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Titolo:
Purification, molecular cloning, and immunohistochemical localization of dipeptidyl peptidase II from the rat kidney and its identity with quiescent cell proline dipeptidase
Autore:
Araki, H; Li, YH; Yamamoto, Y; Haneda, M; Nishi, K; Kikkawa, R; Ohkubo, I;
Indirizzi:
Shiga Univ Med Sci, Dept Biochem Med, Shiga 5202192, Japan Shiga Univ Med Sci Shiga Japan 5202192 Biochem Med, Shiga 5202192, Japan Shiga Univ Med Sci, Dept Legal Med, Shiga 5202192, Japan Shiga Univ Med Sci Shiga Japan 5202192 t Legal Med, Shiga 5202192, Japan Shiga Univ Med Sci, Dept Internal Med, Shiga 5202192, Japan Shiga Univ MedSci Shiga Japan 5202192 nternal Med, Shiga 5202192, Japan
Titolo Testata:
JOURNAL OF BIOCHEMISTRY
fascicolo: 2, volume: 129, anno: 2001,
pagine: 279 - 288
SICI:
0021-924X(200102)129:2<279:PMCAIL>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
LYSOSOMAL SERINE PROTEASE; PORCINE SEMINAL PLASMA; MALE GENITAL-TRACT; ALANYL AMINOPEPTIDASE; IV; SEQUENCE; PROTEINASES;
Keywords:
cDNA and identification; dipeptidyl peptidase II (DPP II); quiescent cell proline dipeptidase (QPP); rat kidney;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Ohkubo, I Shiga Univ Med Sci, Dept Biochem Med, Shiga 5202192, Japan ShigaUniv Med Sci Shiga Japan 5202192 d, Shiga 5202192, Japan
Citazione:
H. Araki et al., "Purification, molecular cloning, and immunohistochemical localization of dipeptidyl peptidase II from the rat kidney and its identity with quiescent cell proline dipeptidase", J BIOCHEM, 129(2), 2001, pp. 279-288

Abstract

We purified dipeptidyl peptidase II (DPP II) to homogeneity from rat kidney and determined its physicochemical properties, including its molecular weight, substrate specificity, and partial amino acid sequence. Furthermore, we screened a rat kidney cDNA library, isolated the DPP II cDNA and determined its structure. The cDNA was composed of 1,720 base pairs of nucleotides, and 500 amino acid residues were predicted from the coding region of cDNA. Human quiescent cell proline dipeptidase (QPP) cloned from T-cells is a 58-kDa glycoprotein existing as a homodimer formed with a leucine zipper motif. The levels of amino acid homology were 92.8% (rat DPP II vs, mouse QPP)and 78.9% (rat DPP II vs. human QPP), while those of nucleotide homology were 93.5% (rat DPP II vs. mouse QPP) and 79.4% (rat DPP II vs. human QPP). The predicted amino acid sequences of rat DPP II and human and mouse QPP possess eight cysteine residues and a leucine zipper motif at the same positions. The purified DPP II showed similar substrate specificity and optimal pH to those of QPP. Consequently, it was thought that DPP II is identical toQPP. Northern blot analysis with rat DPP II cDNA revealed prominent expression of DPP II mRNA in the kidney, and the order for expression was kidney >> testis greater than or equal to heart > brain greater than or equal to lung > spleen > skeletal muscle > liver. In parallel with Northern blot analysis, the DPP II antigen was detected by immunohistochemical staining in the cytosol of epithelial cells in the kidney, testis, uterus, and cerebrum.

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Documento generato il 30/11/20 alle ore 16:43:42