Download PDF
Horm Metab Res 2002; 34(10): 556-560
DOI: 10.1055/s-2002-35427
Original Basic
© Georg Thieme Verlag Stuttgart · New York

The Influence of a New Vanadium Compound, Bis(2,2’-bipyridine)oxovanadium(IV) Sulphate on Liver Golgi Complexes from Control and Streptozotocin-Diabetic Rats

A.  M.  Kordowiak 1 , W.  Dąbroś 2 , B.  Kajda 1
  • 1Institute of Molecular Biology and Biotechnology, Jagiellonian University, Department of General Biochemistry, Cracow, Poland
  • 2Department of Clinical and Experimental Pathomorphology, Collegium Medicum Jagiellonian University, Cracow, Poland
Further Information

Publication History

Received: 17 January 2002

Accepted after second revision: 9 July 2002

Publication Date:
19 November 2002 (online)

Also available at
    Permissions and Reprints

Abstract

Among the previously studied organic vanadium derivatives showing an anti-diabetic action, we investigated a new complex, bis(2,2′-bipyridine)oxovanadium(IV) sulphate. We tested its ability to normalise parameters previously described for streptozotocin (STZ)-diabetes, such as lower yields of Golgi-rich membrane fraction isolation, decreased activity of Golgi membrane marker enzyme - galactosyltransferase (GalT) - and altered morphology of rat liver Golgi complexes. Oral application as a drinking solution of 1.8 mmol bis(2,2′-bipyridine)oxovanadium(IV) (dissolved in 0.09 M NaCl) caused a similar dispersion of GalT activities in both vanadium treated groups, control and diabetic. Very low activities of the enzyme (characteristic for untreated diabetes) we found only in approximately 35 % of the STZ-diabetic rats treated with the new vanadium compound. The morphology of liver Golgi complexes in diabetic rats treated with bis(2,2′-bipyridine)oxovanadium(IV) sulphate was improved, which manifested itself in the reappearance of vacuoles with VLDL and coated and uncoated secretory vesicles. In view of biochemical and morphological parameters of normalised diabetic rat liver Golgi apparatus, the new vanadium complex was more effective than bis(oxalato)oxovanadium(IV) or bis(kojato)oxovanadium(IV), but in our experimental model, the best anti-diabetic, orally applied drug was the bis(maltolato)oxovanadium(IV) previously investigated.

Key words

Golgi Complexes - Bis(2,2′-bipyridine)oxovanadium(IV) - Galactosyltransferase (GalT) - Pathology - Liver - Streptozotocin (STZ)

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 Tsiani E, Fantus I G. Vanadium compounds. Biological actions and potential as pharmacological agents.  Trends Endocrinol Metab. 1997;  8 51-58
    PubMedGoogle Scholar
  • 3 Domingo J L. Vanadium and diabetes. What about vanadium toxicity?.  Mol Cell Biochem. 2000;  203 185 -187
    CrossrefPubMedGoogle Scholar
  • 4 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
  • 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 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
  • 7 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
  • 8 Crans D C. Chemistry and insulin-like properties of vanadium(IV) and vanadium(V) compounds.  J Inorg Biochem. 2000;  80 123-131
    CrossrefPubMedGoogle Scholar
  • 9 Fantus I G, Tsiani E. Multifunctional actions of vanadium compounds on insulin signalling pathways: evidence for preferention enhancement of metabolic vs. mitogenic effects.  Mol Cell Biochem. 1998;  182 109-119
    CrossrefPubMedGoogle Scholar
  • 10 Cam M C, Li W M, McNeill J H. Partial preservation of pancreatic beta cells by vanadium. Evidence for long-term amelioration of diabetes.  Metabolism. 1997;  46 769-778
    CrossrefPubMedGoogle Scholar
  • 11 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
  • 12 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
  • 13 Da˛brosŽ W, Dziga D, GrybosŽ 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
  • 14 Da˛brosŽ 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
  • 15 Kordowiak A M, Nikiforuk A, Da˛brosŽ 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] × 2H2O. Part I. One-week treatment with vanadium compound.  Pol J Pathol. 2000;  1 9-16
    PubMedGoogle Scholar
  • 16 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
  • 17 Yuen V G, Orvig C, McNeill J H. Comparison of the glucose-lowering properties of vanadyl sulfate and bis(maltolato)oxovanadium(IV) following acute and chronic administration.  Can J Physiol. 1995;  75 55-64
    PubMedGoogle Scholar
  • 18 Bhanot S, Girn J, Poucheret P, McNeill J H. Effects of bis(maltolato)oxovanadium(IV) on protein serine kinases in skeletal muscle of streptozotocin-diabetic rats.  Mol Cell Biochem. 1999;  202 131-140
    CrossrefPubMedGoogle Scholar
  • 19 Kordowiak A M, Trzos R, GrybosŽ 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
  • 20 Kordowiak A M, Dudek B, GrybosŽ 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
  • 21 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
  • 22 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
  • 23 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
  • 24 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
  • 25 Kordowiak A M, PolanŽski M, Da˛brosŽ 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
  • 26 Fleischer B. Isolation and characterisation of Golgi apparatus from rat liver. In: Fleischer S, Packer L (eds) Methods in Enzymology. New York; Acad Press Inc 1974 31A: 180-191
    Google Scholar
  • 27 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
  • 28 Somogyi M J, Nelson N. Determination of reducing sugars and carbohydrates. In: Whistler R, Wolprom R (eds) Methods in Carbohydrate Chemistry. New York, London; Acad Press Inc 1962 1: 380-394
    Google Scholar
  • 29 Karnovsky M J. A formaldehyde-glutaraldehyde fixative of high osmolarity for use in electron microscopy.  J Cell Biol. 1965;  27 137A-138A
    PubMedGoogle Scholar
  • 30 Venable J H, Coggeshall R A. Simplified lead citrate stain for use in electron microscopy.  J Cell Biol. 1965;  25 407- 408
    CrossrefPubMedGoogle Scholar
  • 31 Kurup S, Bhonde R R. Combined effect of nicotinamide and streptozotocin on diabetic status in partially pancreatectomized adult BALB/c mice.  Horm Metab Res. 2000;  32 330-334
    PubMedGoogle Scholar
  • 32 Z˙endzian-Piotrowska M, Bucki R, Górska M, Górski J. Diabetes affects phospholipid content in the nuclei of the rat liver.  Horm Metab Res. 2000;  32 386-389
    PubMedGoogle Scholar

Dr. hab. Anna M. Kordowiak

Institute of Molecular Biology and Biotechnology, Jagiellonian University ·

Ul. Gronostajowa 7,30-387 · Cracow · Poland

Fax: + 48-12-252 6902

      >