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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
28
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pubmed:dateCreated |
1993-11-24
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pubmed:databankReference | |
pubmed:abstractText |
Meprins are plasma membrane homo- or hetero-oligomeric metalloendopeptidases that contain glycosylated alpha and/or beta subunits. This paper reports the cloning and sequencing of the mouse kidney beta subunit. The primary translation product is composed of 704 amino acids which includes a transient signal sequence of 20 amino acids at the NH2 terminus. The protease domain (Asn-63 to Leu-260) contains the putative zinc-binding motif characteristic of metalloendopeptidases of the "astacin family." The COOH terminus contains an epidermal growth factor-like domain, a potential membrane-spanning domain, and an additional 26 amino acids. The beta subunit has an overall 42% identity to the alpha subunit, however, a 56-amino acid segment near the COOH terminus of alpha is missing in beta, and the putative transmembrane and cytoplasmic domains of the subunits share no significant sequence similarity. NH2-terminal analyses of detergent-solubilized mature forms revealed that, unlike alpha, the prosequence (Leu-21 to Lys-62) is not removed from the beta subunit. Northern blot analysis revealed a 2.5-kilobase message for the beta subunit in the kidney and intestine of C57BL/6 and C3H/He mice. The gene for the beta subunit was localized to mouse chromosome 18. These studies indicate that alpha and beta probably derived from a common ancestral gene, but have evolved so that their genes are on two different chromosomes, and their tissue-specific expression and post-translational processing differ.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
268
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pubmed:geneSymbol |
Mep-1&bgr;
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21035-43
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8407940-Amino Acid Sequence,
pubmed-meshheading:8407940-Animals,
pubmed-meshheading:8407940-Base Sequence,
pubmed-meshheading:8407940-Chromosome Mapping,
pubmed-meshheading:8407940-Cloning, Molecular,
pubmed-meshheading:8407940-DNA, Complementary,
pubmed-meshheading:8407940-Genes,
pubmed-meshheading:8407940-Male,
pubmed-meshheading:8407940-Mice,
pubmed-meshheading:8407940-Mice, Inbred C3H,
pubmed-meshheading:8407940-Mice, Inbred C57BL,
pubmed-meshheading:8407940-Molecular Sequence Data,
pubmed-meshheading:8407940-Protein Conformation,
pubmed-meshheading:8407940-Sequence Homology, Amino Acid,
pubmed-meshheading:8407940-Tiopronin
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pubmed:year |
1993
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pubmed:articleTitle |
Cloning, expression, and chromosomal localization of the mouse meprin beta subunit.
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pubmed:affiliation |
Department of Biological Chemistry, Pennsylvania State University College of Medicine, Hershey 17033.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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