tissues and in tissues from patients with neurological disorders. It is believed that this soluble MAG might contribute to the lack of CNS neuron regeneration after injury.
Endoplasmic Reticulum Mannosyl-Oligosaccharide 1,2-α-Mannosidase (MAN1B1) belongs to the glycosyl hydrolase 47 family. MAB1B1 is a single-pass type II membrane protein and widely expressed in many tissues. MAB1B1 is involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. MAB1B1 can be inhibited by both 1-deoxymannojirimycin (dMNJ) and kifunensine. Defects in MAN1B1 are the cause of mental retardation autosomal recessive type 15 (MRT15). Mental retardation is characterized by significantly below average general intellectual functioning, it is also associated with impairments in adaptative behavior and manifested during the developmental period.
Mesencephalic astrocyte-derived neurotrophic factor, also known as Protein ARMET, Arginine-rich protein, MANF and ARMET, is a secreted protein which belongs to the ARMET family. ARMET selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. It modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. ARMET enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. ARMET inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. The N-terminal region of ARMET may be responsible for neurotrophic activity while the C-terminal region may play a role in the ER stress response. MANF reduces endoplasmic reticulum (ER) stress and has neurotrophic effects on dopaminergic neurons. Intracortical delivery of recombinant MANF protein protects tissue from ischemic brain injury. MANF has been described as a survival factor for dopaminergic neurons. MANF expression was widespread in the nervous system and non-neuronal tissues. In the brain, relatively high MANF levels were detected in the cerebral cortex, hippocampus and cerebellar Purkinje cells. The widespread expression of MANF together with its evolutionary conserved nature and regulation by brain insults suggest that it has important functions both under normal and pathological conditions in many tissue types.
Mesencephalic astrocyte-derived neurotrophic factor(MANF) is a secreted protein which belongs to the ARMET family. MANF selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. It modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. MANF enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. MANF inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. The N-terminal region of ARMET may be responsible for neurotrophic activity while the C-terminal region may play a role in the ER stress response. MANF reduces endoplasmic reticulum (ER) stress and has neurotrophic effects on dopaminergic neurons. Intracortical delivery of recombinant MANF protein protects tissue from ischemic brain injury. MANF has been described as a survival factor for dopaminergic neurons. MANF and a homologous protein, the conserved dopamine neurotrophic factor (CDNF), form a novel evolutionary conserved family of neurotrophic factors. MANF expression was widespread in the nervous system and non-neuronal tissues.
MANSC domain-containing protein 1(MANSC1) is encoded by MANSC1 gene. MANSC1 is a Single-pass type I membrane protein which contains 1 MANSC domain. It is widely expressed in many tissues and mainly located in membrane.
Methionine aminopeptidase 1D, also known as MAP1D, is a member of thepeptidase M24A family. N-terminal methionine removal is an important cellular process required for proper biological activity, subcellular localization, and eventual degradation of many proteins. The enzymes that catalyze this reaction are called Methionine aminopeptidases (MAPs). MAP1D is overexpressed in colon cancer cell lines and colon tumors as compared to normal tissues (at protein level). Downregulation of MAP1D expression by shRNA in HCT-116 colon carcinoma cells reduces anchorage-independant growth in soft agar. MAP1D binds two cobalt ions per subunit. The true nature of the physiological cofactor is under debate. MAP1D is also active with zinc, manganese or divalent ions. MAP1D removes the amino-terminal methionine from nascent proteins. It may also play an important role in colon tumorigenesis.
Methionine Aminopeptidase 1D (METAP1D) is a mitochondrion protein that belongs to the peptidase M24A family. METAP1D is overexpressed at the protein level in colon cancer cell lines and colon tumors as compared to normal tissues. N-terminal methionine removal is an important cellular process required for proper biological activity, subcellular localization, and eventual degradation of many proteins. METAP1D is also active with zinc, manganese or divalent ions. It may also play an important role in colon tumorigenesis.
Microtubule-Associated Proteins 1A/1B Light Chain 3A (MAP1LC3A) belongs to the MAP1 LC3 family. MAP1LC3A is found most abundantly in the heart, brain, liver, skeletal muscle, and testis. But it is absent in the thymus and peripheral blood leukocytes. MAP1LC3A is thought to take part in the formation of autophagosomal vacuoles and is one of the light chain subunits that functions together with both MAP1A and/or MAP1B. In addition, MAP1A has an important part in neuronal development and in maintaining the balance between neuronal plasticity and rigidity.
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