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Gene Review

Mep1a  -  meprin 1 alpha

Mus musculus

Synonyms: AI098089, AW107200, Endopeptidase-2, MEP-1, Mep-1, ...
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Disease relevance of Mep1a

  • Thus, disruption of the meprin beta allele in mice affects embryonic viability, birth weight, renal gene expression profiles, and the distribution of meprin alpha in kidney and intestine [1].
  • Meprin-alpha in chronic diabetic nephropathy: interaction with the renin-angiotensin axis [2].
  • In the primary rat tumors and transplanted rat or nude mouse tumors, MEP-1 reacted specifically with the fibroblastlike cells but not with the histiocytelike cells or xanthoma cells [3].
  • Immunological properties of a model polyepitope immunogen (MEP-1) consisting of selected determinants from envelope proteins of hepatitis B virus (HBV) were examined [4].
  • The binding of a mouse monoclonal antibody (MEP-1) reacting specifically with type I pneumocytes was assessed on paraffin sections of normal specimens as well as those with pulmonary fibrosis induced by bleomycin or radiation treatment [5].

High impact information on Mep1a


Biological context of Mep1a


Anatomical context of Mep1a

  • The meprin alpha subunit, a multidomain metalloproteinase, is synthesized as a type I membrane protein and proteolytically cleaved during biosynthesis in the endoplasmic reticulum (ER), consequently losing its membrane attachment and COOH-terminal domains [11].
  • The 3.6-kilobase mRNA meprin alpha subunit message was also detected in the small intestine of the rat but not in mice [12].
  • The present work shows that reducing agents solubilized meprin alpha subunits (approximately 90%), but not beta subunits, from mouse kidney brush border membranes [13].
  • These studies show that meprin alpha and beta are expressed in leukocytes of the mouse mesenteric lymph node, and meprin alpha, but not beta, decreased during intestinal inflammation [14].
  • The work herein, however, reports that low levels of meprin alpha subunit mRNA and protein are detectable in mouse intestine and are present in increasing concentrations from the duodenum to the ileum [15].

Associations of Mep1a with chemical compounds

  • Western blotting with antisera specific to the meprin-alpha and the meprin-beta subunits established that the only form of meprin present in urine samples was derived from meprin-alpha [16].
  • In addition, another proposed zinc binding ligand, H167, in the conserved (HEXXH) zinc binding motif of the meprin alpha protease domain was replaced by an alanine residue [17].
  • However, all changes in meprin alpha subunit NH2-terminal structure were found to decrease the thermal stability of the enzyme [18].
  • The alpha(1-528) mutant was as active as wild-type meprin alpha against a bradykinin substrate, but had no activity against azocasein, and it, as all other mutants, was more vulnerable to extensive degradation by proteases than the wild-type protein [19].
  • These results indicate that there is no one specific glycosylation site or type of oligosaccharide (high mannose- or complex-type) that determines apical sorting, but that core N-linked carbohydrates are required for optimal enzymatic activity and for secretion of meprin alpha [20].

Physical interactions of Mep1a


Other interactions of Mep1a


Analytical, diagnostic and therapeutic context of Mep1a


  1. Targeted disruption of the meprin beta gene in mice leads to underrepresentation of knockout mice and changes in renal gene expression profiles. Norman, L.P., Jiang, W., Han, X., Saunders, T.L., Bond, J.S. Mol. Cell. Biol. (2003) [Pubmed]
  2. Meprin-alpha in chronic diabetic nephropathy: interaction with the renin-angiotensin axis. Mathew, R., Futterweit, S., Valderrama, E., Tarectecan, A.A., Bylander, J.E., Bond, J.S., Trachtman, H. Am. J. Physiol. Renal Physiol. (2005) [Pubmed]
  3. Immunohistochemical, quantitative immunoelectron microscopic, and DNA cytofluorometric characterization of chemically induced rat malignant fibrous histiocytoma. Tsuchiya, T., Takahashi, K., Takeya, M., Hosokawa, Y., Hattori, T., Takagi, K. Am. J. Pathol. (1993) [Pubmed]
  4. Immunological characteristics of a recombinant hepatitis B virus-derived multiple-epitope polypeptide: a study in polyvalent vaccine design. Kumar, A., Kumar, V., Shukla, G.C., Rao, K.V. Vaccine (1994) [Pubmed]
  5. Immunohistochemistry of new type I alveolar epithelial cell markers of the rat. Kasper, M., Takeya, M., Takahashi, K., Grossmann, H., Schuh, D., Müller, M. Histol. Histopathol. (1996) [Pubmed]
  6. Mep-1 gene controlling a kidney metalloendopeptidase is linked to the major histocompatibility complex in mice. Bond, J.S., Beynon, R.J., Reckelhoff, J.F., David, C.S. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  7. Mannan-binding protein blocks the activation of metalloproteases meprin alpha and beta. Hirano, M., Ma, B.Y., Kawasaki, N., Okimura, K., Baba, M., Nakagawa, T., Miwa, K., Kawasaki, N., Oka, S., Kawasaki, T. J. Immunol. (2005) [Pubmed]
  8. Proximity of the Mep-1 gene to H-2D on chromosome 17 in mice. Reckelhoff, J.F., Bond, J.S., Beynon, R.J., Savarirayan, S., David, C.S. Immunogenetics (1985) [Pubmed]
  9. Critical amino acids in the active site of meprin metalloproteinases for substrate and peptide bond specificity. Villa, J.P., Bertenshaw, G.P., Bond, J.S. J. Biol. Chem. (2003) [Pubmed]
  10. Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity. Bertenshaw, G.P., Turk, B.E., Hubbard, S.J., Matters, G.L., Bylander, J.E., Crisman, J.M., Cantley, L.C., Bond, J.S. J. Biol. Chem. (2001) [Pubmed]
  11. Transport of meprin subunits through the secretory pathway: role of the transmembrane and cytoplasmic domains and oligomerization. Hengst, J.A., Bond, J.S. J. Biol. Chem. (2004) [Pubmed]
  12. Tissue-specific expression and chromosomal localization of the alpha subunit of mouse meprin A. Jiang, W., Sadler, P.M., Jenkins, N.A., Gilbert, D.J., Copeland, N.G., Bond, J.S. J. Biol. Chem. (1993) [Pubmed]
  13. Membrane association and oligomeric organization of the alpha and beta subunits of mouse meprin A. Marchand, P., Tang, J., Bond, J.S. J. Biol. Chem. (1994) [Pubmed]
  14. Deletion of the mouse meprin beta metalloprotease gene diminishes the ability of leukocytes to disseminate through extracellular matrix. Crisman, J.M., Zhang, B., Norman, L.P., Bond, J.S. J. Immunol. (2004) [Pubmed]
  15. Expression and distribution of meprin protease subunits in mouse intestine. Bankus, J.M., Bond, J.S. Arch. Biochem. Biophys. (1996) [Pubmed]
  16. Characterization of the soluble, secreted form of urinary meprin. Beynon, R.J., Oliver, S., Robertson, D.H. Biochem. J. (1996) [Pubmed]
  17. Zinc ligands in an astacin family metalloprotease meprin A. Doll, B.A., Villa, J.P., Ishmael, F.T., Bond, J.S. Biol. Chem. (2002) [Pubmed]
  18. Activation mechanism of meprins, members of the astacin metalloendopeptidase family. Johnson, G.D., Bond, J.S. J. Biol. Chem. (1997) [Pubmed]
  19. Role of the COOH-terminal domains of meprin A in folding, secretion, and activity of the metalloendopeptidase. Tsukuba, T., Bond, J.S. J. Biol. Chem. (1998) [Pubmed]
  20. N-Linked oligosaccharides on the meprin A metalloprotease are important for secretion and enzymatic activity, but not for apical targeting. Kadowaki, T., Tsukuba, T., Bertenshaw, G.P., Bond, J.S. J. Biol. Chem. (2000) [Pubmed]
  21. Chaperone interactions of the metalloproteinase meprin A in the secretory or proteasomal-degradative pathway. Tsukuba, T., Kadowaki, T., Hengst, J.A., Bond, J.S. Arch. Biochem. Biophys. (2002) [Pubmed]
  22. A testis-specific gene Tpx-1 maps between Pgk-2 and Mep-1 on mouse chromosome 17. Kasahara, M., Passmore, H.C., Klein, J. Immunogenetics (1989) [Pubmed]
  23. Purification of mouse MEP-1, a nuclear protein which binds to the metal regulatory elements of genes encoding metallothionein. Labbé, S., Larouche, L., Mailhot, D., Séguin, C. Nucleic Acids Res. (1993) [Pubmed]
  24. Assignment of Mep 1a to mouse chromosome band 17C1-D1 by in situ hybridization. Jiang, W., Beatty, B.G. Cytogenet. Cell Genet. (1997) [Pubmed]
  25. Characterization of the mouse metal-regulatory-element-binding proteins, metal element protein-1 and metal regulatory transcription factor-1. Larochelle, O., Stewart, G., Moffatt, P., Tremblay, V., Séguin, C. Biochem. J. (2001) [Pubmed]
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