Elastin: structure, properties and metabolism

• Autorzy: Gacko M.
• Języki publikacji: EN

Abstrakty

EN

Soluble tropoelastin is a precursor of elastin. It is transported by elastin binding protein (EBP) into intercellular space. The EBP-tropoelastin complex undergoes disintegration in the intercellular space. EBP returns to the cell and tropoelastin joins with microfibril proteins. Lysine residues of tropoelastin undergo oxidative deamination. Desmosine, isodesmosine and cross bonds arise. Thus tropoelastin loses solubility and transforms to elastin. The elastic fiber created consists of microfibrils on the periphery and an elastin core inside. Elastin provides blood vessels, lungs, cartilage and skin with the ability to reverse deformations. A decrease of elastin content or changes in this protein structure results in pathological conditions such as aneurysms and pulmonary emphysema.

Słowa kluczowe

EN

metabolism; tropoelastin; structure; fibrillin; elastin; binding protein; elastase

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2000
• Tom: 05
• Numer: 3
• Opis fizyczny: p.327-348,fig.

Twórcy

autor

Gacko M.

• Medical University of Bialystok, Marii Sklodowskiej-Curie 24A, 15-276 Bialystok, Poland

Bibliografia

• 1. Drożdż, M., Kucharz, E., Olczyk, K. Struktura i metabolizm elastyny w stanach prawidłowych i patologicznych. Post. Hig. Med. Dośw. 5 (1976) 709-734.
• 2. Sauvage, M., Jacob, M. P., Osbome-Pellegrin, M. Aortic elastin and collagen content and synthesis in two strains of rats with different susceptibilities to rupture of the internal elastin lamina. J. Vasc. Res. 34 (1997) 126-136.
• 3. Watanable, M., Sawai, T., Nagura, H., Suyama, K. Age-related alternation of cross-linking amino acids of elastin in human aorta. Thoku J. Exp. Med. 180 (1996) 115-130.
• 4. Wrenn, D. S., Mecham, R. P. Immunology of elastin. Meth. Enzymol. 144 (1987) 246-259.
• 5. Raju, K., Anwar, R. A. Primary structure of bovine elastin a, b and c deduced from the sequence of cDNA clones. J. Biol. Chem. 262 (1987) 5755-5762.
• 6. Gibson, M., Kumaratilake, J. S., Cleary. E. G. The protein components of the 12 nm microfibrills of elastic and nonelastic tissue. J. Biol. Chem. 264 (1989) 4590-4598.
• 7. Hinek, A., Hinek, A. Funkcje biologiczne receptora elastynowego. Post. Biol. Kom. 23 (1996) 243-259.
• 8. Reinhard, D. P., Keene, D. R., Corson, G. M., Poschl, E., Bachinger, H. P., Gambee, J. E., Sakai, L. Y. Fibrillin-1: organization in microfibrils and structural properties. J. Mol. Biol. 258 (1996) 104-116.
• 9. Sakai, L. Y., Keene, D. R., Enqvall, E. Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils. J. Cell. Biol. 103 (1986) 2499-2509.
• 10. Gibson, M. A, Sandberg, L. B., Gross, Le, Cleary, E. G. Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discerted component of the elastin-associated microfibrils. J. Biol.Chem. 266 (1991) 7596-7601.
• 11. Horrigan, S. K., Rich, C. B., Streeten, B. W., Li, Z. Y., Foster, J. A. Characterization of an associated microfibrilar protein through recombinant DNA techniques. J. Biol. Chem. 267 (1992) 10087-10095.
• 12. Pereira, L, D’Alessio, M., Ramirez, F., Lynch, J. R., Sykes, B., Pangilinan, T., Bonadio, J. Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome. Hum. Molec. Gen. 2 (1993) 961-968.
• 13. Brown-Augsburger, P., Broekelmann, T., Rosenbloom, J., Mecham R. P. Functional domains on elastin and microfibril-associated glycoprotein involved in elastic fibre assembly. Biochem. J. 318 (1996) 149-155.
• 14. Rosenbloom, J., Abrams, W. R., Mecham, R. Q. Extracellular matrix. 4. Elastin fiber. FASEB J. 7 (1993) 1208-1218
• 15. Sandberg, L. B., Soskel, N. T., Leslie, J. G. Elastin structure, biosynthesis and relation to disease states. N. Engl. J. Med. 304 (1981) 566-579.
• 16. Hornebeck, W., Brechemier, D., Bellon, G., Adnet, J. J., Robert, L. Biological significance of elastase-like enzymes in arteriosclerosis and human breast cancer. In: Proteinases and tumor invasion. (Strauli, P., Barret A. J., Baici, A., Eds.), Raven Press, New York (1980) 117-141.
• 17. Burton, A. C. Relation of structure to function of tissues of the wall of blood vessels. Physiol. Rev. 34 (1954) 619-642.
• 18. Mecham, R., Broekelmann, T. J., Fliszar, C. J., Shapiro, S. D., Welgus, H. G., Senior, R. M. Elastin degradation by matrix metalloproteinases. J. Biol. Chem. 272 (1997) 18071-18076.
• 19. Stone, P. J., Franzblam, C., Kagan, H. M. Proteolysis in insoluble elastin. Meth. Enzymol. 82 A (1982) 588-605.
• 20. Werb, Z., Banda, M. J., McKerrow, J. H., Sandhaus, R. A. Elastases and elastin degradation. J. Invest. Dermatol. 79 suppl.l (1982) 154-159.
• 21. Shapiro, S. D. The pathogenesis of emphysema: the elastase: antielastase hypothesis 30 years later. Proc. Ass. Am. Physic. 107 (1995) 346-352.
• 22. Okamoto, T., Akaike, T., Suga, M., Tanase, S., Horie, H., Miyujima, S., Ando, M., Ichinose, Y., Maeda, H. Activation of human matrix metalloproteinases by various bacterial proteinases J. Biol. Chem. 272 (1997) 6059-6066.
• 23. Gacko, M. Patogeneza tętniaka aorty. Pol. Przegl. Chir. 69 (1997) 94-101.
• 24. Robert, L., Robert, A. M. Elastin, elastase and arteriosclerosis. Front. Matrix Biol. 8 (1980) 130-173
• 25. Tomaszewski, J., Hanzlik, J., Grzywa, M., Zawiślak, H., Stępień, A. Badania nad składem chemicznym ściany naczyniowej. XIV. Kolagen i elastyna ściany ludzkiej tętnicy głównej w procesie starzenia fizjologicznego. Pol. Arch. Med. Wewn. 55 (1976) 557-566.
• 26. Maeda, H., Yamamoto, T. Pathogenic mechanisms induced by microbial proteases in microbial infections. Biol. Chem. Hoppe-Seyler 377 (1996) 217-226.
• 27. Gmiński, J., Drożdż, M. Przeciwciała antyelastynowe - powstawanie, występowanie, znaczenie diagnostyczne. Diagn. Lab. 25 (1989) 16-21.
• 28. Velebny, V., Ledvina, M. Biological effects of elastin peptides. Sbor. Ved. Praci. LF UK Hradec Kralove 31 (1988) 7-18.
• 29. Katemba, J. M. Experimental arterial thrombosis formation in vivo by proteolitic enzyme perfusion and the role of elastin layer. Surgery 73 (1973) 438-443.
• 30. Sekiya, K., Okuda, H. Inhibitory action of soluble elastin on tromboxan B2 formation in blood platelets. Biochim. Biophys. Acta 797 (1984) 348-453.