Biology:MEP1A
From HandWiki
 Generic protein structure example |
Meprin A subunit alpha also known as endopeptidase-2 or PABA peptide hydrolase is the alpha subunit of the meprin A enzyme that in humans is encoded by the MEP1A gene.[1][2] The MEP1A locus is on chromosome 6p in humans and on chromosome 17 in mice.[3]
Function
The meprin alpha subunit product of the MEP1A gene is processed in the endoplasmic reticulum during intracellular transport, and is secreted as homomeric meprin A. Meprin alpha subunits may self-associate, and once secreted, form very large multimers, with a molecular mass of over 1 million daltons. In cells concurrently expressing MEP1B, the meprin alpha and meprin beta subunits form disulfide dimers that interact to form membrane bound heterotetrameric meprin A.
References
- ↑ "The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively". Genomics 25 (1): 300–3. Jul 1995. doi:10.1016/0888-7543(95)80142-9. PMID 7774936.
- ↑ "Entrez Gene: MEP1A meprin A, alpha (PABA peptide hydrolase)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4224.
- ↑ "MEP1A allele for meprin A metalloprotease is a susceptibility gene for inflammatory bowel disease". Mucosal Immunol 2 (3): 220–31. May 2009. doi:10.1038/mi.2009.3. PMID 19262505.
Further reading
- "The astacin family of metalloendopeptidases". J. Biol. Chem. 266 (32): 21381–5. 1991. PMID 1939172.
- "Action of rat liver cathepsin L on glucagon". Acta Biol. Med. Ger. 40 (9): 1139–43. 1982. PMID 7340337.
- "An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin". J. Cell Biol. 126 (5): 1319–27. 1994. doi:10.1083/jcb.126.5.1319. PMID 8063866.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells". FEBS Lett. 335 (3): 367–75. 1994. doi:10.1016/0014-5793(93)80421-P. PMID 8262185.
- "Expression and distribution of meprin protease subunits in mouse intestine". Arch. Biochem. Biophys. 331 (1): 87–94. 1996. doi:10.1006/abbi.1996.0286. PMID 8660687.
- "Identification of the cysteine residues implicated in the formation of alpha 2 and alpha/beta dimers of rat meprin". Biochem. J. 317 (Pt 3): 731–8. 1996. doi:10.1042/bj3170731. PMID 8760356.
- "Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells". Eur. J. Biochem. 247 (3): 920–32. 1997. doi:10.1111/j.1432-1033.1997.00920.x. PMID 9288916.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits". Eur. J. Biochem. 259 (1–2): 496–504. 1999. doi:10.1046/j.1432-1327.1999.00071.x. PMID 9914532.
- "Composition of the peptide fraction in human blood plasma: database of circulating human peptides". J. Chromatogr. B 726 (1–2): 25–35. 1999. doi:10.1016/S0378-4347(99)00012-2. PMID 10348167.
- "Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro". FEBS Lett. 465 (1): 2–7. 2000. doi:10.1016/S0014-5793(99)01712-3. PMID 10620696.
- "Structure and expression of the human MEP1A gene encoding the alpha subunit of metalloendopeptidase meprin A". Arch. Biochem. Biophys. 379 (2): 183–7. 2000. doi:10.1006/abbi.2000.1873. PMID 10898933.
- "Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning". Biochim. Biophys. Acta 1518 (1–2): 106–14. 2001. doi:10.1016/S0167-4781(01)00188-9. PMID 11267665.
- "Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity". J. Biol. Chem. 276 (16): 13248–55. 2001. doi:10.1074/jbc.M011414200. PMID 11278902.
- "Multimeric structure of the secreted meprin A metalloproteinase and characterization of the functional protomer". J. Biol. Chem. 276 (25): 23207–11. 2001. doi:10.1074/jbc.M102654200. PMID 11301339.
- "Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system". J. Biol. Chem. 277 (43): 40650–8. 2002. doi:10.1074/jbc.M206203200. PMID 12189145.
- "Targeted Disruption of the Meprin β Gene in Mice Leads to Underrepresentation of Knockout Mice and Changes in Renal Gene Expression Profiles". Mol. Cell. Biol. 23 (4): 1221–30. 2003. doi:10.1128/MCB.23.4.1221-1230.2003. PMID 12556482.
- "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. 2006. doi:10.1101/gr.4039406. PMID 16344560.
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