PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
1996 | 43 | 4 |

Tytuł artykułu

Cathepsin A activity of normal bovine ocular tissues and pathological human intraocular fluids

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Cathepsin A activity assayed with N-Cbz-Phe-Ala, N-Cbz-Glu-Tyr and N-Cbz- -Glu-Phe as substrates, was measured in fresh corneas, lenses, aqueous humor, vitreous humor and choroid plus retinal pigment epithelium taken from normal bovine eye balls and in human intraocular fluids from the eye balls in various ocular diseases (cataract, glaucoma, diabetes, intraocular tumors). Cathepsin A exhibited a pH optimum at 5.0 and showed the highest specificity towards N-Cbz-Phe-Ala as a substrate. In bovine ocular tissues high cathepsin A activity was found in the choroid plus retinal pigment epithelium and in cornea. The lens and the vitreous humor showed low enzyme activity and the aqueous humor none at all. In the human aqueous humor of the eye with cataract cathepsin A activity was more than three times higher then in the eye with choroid tumor. In human vitreous humor in absolute glaucoma the activity was twice as high as in melanoma and almost three times higher than in the case of lung metastatic tumor. Diabetes in glaucoma increased seven fold cathepsin A activity in the vitreous humor.

Wydawca

-

Rocznik

Tom

43

Numer

4

Opis fizyczny

p.687-692

Twórcy

  • Medical Academy of Bialystok, M.Sklodowskiej-Curie 24a, 15-276 Bialystok, Poland
autor

Bibliografia

  • 1. Hayasaka, S., Hara, 5., Takaku, Y. & Mizuno, K. (197S) Distribution and some properties of cathepsin B in the bovine eves. Exp. Eye Res. 26, 57-63.
  • 2 Yamada, T., Hara, S. & Tamai, M. (1990) Immu- nohistochemical localization of cathepsin D in ocular tissues. Invest. Ophthalmol. Vis. Sci. 31. 1217-1223.
  • 3. Hayasaka, S. & Hayasaka, I. (1978) The distri­bution and some properties of collagenolytic cathepsin in the bovine eye. Albrecht von Graefes Arch. Klin. Ophthalmol. 206,163-168.
  • 4. Schive, K. & Volden, G. (1982) Cathepsin B, cathepsin C and arylamidase in rabbit cornea. Acta Ophthalmol. 60,765-772.
  • 5. Sharma, K.K. & Kester, K. (1996) Peptide hydrolysis in lens: Role of leucine amino- peptidase, aminopeptidase 111, prolylo- ligopeptidase and acylpeplidehydrolase. Curr. Eye Res. 15,363-371.
  • 6. Sulochoma, K.N., Ramakrishnan, S. & Arunagiri, K. (1996) Purification and characte­rization of a new enzyme dipeptidase from human lens. Exp. Eye Res. 62,221-231.
  • 7. Miller, S.P., Arya, D.V. & Sirrastava, S.K. (1976) Studies of gamma-glutamyl transpeptidase in human ocular tissues. Exp. Eye Res. 22,329-334.
  • 8. Fini, M.E. & Girard, M.T. (1990) Expression of collagenolytic/gelatinolytic metalloproteinases by normal cornea. Invest. Ophthalmol. Vis. Sci. 31, 1779-1788.
  • 9. Plantner, J.J. & Drew, T.A. (1994) Polarized distribution of metalloproteinases in the bovine interphotoreceptor matrix. Exp. Eye Res. 59, 577-587.
  • 10. Sharma, K.K. & Ortwerth, B.J. (1986) Amino- peptidase III activity in normal and cataractous lenses. Curr. Eye Res. 5,378-380.
  • 11. Swanson, A.A., Davis, R.M. & McDonald, J.K. (1984) Dipeptydyl peptidase III of human cataractous lenses. Partial purification. Curr. Eye Res. 3,287-291.
  • 12. YVolariska, M. & Bakunowicz-Lazarczvk, A. (1992) Proteins of vitreous humor. IV. Proteo­lytic activity of pathological vitreous humor. Klin. Oczna 94,44-45, (in Polish).
  • 13. Rakoczy, P.E., Mann, K., Cavaney, D.M., Robertson,'!"., Papadimitreou, I. & Constable, I.J. (1994) Detection and possible functions of a cysteine protease involved in digestion of rod outer segments by retinal pigment epithelial cell. Invest. Ophthalmol. Vis. Sci. 35,4100-4108.
  • 14. Bakunowicz-Lazarczyk, A., Stankiewicz, A., Wolariska, M. & Wrobel, K. (1992) Proteolytic activity of the subretinal fluid. Klin. Oczna 94, 239-240, (in Polish).
  • 15. Fukuchi, I., Yue, B.Y.I.T., Sugar, I. & Lams, S. (1994) Lysosomal enzyme activities in conjunctival tissues of patients with keratoconus. Arch. Ophthalmol. 112,1368-1377.
  • 16. Reim, M., Bahrke, C., Kuckelkorn, R. & Kuwert, T. (1993) Investigation of enzyme activities in severe burns of the anterior eye segment. Al­brecht von Graefes Arch. Klin. Exp. Ophthalmol. 231, 308-312.
  • 17. Luna, A., Jimenez-Rios, G. & Villanueva, E. (1985) Aminopeptidase and cathepsin Aactivitv in vitreous humor in relation to cause of death. iorcnsic Sci. Int. 29,171-178.
  • 18. Moss, S.E., Klein, R. & Klein, B.E.K. (1988) The incidence of vision loss in a diabetic population. Ophthalmology 95,1340-1348.
  • 19. Caprioli, J. (1992) Discrimination between normal and glaucomatous eyes. Invest. Ophthal­mol. Vis. Sci. 33,153-159.
  • 20. Matsuda, K. (1976) Studies on cathepsins of rat liver lysosomes. 111. Hydrolysis of peptides and inactivation of angiotensin and bradykinin by cathepsin A. /. Biochem. 80, 659-669.
  • 21. Miller, J.J., Chargasi, S.D.G. & I>evy, R.S. (1992) Purification, subunit structure and inhibitor profile of cathepsin A. J. Chromatogr. 627, 153-162.
  • 22. Galjart, N.J., Morreau, H., Willemsen, R., Gillemans, N., Bonten, E.J. & d'Azzo, A. (1991) Human lysosomal protective protein has cathe- psin A«like activity distinct from its protective function. J. Biol. Chan. 266,14754-14762.
  • 23. Cabral, L., Unger, W., Boulton, M., Lightfoot, R., McKechnie, N., Cierson, I. & Marshall, J. (1990) Regional distribution of lysosomal enzymes in the canine retinal pigment epithelium. Invest. Ophthalmol. Vis. Sci. 31,670-676.
  • 24. Hara, S., Plantner, J.J. & Kean, li.L. (1983) The enzymatic cleavage of rhodopsin by the retinal pigment epithelium. I. Enzyme preparation, properties and kinetics: Characterization of the glvcopeptide product. Exp. Eye Res. 36,799-813.
  • 25. Frank, R.N. (1991) On the pathogenesis of diabetic retinopathy. Ophthalmology 98,586-588.
  • 26. Jarmak, A. (1995) Biochemical aspects of lens opacity development. Klin. Oczna 97, 348-352, (in Polish).

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-9696a7cd-175f-4114-a2eb-4af7e8cfc2f4
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.