Neurexin-3-beta; also known as Neurexin III-beta and NRXN3; is a single-pass type I membrane protein which belongs to theneurexin family. It contains onelaminin G-like domain. It is a neuronal cell surface protein that may be involved in cell recognition and cell adhesion. Neurexins are a family of proteins that function in the vertebrate nervous system as cell adhesion molecules and receptors. They are encoded by several unlinked genes of which two; NRXN1 and NRXN3; are among the largest known human genes. Three of the genes ( NRXN1; NRXN2; NRXN3 ) utilize two alternate promoters and include numerous alternatively spliced exons to generate thousands of distinct mRNA transcripts and protein isoforms. The majority of transcripts are produced from the upstream promoter and encode alpha-neurexin isoforms; a much smaller number of transcripts are produced from the downstream promoter and encode beta-neurexin isoforms. The alpha-neurexins contain EGF-like sequences and laminin G domains; and have been shown to interact with neurexophilins. The beta-neurexins lack EGF-like sequences and contain fewer laminin G domains than alpha-neurexins. NRXN3 have been linked to genetic predisposition towards a number of conditions such as alcohol or drug addiction; or obesity.
Gamma-enolase; also known as Enolase 2; belongs to the enolase family. The alpha/alpha homodimer of ENO2 is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle; and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. During ontogenesis; there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells; and to the alpha/gamma heterodimer in nerve cells. Levels of ENO2 increase dramatically in cardiovascular accidents; cerebral trauma; brain tumors and Creutzfeldt-Jakob disease. ENO2 has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. It binds to cultured neocortical neurons and promotes cell survival in a calcium-dependent manner.
NTPDase 2, also known as ENTPD2, belongs to the ecto-nucleoside triphosphate diphosphohydrolase family (E-NTPDase). Members of E-NTPDase family are nucleotidases able to hydrolyze 5′-nucleoside tri- and/or diphosphates; the main role of these enzymes is the termination of purinergic signaling. NTPDases are ubiquitous and were previously shown in other parasites including the trypanosomatides of genus Leishmania and in T. brucei. NTPase activity would act as a timer and is crucial to T. gondii infection. In L. pneumophila it was demonstrated that an E-NTPDase, similar to CD39, is essential for intracellular bacterial multiplication. NTPDase 2 is an integral membrane protein. In the nervous system, it could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Alternative splicing of NTPDase 2 gene results in multiple transcript variants.
DPEP2 (MBD-2) belongs to the membrane-bound dipeptidase family. There are three members of this family as membrane-bound dipeptidase-1 (MBD-1),membrane-bound dipeptidase-2 (MBD-2) and membrane-bound dipeptidase-3 (MBD-3).MBD-2 is expressed at highest levels in lung, heart, and testis and at some what lower levels in spleen.MBD-2 is membrane-bound through a glycosylphosphatidyl-inositol linkage and probably is a metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4).It is generally recognized that rapid cleavage of LTD4 is important in inactivating the broncho-and vaso-constrictive effects of cysteinyl LTs in asthmatic and inflammatory processes.
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