<b>A specific tripeptidyl substrate for tripeptidyl peptidase activity is effectively hydrolyzed by alanyl aminopeptidase/</b><b>aminopeptidase N/CD13 in the rat kidney </b>

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Author(s)

    • Shibata Masahiro
    • Department of Morphological Sciences, Kagoshima University Graduate School of Medical and Dental Sciences,
    • Koike Masato
    • Department of<sup> </sup>Cell Biology and Neuroscience, Juntendo University Graduate School of Medicine,
    • Kusumi Satoshi
    • Department of Morphological Sciences, Kagoshima University Graduate School of Medical and Dental Sciences,
    • Sato Noboru
    • Division of Gross Anatomy and Morphogenesis,Department of Regenerative and Transplant Medicine,Niigata University Graduate School of Medical and Dental Sciences,
    • Uchiyama Yasuo
    • Department of Cellular and Molecular Neuropathology, Juntendo University Graduate School of Medicine,

Abstract

<b>L-Alanyl-L-alanyl-L-phenylalanine 4-methylcoumaryl-7-amide (AAF-MCA) is one of the classic substrates for use with tripeptidyl peptidases (TPP-I and TPP-II). We have previously clarified the tissue distribution of TPP-I in detail and noted that the protein expression of TPP-I is often incompatible with its enzyme activity. Herein, we describe the unknown peptidase, which could effectively hydrolyze AAF-MCA, in the rat kidney. The peptidase was purified after four chromatography steps, and its enzyme characteristics were elucidated. The peptidase activity was inhibited by amastatin, bestatin, and o-phenanthroline and was also inhibited by zinc and copper ions. The substrate specificity for several monoamino acidic-MCAs revealed that the peptidase had an affinity for alanyl-MCA. Th</b><b>e </b><b>amino terminal amino acid sequence of the peptidase was x-Ala-Pro-x-Leu-Pro-Gly-Ser-Thr-Ser-Ala-Thr-x-x-Ser, where x indicates undetectable amino acid residues, and the antiserum against the peptidase was immunopositive for the brush border of a renal proximal tubule and the small intestine, and the surface membrane of bile canaliculi. These results indicate that the unknown peptidase that hydrolyzed AAF-MCA is the soluble form of aminopeptidase N/CD13, and caution is required when using AAF-MCA as a substrate for tripeptidyl peptidase </b><b>assays.</b>

Journal

  • Archives of Histology and Cytology

    Archives of Histology and Cytology 76(1), 1-8, 2016

    International Society of Histology and Cytology

Codes

  • NII Article ID (NAID)
    130005131324
  • Text Lang
    ENG
  • ISSN
    0914-9465
  • Data Source
    J-STAGE 
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