The effect of dietary protein level on selected degradative enzymes activity of hepatocyte cellular subfractions in experimental mice

• Autorzy: Witek B. , Fronczyk W. , Jozwik A. , Walczak M. , Kaminska A. , Kolataj A.
• Języki publikacji: EN

Abstrakty

EN

Studied was the activity of selected degradative enzymes of lysosomal, microsomal and cytoplasmic fraction of hepatocytes as affected by different protein levels in the diet of experimental mice. The control animals were fed with standard 16% protein level in the diet, while experimental animals with low (10%) or high (40%) protein diet. The animals were fed ad libitum. Changes in fractions depended on the kind of enzyme, cell fraction and protein level in examined diets. The high protein diet increased activity of six enzymes in the lysosomal fraction and decreased activity of β-Gal only,while the low protein diet caused an increase of activity of this fraction of seven enzymes. The 40% protein diet decreased the activity of nine enzymes in the microsomal fraction, the AcP did not change only. The 10% protein diet in this fraction decreased the activity of seven enzymes and increased activity of two enzymes. In the cytoplasmic fraction, the high protein diet decreased the activity of eight enzymes. Higher activity was observed only for AcP. The low protein diet caused a decrease in seven enzymes activity, and an increase of β-GlcUr activity only. The change of normal standard protein diet in animal feeding on its high or low-protein level occurred to be a significantfactor disordering the biochemical homeostasis of the cell.

• Wydawca: -
• Czasopismo: Animal Science Papers and Reports
• Rocznik: 2014
• Tom: 32
• Numer: 3
• Opis fizyczny: p.269-277,ref.

Twórcy

autor

Witek B.

• Department of Animal Physiology, The Jan Kochanowski University in Kielce, Swiętokrzyska 15, 25-406 Kielce, Poland

autor

Fronczyk W.

• Department of Animal Physiology, The Jan Kochanowski University in Kielce, Swiętokrzyska 15, 25-406 Kielce, Poland

autor

Jozwik A.

• Polish Academy of Sciences Institute of Genetics and Animal Breeding, Jastrzebiec, Postepu 36A, 05-552 Magdalenka, Poland

autor

Walczak M.

• Polish Academy of Sciences Institute of Genetics and Animal Breeding, Jastrzebiec, Postepu 36A, 05-552 Magdalenka, Poland

autor

Kaminska A.

• Medical Practice, Mehoffera 160J, 03-081 Warszawa, Poland
• Cardinal Stefan Wyszynski University in Warsaw, Woycickiego 1/3, 01-938 Warszawa, Poland

autor

Kolataj A.

• Polish Academy of Sciences Institute of Genetics and Animal Breeding, Jastrzebiec, Postepu 36A, 05-552 Magdalenka, Poland

Bibliografia

• BARRETT A.J., HEATH M.F., 1977 – Lysosomal enzymes. In: Lysosomes. A Laboratory Handbook [J.T. Dingle, Ed.], North-Holland Publ. Co., Amsterdam, New York, Oxford, 19-145.
• CAYLAK E., AYTEKIN M., HALIFEOGLU I., 2008 – Antioxidant effects of methionine, alphalipoic acid, N-acetylcysteine and homocysteine on lead-induced oxidative stress to erythrocytes in rats. Experimental and Toxicologic Pathology 60, 289-294.
• DRÖGE W., 2005 – Oxidative stress and ageing: is ageing a cysteine deficiency syndrome? Philosophical Transactions of the Royal Society B: Biological Sciences 360, 2355-2372.
• EDWARDS A.G., DONATO A.J., LESNIEWSKI L.A., GIOSCIA R.A., SEALS D.R., MOORE R.L., 2010 – Life-long caloric restriction elicits pronounced protection of the aged myocardium: a role for AMPK. Mechanisms of Ageing and Development 131, 739-742.
• GRUNE T., REINHECKEL T., DAVIES K.J.A., 1997 – Degradation of oxidized proteins in mammalian cells. The FASEB Journal, 11, 526-534.
• HARDIE D.G., 2011 – AMP-activated protein kinase: a cellular energy sensor with a key role in metabolic disorders and in cancer. Biochemical Society Transactions 39, 1-13.
• JÓŹWIK A., BAGNICKA E., STRZAŁKOWSKA N., ŚLIWA-JÓŹWIK A., HORBAŃCZUK K.,COOPER R.G., PYZEL B., KRZYŻEWSKI J., ŚWIERGIEL A.H., HORBAŃCZUK J.O., 2010 –The oxidative status of milking goats after per os administration of N-acetylcysteine. Animal Science Papers and Reports 2, 143-152.
• JÓŹWIK A., POŁAWSKA E., STRZAŁKOWSKA N., NIEMCZUK K., ŁYSEK-GŁADYSIŃSKA M., KAMIŃSKA A., MICHALCZUK M., 2013 – Effect of linseed, rapeseed, and vitamin E long term supplementation on the activity of the lysosomal enzymes in ostrich liver. Bulletin of theVeterinary Institute in Pulawy 57, 4 (in press).
• KIRSCHKE H., WIEDERANDERS B., 1984 – Methoden zur Aktivitätsbestimmung von Proteinases. Martin-Luther-Universität, Halle-Wittenberg Wissenschaftliche Beiträge, Halle/Salle 11-17.
• KOŁĄTAJ A., JÓŹWIK A., ŚLIWA-JÓŹWIK A., 2001 – The lysosomal cell complex as stress response indicator. Animal Science Papers and Reports 3, 177-192.
• LANGNER J., WAKIL A. ZIMMERMANN M., ANSORGE S., BOHLEY P., KIRSCHKE H.WIEDERANDERS B., 1973 – Aktivitätsbestimmung proteolytischer Enzyme mit Azocasein als Substrat. Acta Biologica et Medica Germanica 31, 1-18.
• MARSCHNER K., KOLLMANN K., SCHWEIZER, M., BRAULKE T., POHL S., 2011 – A Key Enzyme in the Biogenesis of Lysosomes is a Protease that Regulates Cholesterol Metabolism.Science 6038, 87-90.
• MARZELLA L., GLAUMANN H., 1980 – Inhibitory effect of vinblastine on protein degradation. Virchows Archiv - B Cell Pathology 34, 111-122.
• MC DONALD J.K., BARRETT A.J. 1986 – Exopeptidases. In: Mammalian Proteases: A Glossary and Bibliography, Academic Press, (London), 111-144.
• NAKAHARA K., OKAME R., KATAYAMA T., MI YAZATO M., KANGAWA K.,MURAKAMI N., 2010 – Nutritional and environmental factor affecting plasma ghrelin and leptin levels in rats.Journal of Endocrinology 207, 95-103.
• SCHULTZ M.L., TECEDOR L., CHANG M., DAVIDSON B.L., 2011 – Clarifying lysosomal storage diseases. Trends in Neurosciences 34, 401- 410.
• SHANG L., CHEN S., DU F., LI S., ZHAO L., WANG X., 2011 – Nutrient starvation elicits and acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK. Proceedings of the National Academy of Sciences of the United States of America 108,4788-4793.
• SMITH D.L. Jr., NAGY T.R., ALLISON D.B., 2010 – Calorie restriction: what recent results suggest for the future of ageing research. European Journal of Clinical Investigation 40, 440-450.
• STASZCZAK M., ZDUNEK E., 1999 – Proteoliza wewnątrzkomórkowa. Postępy Biochemii 45,32-41.
• TURNER R.T., IWANIEC U.T., 2010 – Moderate weight gain does not influence bone metabolism in skeletally mature female rats. Bone 47, 3, 631-635.
• TYAGI N., SEDORIS K.C., STEED M., OVECHKIN A.V., MOSHAL K.S., TYAGI S.C., 2005 – Mechanisms of homocysteine-induced oxidative stress. American Journal of Physiology: Heart and Circulatory Physiology 289, H2649-H2656.
• WITEK B., OCHWANOWSKA E., BARANOWSKA D., KOŁĄTAJ A., 2007 – The effect of selection for body weight on the activity of lysosomal enzymes in rat liver and kidney of mice.Animal Science Papers and Reports 25, 119-125.
• WITEK B., OCHWANOWSKA E., WRÓBEL A., KOŁĄTAJ A., 2011 – Effect of morphine on activity of five selected lysosomal enzymes in liver and kidneys of mice. Animal Science Papers and Reports 29, 151-159.