Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning (Q28206608)

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scientific article (publication date: 19 March 2001)

Language	Label	Description	Also known as
English	Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning	scientific article (publication date: 19 March 2001)

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scholarly article

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Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning (English)

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author name string

J M Kumar

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J S Bond

2

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language of work or name

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publication date

19 March 2001

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Biochimica et Biophysica Acta

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1518

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1-2

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106-14

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The astacin family of metalloendopeptidases

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Distribution of meprin in kidneys from mice with high- and low-meprin activity

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Proteins of the kidney microvillar membrane. Structural and immunochemical properties of rat endopeptidase-2 and its immunohistochemical localization in tissues of rat and mouse

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N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides.

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Meprin mRNA in rat intestine during normal and glucocorticoid-induced maturation: divergent patterns of expression of alpha and beta subunits

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Meprins A and B.

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Unveiling the substrate specificity of meprin beta on the basis of the site in protein kinase A cleaved by the kinase splitting membranal proteinase

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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

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Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro

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Meprin: a membrane-bound metallo-endopeptidase.

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The role of meprin A in the pathogenesis of acute renal failure

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The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively

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Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits

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Expression and distribution of meprin protease subunits in mouse intestine

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10.1016/S0167-4781(01)00188-9

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