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1999 | 46 | 4 |

Tytuł artykułu

Accumulation of collagen in ovarian benign tumours

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Extracellular matrix components of benign ovarian tumours (cystadenoma, adenofibroma, cystadenofibroma) were analysed. The investigated tumours contained twice as much collagen than control ovarian tissues. Significant alterations in mutual quantitative relationships between collagens of various types were observed. The proportion of type I collagen decreased and that of type III collagen increased. The accumulation of collagen was accompanied by a reduction in sulphated glycosaminoglycan content whereas the amount of hyaluronic acid was not changed. Dermatan sulphate was the most abundant glycosaminoglycan component. It is suggested that the accumulation of collagen (natural barrier to the migration of tumour cells) and underexpression of glycosaminoglycans/proteoglycans (binding some growth factors and interleukins) may exert an inhibitory effect on tumour growth.

Wydawca

-

Rocznik

Tom

46

Numer

4

Opis fizyczny

p.941-947,fig.

Twórcy

autor
  • Medical Academy of Bialystok, A.Mickiewicza 2, 15-230 Bialystok 8, Poland
autor

Bibliografia

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  • 2. Iozzo, R.V. (1988) Proteoglycans and neopla­sia. Cancer Metastasis Rev. 7, 39-50.
  • 3. Bańkowski, E., Rzeczycki, W., Nowak, H.F. & Jodczyk, K.J. (1978) Decrease of collagen biosynthesis ability of rat kidney fibroblasts transformed with SV-40 virus. Mol Cell Riochem. 20. 77-83.
  • 4. Kamine, J. & Rubin, H. (1977) Coordinate con­trol of collagen synthesis and cell growth in chick embryo fibroblasts and the effect of viral transformation on collagen synthesis. J. Cell Physiol. 92. 1-12.
  • 5. Levinson, W., Bhatnagar, R.S. & Liu, T.Z. (1975) Loss of ability to synthesize collagen in fibroblasts transformed by Rous sarcoma vi­rus. J. Natl Cancer Inst. 55, 807-810.
  • 6. Klagsbrun, M. (1976) The decreased synthesis of chondroitin sulfate containing extracellular proteoglycans by SV-40 transformed Balb c/3T3 cells. Biochim. Riophys. Acta. 451, 170-183.
  • 7. Pacifici, M., Boettiger, D., Roby, K. & Holtzer, H. (1977) Transformation of chondroblasts by Rous sarcoma virus and synthesis of the sul­fated proteoglycan matrix. Cell 11, 891-899.
  • 8. Sobolewski, K. & Bańkowski, E. (1984) Heter­ogeneity of collagen isolated from methyl- cholanthrene induced sarcoma. Acta Biochim. Polon. 31, 317-328.
  • 9. Asokan, R., Puvanakrishnan, R., Ravichan- dran, L.V., Kokila, V., Reddy, G.K. & Dhar, S.C. (1993) Purification and characterization of collagens from rat fibrosarcoma induced by 3-methylcholanthrene. Mol Cell Biochem. 121, 99-107.
  • 10. Bańkowski, E., Sobolewski, K., Ayad, S., Gadher, S. & Woolley, D.E. (1994) Rat fibrosarcoma as a source of stable co-polymer of type I and type III collagens. Pathobiology 62, 160-164.
  • 11. Prockop, D.W. & Udenfriend, S. (1960) A spe­cific method for analysis of hydroxyproline in tissues and urine. Anal. Biochem. 1,228-239.
  • 12. Murata, K., Moteyama, T. & Kotake, C. (1986) Changes of collagen types in various layers of the human aorta and their changes with the atherosclerotic process. Atherosclerosis 60, 251-262.
  • 13. Bańkowski, E., Sobolewski, K., Romanowicz, L., Chyczewski, L. & Jaworski, S. (1996) Colla­gen and glycosaminoglycans of Wharton's jelly and their alterations in EPH-gestosis. Eur. J. Obst. Gyn. Reprod. Biol. 66,109-117.
  • 14. Cecho wska-Pasko, M., Pałka, J. & Bańkowski, E. (1996) Decrease in the glycosaminoglycan content in the skin of diabetic rats. The role of IGF-1, IGF-binding proteins and proteolytic ac­tivity. Moi Cell Biochem. 154, 1-8.
  • 15. Snow, A.D., Kisilevsky, R.. Stephens, C.H. & Anastassiades, T. (1987) Electrophoresis of glycosaminoglycans isolated from normal hu­man plasma. Direct evidence for the presence of a heparin-like molecule. Biomed. Biochim. Acta 46, 537-546.
  • 16. Carney, S.L. (1986) Proteoglycans. Proteogly­can constituent analytical techniques. The Elson-Morgan assay for hexosamine; in Carbo­hydrate Analysis. A practical Approach (Chap­lin, M.F., Kennedy, J.F., eds.) pp. 97-142, JRL Press, Oxford-Washington.
  • 17. Bitter, T. & Muir, H.M. (1962) A modified uronic acid carbazole reaction. AnaL Biochem. 4, 330-334.
  • 18. Elliott, R.J. (1996) The Fastin Elastin Assay, 2nd edn., Biocolor Ltd., Belfast.
  • 19. Woolley, D.E. (1984) Collagenolytic mecha­nism in tumor cell invasion. Cancer Metastasis Rev. 3, 361-372.
  • 20.Iozzo, R.V. (1998) Matrix proteoglycans: From molecular design to cellular function. Annu. Rev. Biochem. 67, 609-652.
  • 21. Taipale, J. & Keski-Oja, J. (1997) Growth fac­tors in the extracellular matrix. FASEBJ. 11, 51-59.
  • 22.Imai, K., Hiramatsu, A., Fukushima, D., Pierschbacher, M.D. & Okada, Y. (1997) Deg­radation of decorin by matrix metallo- proteinases: Identification of the cleavage sites, kinetics analyses and transforming growth factor-beta 1 release. Biochem. J. 322, 809-814.
  • 23. Kresse, H., Hausser, H., Schonherr, E. & Bittner, K. (1994) Biosynthesis and interac­tions of small chondroitin/ dermatan sulphate proteoglycans. Eur. J. Clin. Chem. Clin. Biochem. 32, 259-264. 947
  • 24. Kjellen, L. & Lindahl, V. (1991) Proteoglycans: Structures and interactions. Annu. Rev. Biochem. 60, 443-475.

Typ dokumentu

Bibliografia

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