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Czasopismo

2006 | 65 | 2 |

Tytuł artykułu

The activity and immunoexpression of cathepsin D in rat male reproductive organs

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Cathepsin D is a cysteine endopeptidase that belongs to the lysosomal enzyme family. The aim of the study was to evaluate the enzyme immunoexpression and activity in selected male genital organs in mature Wistar rats. The activity of cathepsin D was measured spectrophotometrically in homogenates of the testis, epididymis, seminal vesicle and prostate. Immunohistochemical staining was also performed in the ductus deferens. Enzyme activity was found in the following sequence: testis>epididymis>dorsal prostatic lobe>seminal vesicle>lateral prostatic lobe>ventral prostatic lobe. Although there were differences in enzyme activity between various organs of the male reproductive system, cathepsin D immunoreactivity was seen exclusively in the Sertoli and Leydig cells in the testis.

Wydawca

-

Czasopismo

Rocznik

Tom

65

Numer

2

Opis fizyczny

p.111-115,fig.,ref.

Twórcy

autor
  • Medical University of Lublin, Lublin, Poland
autor
autor
autor
autor

Bibliografia

  • 1. Adamali HI, Somani IH, Huang JQ, Gravel RA, Trasler JM, Hermo L (1999) Characterization and development of the regional- and cellular-specific abnormalities in the epididymis of mice with beta-hexosaminidase A deficiency. J Androl, 20: 803–824.
  • 2. Andonian S, Hermo L (1999) Cell- and region-specific localization of lysosomal and secretory proteins and endocytic receptors in epithelial cells of the cauda epididymidis and vas deferens of the adult rat. J Androl, 20: 415–429.
  • 3. Augereau P, Garcia M, Mattei MG, Cavailles V, Depadova F, Derocq D, Capony F, Ferrara P, Rochefort H (1988) Cloning and sequencing of the 52K cathepsin D complementary deoxyribonucleic acid of MCF7 breast cancer cells and mapping on chromosome 11. Mol Endocrinol, 2: 186–192.
  • 4. Burdan F, Siezieniewska Z, Maciejewski R, Burski K, Wojtowicz Z (2000) Temporary elevation of pancreatic lysosomal enzymes, as a result of the omeprazole-induced peripancreatic inflammation in male Wistar rats. J Physiol Pharmacol, 51: 463–470.
  • 5. Burdan F, Siezieniewska Z, Maciejewski R, Madej B, Radzikowska E, Wojtowicz Z (2002) Hepatic lysosomal enzymes activity and liver morphology after short-time omeprazole administration. Exp Toxicol Pathol, 53: 453–459.
  • 6. Burdan F, Szumilo J, Korobowicz A, Dudka J, Korobowicz E, Wallner G, Maciejewski R (2003) Biochemical and immunohistochemical study on physiological activity and distribution of hepatic cathepsin D. Acta Physiol Hung, 90: 47–56.
  • 7. Faust PL, Kornfeld S, Chirgwin JM (1985) Cloning and sequence analysis of cDNA for human cathepsin D. Proc Natl Acad Sci USA, 82: 4910–4914.
  • 8. Fouchecourt S, Metayer S, Locatelli A, Dacheux F, Dacheux JL (2000) Stallion epididymal fluid proteome: qualitative and quantitative characterization; secretion and dynamic changes of major proteins. Biol Reprod, 62: 1790–1803.
  • 9. Hermo L, Andonian S (2003) Regulation of sulfated glycoprotein-1 and cathepsin D expression in adult rat epididymis. J Androl, 24: 408–422.
  • 10. Igdoura SA, Morales CR, Hermo L (1995) Differential expression of cathepsins B and D in testis and epididymis of adult rats. J Histochem Cytochem, 43: 545–557.
  • 11. Islam AH, Kato H, Nishizawa O, Hayama M (2002) Distribution of cathepsin D granules in normal and pathologic conditions in human prostate. Hinyokika Kiyo, 48: 647–652.
  • 12. Lee C, Sensibar JA, Dudek SM, Hiipakka RA, Liao ST (1990) Prostatic ductal system in rats: regional variation in morphological and functional activities. Biol Reprod, 43: 1079–1086.
  • 13. Mathur PP, Grima J, Mo MY, Zhu LJ, Aravindan GR, Calcagno K, O’Bryan M, Chung S, Mruk D, Lee WM, Silvestrini B, Cheng CY (1997) Differential expression of multiple cathepsin mRNAs in the rat testis during maturation and following lonidamine induced tissue restructuring. Biochem Mol Biol Int, 42: 217–233.
  • 14. Morikawa W, Yamamoto K, Ishikawa S, Takemoto S, Ono M, Fukushi J, Naito S, Nozaki C, Iwanaga S, Kuwano M (2000) Angiostatin generation by cathepsin D secreted by human prostate carcinoma cells. J Biol Chem, 275: 38912–38920.
  • 15. Nomura T, Katunuma N (2005) Involvement of cathepsins in the invasion, metastasis and proliferation of cancer cells. J Med Invest, 52: 1–9.
  • 16. Raczek S, Yeung CH, Hasilik A, Robenek H, Hertle L, Schulze H, Cooper TG (1995) Immunocytochemical localisation of some lysosomal hydrolases, their presence in luminal fluid and their directional secretion by human epididymal cells in culture. Cell Tissue Res, 280: 415–425.
  • 17. Sakai H, Saku T, Kato Y, Yamamoto K (1989) Quantitation and immunohistochemical localization of cathepsins E and D in rat tissues and blood cells. Biochim Biophys Acta, 991: 367–375.
  • 18. Sensibar JA, Liu XX, Patai B, Alger B, Lee C (1990) Characterization of castration-induced cell death in the rat prostate by immunohistochemical localization of cathepsin D. Prostate, 16: 263–276.
  • 19. Shewale JG, Tang J (1984) Amino acid sequence of porcine spleen cathepsin D. Proc Natl Acad Sci USA, 81: 3703–3707.
  • 20. Stroev EA, Dmitriev AV (1987) Hormonal aspects of cathepsin D regulation in seminal follicles. Vopr Med Khim, 33: 107–112.
  • 21. Wang F, Duan R, Chirgwin J, Safe SH (2000) Transcriptional activation of cathepsin D gene expression by growth factors. J Mol Endocrinol, 24: 193–202.
  • 22. Wilson MJ, Whitaker JN, Sinha AA (1991) Immunocytochemical localization of cathepsin D in rat ventral prostate: evidence for castration-induced expression of cathepsin D in basal cells. Anat Rec, 229: 321–333.

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Bibliografia

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