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Horm Metab Res 2004; 36(3): 148-154
DOI: 10.1055/s-2004-814338
Original Basic
© Georg Thieme Verlag Stuttgart · New York

Streptozotocin-induced Alterations in Rat Liver Golgi Complexes are Ameliorated by BMOV [Bis(maltolato)oxovanadium(IV)] Activity

A.  M.  Kordowiak1 , D.  Dziga2 , W.  Dabroś3
  • 1Department of General Biochemistry Faculty of Biotechnology
  • 2Department of Plant Physiology and Development, Faculty of Biotechnology, Jagiellonian University, Krakow
  • 3Department of Clinical and Experimental Pathomorphology, Medical Faculty, Collegium Medicum, Krakow, Poland
Further Information

Publication History

Received 16 June 2003

Accepted after revision 19 September 2003

Publication Date:
01 April 2004 (online)

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Abstract

Twenty years ago, we detected the interdependence between structure and function of rat liver Golgi complexes that are characteristic for streptozotocin diabetes, which served us in further investigations as a useful indicator of the effectiveness of drugs we were testing. This work presented results obtained in eight groups of rats (four control and four diabetic) that were administered orally either bis(maltolato)oxovanadium(IV) [BMOV] or maltol alone. The activities of the rat liver Golgi marker enzyme, galactosyltransferase [GalT], as well as the morphology of Golgi complexes were studied in situ using an electron microscope; parallel estimations of vanadium concentration and phospholipid percentage were made in Golgi-rich preparations isolated from the liver. Our main findings were normalization in diabetic animals orally treated with 1.8 mmol BMOV in 0.09 mol NaCl solutions over seven days, which demonstrated an accompanying increase in phosphatidic acid (PA) percentage (p < 0.05) compared to controls. In the diabetic groups, Pearson’s test showed a positive double correlation between GalT activity, vanadium concentration, and PA percentage in Golgi-rich membrane preparations from the liver. Additionally, a negative correlation was found between vanadium concentration and phosphatidylcholine percentage in the fractions.

Key words

STZ-diabetes - Vanadium - BMOV - Galactosyltransferase - Rat liver Golgi complexes - Phospholipids

References

  • 1 Heyliger C E, Tahiliani A G, McNeill J H. Effect of vanadate on elevated blood glucose and depressed cardiac performance of diabetic rats.  Science. 1985;  227 1474-1477
    PubMedGoogle Scholar
  • 2 Reul B A, Amin S S, Buchet J P, Ongemba L N, Crans D C, Brichard S M. Effects of vanadium complexes with organic ligands on glucose metabolism: a comparison study in diabetic rats.  Brit J Pharmacol. 1999;  126 467-477
    PubMedGoogle Scholar
  • 3 Domingo J L. Vanadium and diabetes. What about vanadium toxicity?.  Mol Cell Biochem. 2000;  203 185-187
    CrossrefPubMedGoogle Scholar
  • 4 Poucheret P, Verma S, Grynpas M D, McNeill J H. Vanadium and diabetes.  Mol Cell Biochem. 1998;  188 73-80
    CrossrefPubMedGoogle Scholar
  • 5 Cam M C, Brownsey R W, McNeill J H. Mechanisms of vanadium action: insulin-mimetic or insulin-enhancing agent.  Can J Physiol Pharmacol. 2000;  78 829-847
    CrossrefPubMedGoogle Scholar
  • 6 Crans D C. Chemistry and insulin-like properties of vanadium(IV) and vanadium(V) compounds.  J Inorg Biochem. 2000;  80 123-131
    CrossrefPubMedGoogle Scholar
  • 7 Tsiani E, Fantus I G. Vanadium compounds. Biological actions and potential as pharmacological agents.  Trends Endocrinol Metab. 1997;  8 51-58
    PubMedGoogle Scholar
  • 8 Aharon Y, Mevorach M, Shamoon H. Vanadyl sulfate does not enhance insulin action in patients with type 1 diabetes.  Diabetes Care. 1998;  21 2194-2195
    PubMedGoogle Scholar
  • 9 Badmaev V, Prakash S, Majeed M. Vanadium: a review of its potential role in the fight against diabetes.  J Alternat Complement Med. 1999;  5 273-291
    PubMedGoogle Scholar
  • 10 Goldfine A B, Patti M E, Zuberi L, Goldstein B J, LeBlanc R, Landaker E J, Jiang Z Y, Willsky G R, Kahn C R. Metabolic effects of vanadyl sulfate in humans with non-insulin-dependent diabetes mellitus: in vivo and in vitro studies.  Metabolism. 2000;  49 400-410
    CrossrefPubMedGoogle Scholar
  • 11 Kaczmarski F, Kordowiak A, Sarnecka-Keller M. Influence of insulin on galactosyltransferase activity and morphology of the rat liver Golgi apparatus in control and streptozotocin-diabetic rats.  Path Res Pract. 1981;  172 130-137
    PubMedGoogle Scholar
  • 12 Kordowiak A, Turyna B, Kaczmarski F, Sarnecka-Keller M. Comparison of rat plasma glycoprotein composition with biochemical activity and morphology of liver Golgi apparatus in streptozotocin-diabetes treated with insulin.  Folia Histochem Cytochem. 1981;  19 181-188
    PubMedGoogle Scholar
  • 13 Kordowiak A. The phospholipid and cholesterol contents of Golgi-rich membrane fraction from streptozotocin- or alloxan-diabetic rats and 6 h after streptozotocin rat livers.  Bull Acad Pol Sci. 1984;  32 165-171
    PubMedGoogle Scholar
  • 14 Kordowiak A M. Cytoprotective effect of 16,16’dimethylprostaglandin E2 (dmPGE2) on streptozotocin-induced biochemical alterations of Golgi-rich membrane fraction in comparison with morphology of rat liver Golgi apparatus in situ.  Path Res Pract. 1986;  181 397-402
    PubMedGoogle Scholar
  • 15 Kordowiak A M. The phospholipid contents in rat liver Golgi-rich membrane fractions after streptozotocin and/or prostaglandin treatment.  Folia Histochem Cytobiol. 1986;  24 39-46
    PubMedGoogle Scholar
  • 16 Kordowiak A M, Polanski M, Dabros W. Influence of LEPK on biochemical activity and morphology in situ of liver Golgi apparatus from control and streptozotocin-diabetic rats.  Pol J Pathol. 1997;  48 87-93
    PubMedGoogle Scholar
  • 17 DažbrosŽ W, Kordowiak A M, Dziga D, GrybosŽ R. Influence of bis(maltolato) oxovanadium(IV) on activity of galactosyltransferase (GalT) and morphology of rat liver Golgi apparatus in control and streptozotocin diabetes.  Pol J Pathol. 1998;  49 67-76
    PubMedGoogle Scholar
  • 18 DažbrosŽ W, Dziga D, Grybos R, Kordowiak A M. Biochemical and morphological alterations in rat liver Golgi complexes after treatment with bis(maltolato)oxovanadium(IV) [BMOV] or maltol alone.  Path Res Pract. 2000;  196 561-568
    PubMedGoogle Scholar
  • 19 DažbrosŽ W, Dziga D, Kordowiak A M. The influence of BMOV[bis(maltolato)oxovanadium(IV)] on biochemical and morphological alterations, characteristic for streptozotocin-diabetic rat liver Golgi complexes.  Pol J Pathol. 2002;  53 205-213
    PubMedGoogle Scholar
  • 20 Kordowiak A M, Nikiforuk A, DažbrosŽ W. Biochemical and morphological study of rat liver Golgi complex in streptozotocin-diabetic and control rats treated with bis(kojato)oxovanadium(IV) [VO(ka)2]x2H2O. Part I. One-week treatment with vanadium compound.  Pol J Pathol. 2000;  1 9-16
    PubMedGoogle Scholar
  • 21 Kordowiak A M, Trzos R, Grybos R. Insulin-like effects on liver Golgi membrane preparations of bis(oxalato)oxovanadate(IV) complex ion, a new vanadium compound.  Horm Metab Res. 1997;  29 104-108
    PubMedGoogle Scholar
  • 22 Kordowiak A M, Dudek B, Grybos R. Influence of sodium(oxalato)oxovanadium(IV) on phospholipids in liver Golgi fractions from control and streptozotocin-diabetic rats.  Comp Biochem Physiol Part C. 2000;  125 11-16
    PubMedGoogle Scholar
  • 23 Kordowiak A M, DažbrosŽ W, Kajda B. The influence of a new vanadium compound, bis(2,2'-bipyridine)oxovanadium(IV) sulphate on liver Golgi complexes from control and streptozotocin-diabetic rats.  Horm Metab Res. 2002;  34 1-5
    Article in Thieme ConnectPubMedGoogle Scholar
  • 24 Yuen V G, Caravan P, Gelmini L, Glover N, McNeill J H, Setyawati I A, Zhou R, Orvig C. Glucose lowering properties of vanadium compounds. Comparison of coordination complexes with maltol or kojic acid as ligands.  J Inorg Biochem. 1997;  68 108-116
    PubMedGoogle Scholar
  • 25 Fleischer B. Isolation and characterisation of Golgi apparatus from rat liver. In: Fleischer S, Packer L. (eds) Methods in Enzymology Vol 31A. New York; Acad Press Inc 1974: 180-191
    Google Scholar
  • 26 Lowry O H, Rosebrough N J, Farr A-L, Randall R-J. Protein measurement with Folin phenol reagent.  J Biol Chem. 1951;  193 265-275
    PubMedGoogle Scholar
  • 27 Somogyi M J, Nelson N. Determination of reducing sugars and carbohydrates. In: Whistler R, Wolprom R. (eds) Methods in Carbohydrate Chemistry vol 1. New York, London; Acad Press Inc 1962: 380-394
    Google Scholar
  • 28 Kates M. Techniques of lipidology. Isolation, analysis and identification of lipids. In: Work TS, Work E (eds) Laboratory Techniques in Biochemistry and Molecular Biology vol.3 New York; Elsevier 1972: 267-502
    Google Scholar
  • 29 Vaskovsky V E, Kostetsky E Y, Vasendin I M. A universal reagent for phospholipid analysis.  J Chromatogr. 1975;  114 129-141
    CrossrefPubMedGoogle Scholar
  • 30 Karnovsky M J. A formaldehyde-glutaraldehyde fixative of high osmolarity for use in electron microscopy.  J Cell Biol. 1965;  27 137A-138A
    PubMedGoogle Scholar
  • 31 Venable J H, Coggeshall R A. Simplified lead citrate stain for use in electron microscopy.  J Cell Biol. 1965;  25 407-408
    CrossrefPubMedGoogle Scholar
  • 32 Marzban L, Bhanot S, McNeill J H. In vivo effects of insulin and bis(maltolato)oxovanadium(IV) in PKB activity in the skeletal muscle and liver of diabetic rats.  Mol Cell Biochem. 2001;  223 147-157
    CrossrefPubMedGoogle Scholar
  • 33 Wang J, Yuen V G, McNeill J H. Effect of vanadium on insulin sensitivity and appetite.  Metabolism. 2001;  50 667-673
    CrossrefPubMedGoogle Scholar
  • 34 Cam M C, Brownsey R W, Rodrigues B, McNeill J H. Lack of in vivo effect of vanadium on GLUT4 translocation in white adipose tissue of streptozotocin-diabetic rats.  Metabolism. 2001;  50 674-680
    CrossrefPubMedGoogle Scholar
  • 35 Sasagawa T, Yoshikawa Y, Kawabe K, Sakurai H, Kojima Y. Bis(6-ethylpicolinato)oxovanadium(IV) complex with normoglycemic activity in KK-Ay mice.  J Inorg Biochem. 2002;  88 108-112
    CrossrefPubMedGoogle Scholar
  • 36 Semiz S, Orvig C, McNeill J H. Effects of diabetes, vanadium and insulin on glycogen synthase activation in Wistar rats.  Mol Cell Biochem. 2002;  231 23-35
    CrossrefPubMedGoogle Scholar
  • 37 Mohammad A, Wang J, McNeill J H. Bis(maltolato)oxovanadium(IV) inhibit the activity of PTP1B in Zucker rat skeletal muscle in vivo. .  Mol Cell Biochem. 2002;  229 125-128
    CrossrefPubMedGoogle Scholar
  • 38 Mohammad A, Bhanot S. McNeill JH. In vivo effects of vanadium in diabetic rats are in dependent of changes in PI-3 kinase activity in skeletal muscle.  Mol Cell Biochem. 2001;  223 103-108
    CrossrefPubMedGoogle Scholar
  • 39 Thompson K H, Tsakuda Y, Xu Z, Battell M, McNeill J H, Orvig C. Influence of chelation and oxidation state on vanadium bioavailability anf their effects on tissue concentrations of zinc, cooper and iron.  Biological Trace Element Research. 2002;  86 31-44 Humana Press Inc.
    CrossrefPubMedGoogle Scholar
  • 40 Rehder D, Pessoa J C, Geraldes C FGC, Castromm C A, Kabanos T, Kiss T, Meier B, Micera G, Petterson L, Rangel M, Salifoglou A, Turel I, Wand D. In vitro study of the insulin-mimetic behaviour of vanadium(IV,V) coordination compounds.  J Biol Inorg Chem. 2002;  7 384-396
    CrossrefPubMedGoogle Scholar
  • 41 Shafrir E, Spielman S, Nachliel I, Khamaisi M, Bar-On H, Ziv E. Treatment of diabetes with vanadium salts: general overview and amelioration of nutritionally induced diabetes in the Psammomys obesus gerbil.  Diabetes Metab Res Rev. 2001;  17 55-66
    CrossrefPubMedGoogle Scholar
  • 42 Woo L CY, Yuen V G, Thompson K H. Vanadyl-biquanide complexes as potential synergistic insulin mimics.  J Inorg Biochem. 1999;  76 251-257
    CrossrefPubMedGoogle Scholar
  • 43 Kordowiak A, Sarnecka-Keller M. The protein patterns of Golgi-rich membrane preparations from the livers of control, insulin treated and streptozotocin diabetic rats.  Bull Acad Pol Sci. 1977;  25 205-209
    PubMedGoogle Scholar
  • 44 Roth M G, Bi K, Ktistakis N T, Yu S. Phospholipase D as an effector for ADP-ribosylation factor in the regulation of vesicular traffic.  Chem Phys Lipids. 1999;  98 141-152
    PubMedGoogle Scholar
  • 45 De Camili P, Emr S D, McPherson P S, Novick P. Phosphoinositides as regulators in membrane traffic.  Science. 1996;  271 1533-1539
    PubMedGoogle Scholar
  • 46 Breton C, Mucha J, Jeanneau C. Structural and functional features of glycosyltransferases.  Biochimie. 2001;  83 713-718
    CrossrefPubMedGoogle Scholar
  • 47 Kordowiak A M, Wojas J, SubczynŽski W K. Fluidity of rat liver Golgi membranes in streptozotocin diabetes. A spin label study.  Biochem Biophys Acta. 1990;  1022 296-302
    PubMedGoogle Scholar
  • 48 Siddhanta A, Shields D. Secretory vesicle budding from the trans-Golgi network is mediated by phosphatidic acid levels.  J Biol Chem. 1998;  273 17 995-17 998
    PubMedGoogle Scholar
  • 49 Siddhanta A, Bacek J M, Shields D. Inhibition of phosphatidic acid synthesis alters the structure of the Golgi apparatus and inhibits secretion of endocrine cells.  J Biol Chem. 2000;  275 12 023-12 031
    PubMedGoogle Scholar

Prof. Dr. A. M. Kordowiak

Department of General Biochemistry, Faculty of Biotechnology

Jagiellonian University · 7 Gronostajowa. St. · 30-387 Krakow · Poland

Phone: +48(12)6646531

Fax: +48(12)6646902 ·

Email: mpdabros@cyf-kr.edu.pl; anna@piryt.net

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