Zmiany aktywnosci enzymow lizosomowych w watrobie i nerkach myszy po iniekcjach glukagonu

• Autorzy: Witek B , Graniczka A. , Ochwanowska E. , Kolataj A.

Warianty tytułu

EN

Changes of the lysosomal enzyme activity in the liver and kidney of mice after glucagon injections

• Języki publikacji: PL

Abstrakty

EN

Changes in the activity of β-glucuronidase, N-acetyl- β -glucosaminidase, cathepsin D and cathepsin L in the liver and kidney of mice, injected intraperitonealy with 15 µg/kg b.w. of glucagon were investigated. The experiment was carried out on 24 8-week-old mice, whose parents were chosen from random match. The homogenates of the liver and kidney were subjected to differentiate centrifuging, and in the lysosomal fractions of the liver and kidney the activities of β -glucuronidase [β -GlcUr], N-acetyl- β -glucosaminidase [NAG], cathepsin D [Cath. D], and cathepsin L [Cath. L] were estimated. Injection of glucagon caused a decrease in the activity of β -glucuronidase in the liver and kidney, cathepsin L in the liver, N-acetyl-b-glucosaminidase in the kidney, and an increase cathepsin D and cathepsin L in the kidney of mice. The results suggest that exogenous glucagon had a significant influence on the activity investigated lysosomal enzymes. The range of the reaction remained in a relationship with the kind of the organ and type of enzyme.

Słowa kluczowe

PL

enzymy lizosomalne; aktywnosc enzymatyczna; nerki; myszy; zmiany aktywnosci; watroba; glukagon; podawanie dootrzewnowe; narzady wewnetrzne

• Wydawca: -
• Czasopismo: Medycyna Weterynaryjna
• Rocznik: 2006
• Tom: 62
• Numer: 06
• Strony: 717-719
• Opis fizyczny: s.717-719,tab.,bibliogr.

Twórcy

autor

Witek B

• Akademia Swietokrzyska, ul.Swietokrzyska 15, 25-406 Kielce

autor

Graniczka A.

autor

Ochwanowska E.

autor

Kolataj A.

Bibliografia

• 1.Abou-Haila A., Fouquet J. P., Tulsiani D. R.: Characterization and immunolocalization of beta-D-glucosidase in mouse testicular germ cells and spermatozoa. Exp. Cell Res. 1999, 25, 48-60.
• 2.Barrett A. J.: Lysosomal enzymes, [w:] Lysosomes. A Laboratory Handbook (Dingle J. T.), North-Holland Publ. Co., Amsterdam 1972, 46-135.
• 3.Beaufay H.: Methods for isolation of lysosomes, [w:] Lysosomes. A Laboratory Handbook (Dingle J. T.), North-Holland Publ. Co., Amsterdam 1972, 1-30.
• 4.Brosnan J. T., Man K. C., Hall D. E., Colbourne S. A., Brosnan M. E.: Interorgan metabolism of amino acids in streptozotocin-diabetic ketoacidotic rats. Am. J. Physiol. 1983, 244, E151-E158.
• 5.Cuervo A. M., Dice J. F.: When lysosomes get old. Exp. Geront. 2000, 35, 119-131.
• 6.Denda M., Tsuchiya T., Elias P. M., Feingold K. R.: Stress alters cutaneous permeability barrier homeostasis. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2000, 278, R367-372.
• 7.Edelman G. M., Crossin K. L.: Cell adhesion molecules: implications for molecular histology. Ann. Rev. Biochem. 1991, 60, 155-190.
• 8.Eskelinen E. L., Tanaka Y., Saftig P.: At the acidic edge: emerging functions for lysosomal membrane proteins. Trends Cell Biol. 2003, 13, 137-145.
• 9.Gao C., Sands M. S., Haskins M. E., Ponder K. P.: Delivery of a retroviral vector expressing human beta-glucuronidase to the liver and spleen decreases lysosomal storage in mucopolysaccharidosis VII mice. Mol. Ther. 2000, 3, 233-244.
• 10.Ghodsi A., Stein C., Derksen T., Yang G., Anderson R. D., Davidson B. L.: Extensive beta-glucuronidase activity in murine central nervous system after adenovirus-mediated gene transfer to brain. Hum. Gene Ther. 1998, 16, 2331- -2340.
• 11.Gromakova I. A., Kovalenko O. A.: Lysosomal proteolysis: effects of aging and insulin. Biochemistry 2003, 68, 772-775.
• 12.Jansson I., Curti M., Epstein P. M., Peterson J. A., Schenkman J. B.: Relationship between phosphorylation and cytochrome P450 destruction. Arch. Biochem. Biophys. 1990, 283, 285-292.
• 13.Jóźwik A., Śliwa-Jóźwik A., Fronczyk W., Kołątaj A.: Aktywność enzymów lizosomowych u myszy pod wpływem selekcji na tempo wzrostu. Medycyna Wet. 2003, 59, 348-350.
• 14.Kankofer M., Wierciñski J., Zerbe H.: Activity of placental b-N-acetyl-glucosaminidase in cows with and without retained fetal membranes. Reprod. Dom. Anim. 2000, 35, 97-100.
• 15.Kirschke H., Wiederanders B.: Methoden zur Aktivitätsbestimmung von Proteinasen. Martin-Luther-Universität, Halle-Wittenberg Wissenschaftl. Beitr. Halle/Salle 1984, 11-17.
• 16.Kirschke H., Langner J., Wiederanders B., Ansorge S., Broghammer U.: VII. Katepsine L und H: zwei neue Proteinasen aus Rattenleberlysosomen. Acta Biol. Med. Germ. 1976, 35, 285-299.
• 17.Klionsky D. J., Emr S. D.: Autophagy as a regulated pathway of cellular degradation. Science 2000, 290, 1717-1721.
• 18.Kołątaj A., Śliwa-Jóźwik A., Jóźwik A.: The lysosomal cell complex as a stress response indicator. Anim. Sci. Papers Reports 2001, 19, 177-192.
• 19.Lloyd J. B.: Lysosome membrane permeability: implications for drug delivery. Adv. Drug Deliv. Rev. 2000, 30, 189-200.
• 20.Morales C., Zhao Q., Lefrancois S.: Biogenesis of lysosomes by endocytic flow of plasma membrane. Biocell. 1999, 23, 149-160.
• 21.Nakano A., Marks D. L., Tietz P. S., Groen P. C., La Russo N. F.: Quantitative importance of biliary excretion to the turnover of hepatic lysosomal enzymes. Hepatology 1995, 22, 262-266.
• 22.Niemann R., Buddecke E.: Substrate specificity and regulation of activity of rat liver b-D-glucuronidase. Hoppe-Seylers, Z. Physiol. Chem. 1982, 363, 591-598.
• 23.Oesch-Bartlomowicz B., Oesch F.: Phosphorylation of cytochrome P-450 isoenzymes in intact hepatocytes and its importance for their function in metabolic process. Arch. Toxicol. 1990, 64, 257-261.
• 24.Ohashi T., Yokoo T., Iizuka S., Kobayashi H., Sly W. S., Eto Y.: Reduction of lysosomal storage in murine mucopolisaccharidosis type VII by transplantation of normal and genetically modified macrophages. Blood 2000, 11, 3631- -3633.
• 25.Patil S., Kanase A.: Cholesterol mediated changes in b-glucuronidase activities of rat theca interstitial cells and granulosa cells. Indian J. Exp. Biol. 1995, 33, 321-324.
• 26.Qureshi S. A., Candelore M. R., Xie D., Yang X., Tota L. M., Ding V. D., Li Z., Bansal A., Miller C., Cohen S. M., Jiang G., Brady E., Saperstein R., Duffy J. L., Tata J. R., Chapman K. T., Moller D. E., Zhang B. B.: Role of glucagon in the pathogenesis of diabetes: the status of the controversy. Metabolism 2001, 27, 1691-1709.
• 27.Sahagian G. G., Novikoff P. M.: Lysosomes, [w:] Asias I. M., Boyer J. L., Fausto N., Jakoby W. B., Schachter D. A., Shafritz D. A.: The Liver: Biology and Pathobiology. Raven Press, Ltd., NY 1994, 275-291.
• 28.Senba M., Kaghige N., Miake F., Watanabe K.: Purification and properties of three b-N-acetyl-glucosaminidases from Lactobacillus casei ATCC 27092. Biosci. Biotechnol. Biochem. 1998, 62, 404-406.
• 29.Sheeler P., Bianchi D. E.: Cell Biology: Structure Biochemistry and Function. John Willey&Sons, NY 1980.
• 30.Witek B.: Wpływ egzogennego glutationu zredukowanego, askorbinianu, retinolu oraz a-tokoferolu na aktywność enzymów układu lizosomowego komórek wątroby, nerki i mięśnia myszy żywionych zróżnicowaną dietą białkową. Wyd. SGGW, Warszawa 2003.
• 31.Witek B., Kołątaj A.: The effect of exogenous glucose on the activity of lysosomal enzymes in some organs of rabbits. Arch. Tierz. 2000, 43, 649-654.
• 32.Witek B., Kołątaj A., Jeżewska G., Witkowski A.: Effect of glucose, glutathione and ethanol on the activities of some lysosomal enzymes in quail. Acta Biol. Cracov. Ser. Zool. 2000, 42, 67-72.
• 33.Witek B., Ochwanowska E., Kołątaj A., Ślewa A., Stanisławska I.: Effect of melatonin administration on activities of some lysosomal enzymes in the mouse. Neuroendocrinol. Lett. 2001, 22, 181-185.