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Molecular cloning of the α‐subunit of rat endopeptidase‐24.18 (endopeptidase‐2) and co‐localization with endopeptidase‐24.11 in rat kidney by in situ hybridization
Author(s) -
Corbeil Denis,
Gaudoux Florence,
Wainwright Sandra,
Ingram Jean,
Kenny A.John,
Boileau Guy,
Crine Philippe
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81095-4
Subject(s) - endopeptidase , neprilysin , in situ hybridization , chemistry , cloning (programming) , microbiology and biotechnology , protein subunit , in situ , prolyl endopeptidase , biochemistry , biology , enzyme , gene , gene expression , computer science , organic chemistry , programming language
Endopeptidase‐24.18 (endopeptidase‐2, EC 3.4.24.18, E‐24.18) is a Zn‐ectoenzyme of rat renal and intestinal microvillar membranes exhibiting an oligometric structure, α 2 ‐β 2 . The primary structure of the α‐subunit of E‐24.18 has been defined by molecular cloning and its expression mapped in rat kidney by in situ hybridization. A 2.9‐kb cDNA coding for the α‐subunit was isolated and sequenced. It had an open reading frame of 2.244 base pairs coding for a type I membrane protein of 748 amino acids. The deduced amino acid sequence showed 87% identity with that of meprin A, a mouse metallo‐endopeptidase, sharing common properties with the rat enzyme, and 85% identity with the human intestinal enzyme, ‘PABA‐peptide hydrolase’. Northern blot analysis revealed the α‐subunit to be encoded by a single mRNA species of 3.2‐kb. In situ hybridization performed on rat kidney showed a co‐localization of E‐24.18 with endopeptidase‐24.11 in proximal tubules of juxtamedullary nephrons, suggesting that the two enzymes have similar or complementary physiological functions in kidney.