Wyniki wyszukiwania

1

A lysosomal high molecular weight multienzyme complex

100%

Ostrowska H., Jedynasta-Kozlowska W., Kalinowska J.

Cellular and Molecular Biology Letters

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2002

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tom 07

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nr Suppl.

2

Cathepsin A and chymotrypsin-like activity of the proteasome in human blood platelet

100%

Ostrowska H., Wojcik C., Worowski K.

Folia Histochemica et Cytobiologica

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1999

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tom 37

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nr 2

3

Role of cathepsin A and cathepsin C in the regulation of glycosidase activity

84%

Minarowska A., Minarowski L., Karwowska A., Milewska A. J., Gacko M.

Folia Histochemica et Cytobiologica

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2012

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tom 50

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nr 1

4

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

84%

Obuchowska I., Stankiewicz A., Mariak Z.

Acta Biochimica Polonica

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1996

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tom 43

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nr 4

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.

5

Lysosomal high molecular weight multienzyme complex

84%

Ostrowska H., Krukowska K., Kalinowska J., Orlowska M., Lengiewicz I.

Cellular and Molecular Biology Letters

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2003

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tom 08

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nr 1

Three acidic glycosidases: β-galactosidase (β-GAL, EC 3.2.1.23), α-neuraminidase (NEUR, sialidase, EC 3.2.1.18), N-acetylaminogalacto-6-sulfate sulfatase (GALNS, EC 3.1.6.4) and serine carboxypepidase cathepsin A (EC 3.4.16.1) form a functional high molecular weight complex in the lysosomes. The major constituent of this complex is cathepsin A, the so-called “lysosomal protective protein” (PPCA). By forming a multienzyme complex, it protects the glycosidases from rapid intralysosomal proteolysis, and it is also required for the intracellular sorting and proteolytic processing of their precursors. In man, a deficiency of cathepsin A leads to a combined deficiency of β-GAL and NEUR activities, called “galactosialidosis”. Multiple mutations identified in the cathepsin A gene are the molecular basis of this lysosomal storage disease. This review describes the structural organization of the lysosomal high molecular weight multienzyme complex and the importance of the protective protein/cathepsin A in physiology and pathology.

6

Cathepsin A activity of a parietal thrombus of an abdominal aortic aneurysm

67%

Siergiejuk M., Gacko M., Worowska A.

Folia Histochemica et Cytobiologica

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2011

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tom 49

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nr 1

7

Inhibitory proteaz lizosomalnych lupin i liscieni nasion wyki

59%

Roszkowska-Jakimiec W., Kiziewicz B., Lahuta L.

Bromatologia i Chemia Toksykologiczna

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2005

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tom 38

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nr Supl.

333-335

Łupiny i liścienie różnych gatunków i odmian wyki zawierają inhibitory katepsyny A, katepsyny В i katepsyny D.

8

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Muscle cathepsins of marine fish and invertebrates

51%

Kolodziejska I., Sikorski Z. E.

Polish Journal of Food and Nutrition Sciences

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1995

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tom 04

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nr 3

Muscle proteases are located mainly in the lysosomes, in the sarcoplasm, and in the extracellular matrix of the connective tissue surrounding each cell. The lysosomal proteases, cathepsins, have optimum activity in the acidic range, although many of them retain high activity also 1 or 2 pH units away from the optimum value. Among the cathepsins there are endopeptidases and exopeptidases. Most cathepsins hydrolyse several proteins of the myofibrils. The major protease of the lysosomes in fish and squid muscles is cathepsin D, an aspartyl endoproteinase. Although it is present in the muscle fibre itself, its generally rather low activity at low temperature limits its significance in tenderization of refrigerated fish of most species. Cathepsin L, a cysteinyl protease, is involved in autolysis and softening in matured chum salmon. Cathepsin B, a cysteinyl carboxypeptidase, is capable to attack also some myofibrillar proteins. Cathepsin A or carboxypeptidase A, and cathepsin C, a dipeptidyl hydrolase and dipeptidyl transferase, contribute to the hydrolysis of muscle proteins in a concerted action with the other cathepsins.

Ograniczanie wyników

A lysosomal high molecular weight multienzyme complex

Cathepsin A and chymotrypsin-like activity of the proteasome in human blood platelet

Role of cathepsin A and cathepsin C in the regulation of glycosidase activity

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

Lysosomal high molecular weight multienzyme complex

Cathepsin A activity of a parietal thrombus of an abdominal aortic aneurysm

Inhibitory proteaz lizosomalnych lupin i liscieni nasion wyki

Muscle cathepsins of marine fish and invertebrates