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

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.

[1]  A. Jarmak [Biochemical aspects of the development of lens opacity]. , 1995, Klinika oczna.

[2]  I. Constable,et al.  Detection and possible functions of a cysteine protease involved in digestion of rod outer segments by retinal pigment epithelial cells. , 1994, Investigative ophthalmology & visual science.

[3]  T. Drew,et al.  Polarized distribution of metalloproteinases in the bovine interphotoreceptor matrix. , 1994, Experimental eye research.

[4]  J. Sugar,et al.  Lysosomal enzyme activities in conjunctival tissues of patients with keratoconus. , 1994, Archives of ophthalmology.

[5]  M. Reim,et al.  Investigation of enzyme activities in severe burns of the anterior eye segment , 1993, Graefe's Archive for Clinical and Experimental Ophthalmology.

[6]  R. S. Levy,et al.  Purification, subunit structure and inhibitor profile of cathepsin A. , 1992, Journal of chromatography.

[7]  N. Gillemans,et al.  Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function. , 1991, The Journal of biological chemistry.

[8]  M. Fini,et al.  Expression of collagenolytic/gelatinolytic metalloproteinases by normal cornea. , 1990, Investigative ophthalmology & visual science.

[9]  M. Boulton,et al.  Regional distribution of lysosomal enzymes in the canine retinal pigment epithelium. , 1990, Investigative ophthalmology & visual science.

[10]  R. Klein,et al.  The incidence of vision loss in a diabetic population. , 1988, Ophthalmology.

[11]  E. Villanueva,et al.  Aminopeptidase and cathepsin A activity in vitreous humor in relation to causes of death. , 1985, Forensic science international.

[12]  R. Frank,et al.  On the pathogenesis of diabetic retinopathy. , 1984, Ophthalmology.

[13]  S. Hara,et al.  The enzymatic cleavage of rhodopsin by the retinal pigment epithelium. I. Enzyme preparation, properties and kinetics: characterization of the glycopeptide product. , 1983, Experimental eye research.

[14]  G. Volden,et al.  CATHEPSIN B, CATHEPSIN C AND ARYLAMIDASE IN RABBIT CORNEA , 1982, Acta ophthalmologica.

[15]  K. Matsuda Studies on cathepsins of rat liver lysosomes. III. Hydrolysis of peptides, and inactivation of angiotensin and bradykinin by cathepsin A. , 1976, Journal of biochemistry.

[16]  Steven P. Miller,et al.  Studies of γ-glutamyl transpeptidase in human ocular tissues , 1976 .

[17]  J Caprioli,et al.  Discrimination between normal and glaucomatous eyes. , 1992, Investigative ophthalmology & visual science.

[18]  B. Ortwerth,et al.  Aminopeptidase III activity in normal and cataractous lenses. , 1986, Current eye research.

[19]  J. Mcdonald,et al.  Dipeptidyl peptidase III of human cataractous lenses. Partial purification. , 1984, Current eye research.