Changes in thermal stability and microunfolding pattern of collagen helix resulting from the loss of α2(I) chain in osteogenesis imperfecta murine

Journal of Molecular Biology

Volumn 331, Issue 1, 2003, Pages 191-200

  Kuznetsova, Natalia V ^a   McBride Jr , Daniel J ^b   Leikin, Sergey ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

Author keywords

Collagen; Microunfolding; Osteogenesis imperfecta; Thermal stability

Indexed keywords

AMINO ACID; COLLAGEN TYPE 1; CYANOGEN BROMIDE; PEPTIDE;

ALPHA CHAIN; AMINO ACID ANALYSIS; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; DENATURATION; ENZYME DEGRADATION; GENE MUTATION; HIGH TEMPERATURE; HOMOZYGOSITY; MOLECULAR DYNAMICS; MOUSE; NONHUMAN; OSTEOGENESIS IMPERFECTA; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN PROCESSING; TENDON; THERMOSTABILITY; WILD TYPE;

MURINAE;

EID: 0037485827     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00715-0     Document Type: Article

References (22)

1. Ramirez F. Organization and evolution of the fibrillar collagen genes. Olsen B.R., Nimni M.E. Collagen. vol. 4:1989;21-30 CRC Press, Boca Raton, FL.
2. Kelly J., Tanaka S., Hardt T., Eikenberry E.F., Brodsky B. Fibril-forming collagens in lamprey. J. Biol. Chem. 263:1988;980-987.
3. Brodsky B., Eikenberry E.F. Characterization of fibrous forms of collagen. Methods Enzymol. 82:1982;127-174.
4. Nicholls A.C., Osse G., Schloon H.G., Lenard H.G., Deak S., Myers J.C., et al. The clinical features of homozygous α2(I) collagen deficient osteogenesis imperfecta. J. Med. Genet. 21:1984;257-262.
5. Dickson L.A., Pihlajaniemi T., Deak S., Pope F.M., Nicholls A., Prockop D.J., Myers J.C. Nuclease S1 mapping of a homozygous mutation in the carboxyl-propeptide-coding region of the pro alpha 2(I) collagen gene in a patient with osteogenesis imperfecta. Proc. Natl Acad. Sci. USA. 81:1984;4524-4528.
6. Nicholls A.C., Valler D., Wallis S., Pope F.M. Homozygosity for a splice site mutation of the COL1A2 gene yields a non-functional pro(alpha)2(I) chain and an EDS/OI clinical phenotype. J. Med. Genet. 38:2001;132-136.
7. Sasaki T., Arai K., Ono M., Yamaguchi T., Furuta S., Nagai Y. Ehlers-Danlos syndrome. A variant characterized by the deficiency of pro alpha 2 chain of type I procollagen. Arch. Dermatol. 123:1987;76-79.
8. Hata R., Kurata S., Shinkai H. Existence of malfunctioning pro alpha2(I) collagen genes in a patient with a pro alpha 2(I)-chain-defective variant of Ehlers-Danlos syndrome. Eur. J. Biochem. 174:1988;231-237.
9. Chipman S.D., Sweet H.O., McBride D.J., Davisson M.T., Marks S.C., Shuldiner A.R., et al. Defective pro(2(I) collagen synthesis in a recessive mutation in mice: a model of human osteogenesis imperfecta. Proc. Natl Acad. Sci. USA. 90:1993;1701-1705.
10. McBride D.J., Choe V., Shapiro J.R., Brodsky B. Altered collagen structure in mouse tail tendon lacking the α2(I) chain. J. Mol. Biol. 270:1997;275-284.
11. Misof K., Landis W.J., Klaushofer K., Fratzl P. Collagen from the osteogenesis imperfecta mouse model (oim) shows reduced resistance against tensile stress. J. Clin. Invest. 100:1997;40-45.
12. Vouyouka A.G., Pfeiffer B.J., Liem T.K., Taylor T.A., Mudaliar J., Phillips C.L. The role of type I collagen in aortic wall strength with a homotrimeric. J. Vasc. Surg. 33:2001;1263-1270.
13. McBride D.J., Kadler K.E., Hojima Y., Prockop D.J. Self-assembly into fibrils of a homotrimer of type I collagen. Matrix. 12:1992;256-263.
14. Kuznetsova N., McBride D.J. Jr, Leikin S. Osteogenesis imperfecta murine: interaction between type I collagen homotrimers. J. Mol. Biol. 309:2001;807-815.
15. Miles C.A., Sims T.J., Camacho N.P., Bailey A.J. The role of the alpha2 chain in the stabilization of the collagen type I heterotrimer: a study of the type I homotrimer in oim mouse tissues. J. Mol. Biol. 321:2002;797-805.
16. Forlino A., Marini J.C. Osteogenesis imperfecta: prospects for molecular therapeutics. Mol. Gen. Metab. 71:2000;225-232.
17. Deak S.B., van der Rest M., Prockop D.J. Altered helical structure of a homotrimer α1(I) chains synthesized by fibroblasts from a variant of osteogensis imperfecta. Collagen Rel. Res. 5:1985;305-313.
18. Leikina E., Mertts M.V., Kuznetsova N., Leikin S. Type I collagen is thermally unstable at body temperature. Proc Natl Acad Sci. USA. 99:2002;1314-1318.
19. Privalov P.L. Stability of proteins. Proteins which do not present a single cooperative system. Advan. Protein Chem. 35:1982;1-104.
20. Ryhanen L., Zaragoza E.J., Uitto J. Conformational stability of type I collagen triple helix: evidence for temporary and local relaxation of the protein conformation using a proteolytic probe. Arch. Biochem. Biophys. 223:1983;562-571.
21. Kadler K.E., Hojima Y., Prockop D.J. Assembly of type I collagen fibrils denovo between 37-degrees and 41 degrees C. The process is limited by micro-unfolding of monomers. J. Biol. Chem. 263:1988;10517-10523.
22. Kuznetsova N., Chi S.L., Leikin S. Sugars and polyols inhibit fibrillogenesis of type I collagen by disrupting hydrogen-bonded water bridges between the helices. Biochemistry. 37:1998;11888-11895.