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.
MARCO (macrophage receptor with collagenous structure) is an 80 kDa type II transmembrane glycoprotein that belongs to the class Ascavenger receptor family. Mouse MARCO consists of a 48 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 449 aa extracellulardomain (ECD) that includes a stalk region, a collagenlikeregion, and one SRCR domain. MARCO is constitutively expressed on the surface of splenic and lymph node macrophages. MARCO binds LPS, lipoteichoic acid, and otherdeterminants on Gram positive and Gram negative bacteria. It also binds modified LDL, CpG oligonucleotides, UGRP1, silica, and TiO2.
MBL (mannose-binding lectin) is primarily a liver-derived collagen-like serum protein, which binds sugar structures on micro-organisms and on dying host cells and is one of the four known mediators that initiate activation of the complement system via the lectin pathway. MBL and the ficolins (Ficolin-1, Ficolin-2 and Ficolin-3) are soluble collagen-like proteins that are involved in innate immune defence. They bind sugar structures or acetylated compounds present on microorganisms and on dying host cells and they initiate activation of the lectin complement pathway in varying degrees. MBL2 encodes the mannose-binding lectin, which is a key player in the innate immune system and has recently been found to play a role in development of type 1 diabetes and gestational diabetes mellitus. Common variant alleles situated both in promoter and structural regions of the MBL2 gene influence the stability and the serum concentration of the protein. Several polymorphisms in the promoter and structural regions of MBL2 adversely affect the plasma concentration and oligomeric state of MBL. The possession of mutant alleles has been linked to disease outcome for a variety of bacterial and viral infections. Mutant MBL2 haplotypes have been linked to disease progression and response to therapy in HCV infection.
Mannose-binding Lectin (MBL) is an acute phase protein bearing to the family of collectins produced by the liver as a monomer that forms a triple helix. Once released in serum, it further polymerizes forming dimers to octamers. The degree of serum polymerization is critical for the biological activity of MBL. MBL has higher affinity to microbial polysaccharides or their glycoconjugates. MBL was shown earlier to bind cell surfaces of bacteria, fungi, protozoa and viruses and acts as an acute-phase plasma protein (APP) during infection and inflammation. MBL activates the lectin-complement pathway, promotes opsonophagocytosis and modulates inflammation.
Monocyte chemoattractant protein 1(CCL2/JE/MCP-1), also called CCL2, belongs to a group of CC chemokines located in chromosome 17q11.2. CCL2/JE/MCP-1 protein interacts with chemokine C-C motif receptor 2(CCR2) to activate and recruit monocytes, macrophages, CD4+ T cells and immature dendritic cells to the site of infection. The presence of CCL2/JE/MCP-1 protein in an adequate concentration is important for granuloma formation and M. tuberculosis clearance.
Mast Cell Protease 1 (MMCP-1), also known as MCP-1, MCPT-1 and β-chymase, is a member of the Chymase family of chymotrypsin-like serine proteases. MCPT-1 is a 26 kDa β-chymase that is a component of mast cell granules. It is a 226 amino acid (aa) protein that has a conserved pattern of six cysteines and one potential glycosylation site. The granule-derived mouse mast cell proteases-1 and -2 (mMCP-1 and -2) colocalize in similar quantities in mucosal mast cells but micrograms of mMCP-1 compared with nanograms of mMCP-2 are detected in peripheral blood during intestinal nematode infection. mMCP-1 isolated from serum is complexed with serpins and both the accumulation and the longevity of mMCP-1 in blood is due to complex formation, protecting it from a pathway that rapidly clears mMCP-2, which is unable to form complexes with serpins. Expression of mMCP-1 is largely restricted to intraepithelial MMC and is thought to play a role in the regulation of epithelial permeability. Its activation is completed by the removal of a two residue N-terminal propeptide by a dipeptidyl peptidase (Cathepsin C). MCPT-1 is upregulated in the intestine in response to nematode infection, or in systemic mucosa in response to anaphylaxis. Like human α-chymase, MCPT-1 is capable of the conversion of angiotensin I to angiotensin II, which plays a key role in the regulation of arterial pressure. The intestinal inflammation associated with gastrointestinal helminths is partly mediated by mMCP-1.
Tryptase beta-2(Tpsb2), also known as Mast cell protease 6(mMCP-6), belongs to the peptidase S1 family and Tryptase subfamily. Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. It plays a role in innate immunity. Tpsb2 can be detected primarily in skin during embryogenesis. Tpsb2 can not be detected at early embryonic stages but is abundantly expressed in later stages with a peak at E17.5-E18.5. Tryptase is a homotetramer. The active tetramer is converted to inactive monomers at neutral and acidic pH in the absence of heparin. Low concentrations of inactive monomers become active monomers at pH 6.0 in the presence of heparin. When the concentration of active monomers is higher, they convert to active monomers and then to active tetramers. These monomers are active and functionally distinct from the tetrameric enzyme. In contrast to the hidden active sites in the tetrameric form, the active site of the monomeric form is accessible for macromolecular proteins and inhibitors eg: fibrinogen which is a substrate for the monomeric but not for the tetrameric form. The monomeric form forms a complex with SERPINB6.
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