Purification, molecular cloning, and immunohistochemical localization of dipeptidyl peptidase II from the rat kidney and its identity with quiescent cell proline dipeptidase

被引:25
作者
Araki, H
Li, YH
Yamamoto, Y
Haneda, M
Nishi, K
Kikkawa, R
Ohkubo, I [1 ]
机构
[1] Shiga Univ Med Sci, Dept Biochem Med, Shiga 5202192, Japan
[2] Shiga Univ Med Sci, Dept Legal Med, Shiga 5202192, Japan
[3] Shiga Univ Med Sci, Dept Internal Med, Shiga 5202192, Japan
关键词
cDNA and identification; dipeptidyl peptidase II (DPP II); quiescent cell proline dipeptidase (QPP); rat kidney;
D O I
10.1093/oxfordjournals.jbchem.a002855
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 to QPP. 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.
引用
收藏
页码:279 / 288
页数:10
相关论文
共 29 条
  • [1] DIPEPTIDYL PEPTIDASES IN BOVINE REPRODUCTIVE-ORGANS AND SECRETIONS
    AGRAWAL, Y
    VANHAPERTTULA, T
    [J]. INTERNATIONAL JOURNAL OF ANDROLOGY, 1986, 9 (06): : 435 - 452
  • [2] ANDERSEN KJ, 1989, RENAL PHYSIOL BIOCH, V12, P32
  • [3] Chiravuri M, 2000, J BIOL CHEM, V275, P26994
  • [4] Chiravuri M, 1999, J IMMUNOL, V163, P3092
  • [5] EISENHAUER DA, 1986, J BIOL CHEM, V261, P8859
  • [6] PURIFICATION AND PROPERTIES OF DIPEPTIDYL PEPTIDASE-II FROM RAT-KIDNEY
    FUKASAWA, K
    FUKASAWA, KM
    HIRAOKA, BY
    HARADA, M
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1983, 745 (01) : 6 - 11
  • [7] STUDY ON DIPEPTIDYLPEPTIDASE-II (DPP-II)
    GOSSRAU, R
    LOJDA, Z
    [J]. HISTOCHEMISTRY, 1980, 70 (01) : 53 - 76
  • [8] Dipeptidyl peptidase II from porcine seminal plasma: Purification, characterization, and its homology to granzymes, cytotoxic cell proteinases (CCP 1-4)
    Huang, K
    Takagaki, M
    Kani, K
    Ohkubo, I
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1996, 1290 (02): : 149 - 156
  • [9] Huang K, 1997, J BIOCHEM, V122, P779
  • [10] COMPARATIVE CYTOCHEMICAL STUDY OF DIPEPTIDYL AMINOPEPTIDASE (DAP)-II AND (DAP)-IV IN NORMAL AND MALIGNANT HEMIC CELLS
    KHALAF, MR
    BEVAN, PC
    HAYHOE, FGJ
    [J]. JOURNAL OF CLINICAL PATHOLOGY, 1986, 39 (08) : 891 - 896