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cDNA Cloning and Characterization of Type II Procollagen α1 Chain in the Skate Raja kenojei

  • Hwang Jae-Ho (Mount Desert Island Biological Laboratory) ;
  • Yokoyama Yoshihiro (Department of Marine Bioscience, Faculty of Biotechnology, Fukui Prefectural University) ;
  • Mizuta Shoshi (Department of Marine Bioscience, Faculty of Biotechnology, Fukui Prefectural University) ;
  • Yoshinaka Reiji (Department of Marine Bioscience, Faculty of Biotechnology, Fukui Prefectural University)
  • Published : 2006.03.01

Abstract

We determined the partial cDNA of Type II procollagen ${\alpha}1$[pro-${\alpha}1$(II)] chain (1802 bp) of the skate Raja kenojei, which codes 581 amino acid residues. The partial structure of the pro-${\alpha}1$(II) chain consisted of a part of triple helical region (309 residues) and a C-domain (272 residues). Comparing the chain to other vertebrates showed relatively low homology (about 50%) at the amino acid level. However, eight Cys residues in the C-domain of the skate pro-${\alpha}1$(II) chain were conserved in common with those of other vertebrates. The skate pro-${\alpha}1$ (II) chain mRNA was detected by RT-PCR of various tissues, but was undetected in tissues containing Type II collagen. The low homology and unexpected expression pattern suggest the presence of another mRNA variant of the skate pro-${\alpha}1$(II) chain. The present study is the first report of the primary structure of pro-${\alpha}1$(II) chain in an elasmobranch.

Keywords

References

  1. Asahina, K., M. Obara and K. Yoshizato. 1999. Expression of genes of type I and type II collagen in the formation and development of the blastema of regenerating newt limb. Dev. Dyn., 216, 59-71 https://doi.org/10.1002/(SICI)1097-0177(199909)216:1<59::AID-DVDY8>3.0.CO;2-B
  2. Birk, D.E., J.M. Fitch, J.P. Babiarz and T.F. Linsenmayer. 1988. Collagen type I and type V are present in the same fibril in the avian corneal stroma. J. Cell Biol., 106, 999-1008 https://doi.org/10.1083/jcb.106.3.999
  3. Bornstein, P. and H. Sage. 1980. Structurally distinct collagen types. Annu. Rev. Biochem., 49, 957-1003 https://doi.org/10.1146/annurev.bi.49.070180.004521
  4. Burgeson, R.E. and D.W. Hollister. 1979. Collagen heterogeneity in human cartilage: Identification of several new collagen chains. Biochem. Biophys. Res. Commun., 87, 1124-1131 https://doi.org/10.1016/S0006-291X(79)80024-8
  5. Capaldi, M.J. and J.A. Chapman. 1982. The C-terminal extrahelical peptide of type I collagen and its role in fibrillogenesis in vitro. Biopolymers, 21, 2291-2313 https://doi.org/10.1002/bip.360211115
  6. Deak, F., W.S. Argraves, I. Kiss, K.J. Sparks and P.F. Goetinck. 1985. Primary structure of the telopeptide and a portion of the helical domain of chicken type II procollagen as determined by DNA sequence analysis. Biochem. J., 229, 189-196 https://doi.org/10.1042/bj2290189
  7. Dion, A.S. and J.C. Myers. 1987. COOH-terminal propeptides of the major human procollagens. Structural, functional and genetic comparisons. J. Mol. Biol., 193, 127-143 https://doi.org/10.1016/0022-2836(87)90632-2
  8. Du, F., G.M. Acland and J. Ray. 2000. Cloning and expression of type II collagen mRNA: evaluation as a candidate for canine oculo-skeletal dysplasia. Gene, 255, 307-316 https://doi.org/10.1016/S0378-1119(00)00324-3
  9. Fichard, A., J.P. Kleman and F. Ruggiero. 1995. Another look at collagen V and XI molecules. Matrix Biol., 14, 515-531 https://doi.org/10.1016/S0945-053X(05)80001-0
  10. Keene, D. R., L.Y. Sakai, H.P. Bachinger and R.E. Burgeson. 1987. Type III collagen can be present on banded collagen fibrils regardless of fibril diameter. J. Cell Biol., 105, 2393-2402 https://doi.org/10.1083/jcb.105.5.2393
  11. Krebsbach, P.H., K. Nakata, S.M. Bernier, O. Hatano, T. Miyashita, C.S. Rhodes and Y. Yamada. 1996. Identification of a minimum enhancer sequence for the type II collagen gene reveals several core sequence motifs in common with the link protein gene. J. Biol. Chem., 271, 4298-4303 https://doi.org/10.1074/jbc.271.8.4298
  12. Kuhn, K. 1987. The Classical Collagens: Types I, II, and III. In: Structure and Function of Collagen Types, Mayne, R. and R.E. Burgeson, eds. Academic Press, NY, 1-42
  13. Linsenmayer, T.F. and C.D. Little. 1978. Embryonic neural retina collagen: in vitro synthesis of high molecular weight forms of type II plus a new genetic type. Proc. Natl. Acad. Sci., U.S.A., 75, 3235-3239
  14. Metsaranta, M., D. Toman, B. de Crombrugghe and E. Vuorio. 1991. Mouse type II collagen gene. Complete nucleotide sequence, exon structure, and alternative splicing. J. Biol. chem., 266, 16862-16869
  15. Miller, E.J. 1972. Structural studies on cartilage collagen employing limited cleavage and solubilization with pepsin. Biochemistry, 11, 4903-4909 https://doi.org/10.1021/bi00776a005
  16. Miosge, N., K. Waletzko, C. Bode, F. Quondamatteo, W. Schultz and R. Herken. 1998. Light and electron microscopic in-situ hybridization of collagen type I and type II mRNA in the fibrocartilaginous tissue of late-stage osteoarthritis. Osteoarthr. Cartil., 6, 278-85 https://doi.org/10.1053/joca.1998.0121
  17. Newsome, D.A., T.F. Linsenmayer and R.L. Trelstad. 1976. Vitreous body collagen. Evidence for a dual origin from the neural retina and hyalocytes. J. Cell Biol., 71, 59-67 https://doi.org/10.1083/jcb.71.1.59
  18. Pesciotta, D.M., L.A. Dickson, A.M. Showalter, E.F. Eikenberry, B. de Crombrugghe, P.P. Fietzek and B.R. Olsen. 1981. Primary structure of the carbohydrate-containing regions of the carboxyl propeptides of type I procollagen. FEBS Lett., 125, 170-174 https://doi.org/10.1016/0014-5793(81)80711-9
  19. Proudfoot, N.J. and G.G. Brownlee. 1976. 3' non-coding region sequences in eukaryotic messenger RNA. Nature, 263, 211-214 https://doi.org/10.1038/263211a0
  20. Richard, D.W. and G.R. Dodge. 1997. Cloning of equine type II procollagen and the modulation of its expression in cultured equine articular chondrocytes. Matrix Biol., 16, 59-64 https://doi.org/10.1016/S0945-053X(97)90073-1
  21. Rosenbloom, J., R. Endo and M. Harsch. 1976. Termination of procollagen chain synthesis by puromycin Evidence that assembly and secretion require a COOH-terminal extension. J. Biol. chem., 251, 2070-2076
  22. Ruoslahti, E. and M.D. Pierschbacher. 1986. Arg-Gly-Asp: a versatile cell recognition signal. Cell, 44, 517-518 https://doi.org/10.1016/0092-8674(86)90259-X
  23. Sandell, L.J., N. Morris, J.R. Robbins and M.B. Goldring. 1991. Alternatively spliced type II procollagen mRNAs define distinct populations of cells during vertebral development: differential expression of the amino-propeptide. J. Cell Biol., 114, 1307-1319 https://doi.org/10.1083/jcb.114.6.1307
  24. Sandell, L.J., H.L. Prentice, D. Kravis and W.B. Upholt. 1984. Structure and sequence of the chicken type II procollagen gene. Characterization of the region encoding the carboxyl-terminal telopeptide and propeptide. J. Biol. Chem., 259, 7826-7834
  25. Strausberg, R.L., E.A. Feingold, L.H. Grouse, J.G. Derge, R.D. Klausner, F.S. Collins, L. Wagner, C.M. Shenmen, G.D. Schuler, S.F. Altschul, B. Zeeberg, K.H. Buetow, C.F. Schaefer, N.K. Bhat, R.F. Hopkins, H. Jordan, T. Moore, S.I. Max, J. Wang, F. Hsieh, L. Diatchenko, K. Marusina, A.A. Farmer, G.M. Rubin, L. Hong, M. Stapleton, M.B. Soares, M.F. Bonaldo, T.L. Casavant, T.E. Scheetz, M.J. Brownstein, T.B. Usdin, S. Toshiyuki, P. Carninci, C. Prange, S.S. Raha, N.A. Loquellano, G.J. Peters, R.D. Abramson, S.J. Mullahy, S.A. Bosak, P.J. McEwan, K.J. McKernan, J.A. Malek, P.H. Gunaratne, S. Richards, K.C. Worley, S. Hale, A.M. Garcia, L.J. Gay, S.W. Hulyk, D.K. Villalon, D.M. Muzny, E.J. Sodergren, X. Lu, R.A. Gibbs, J. Fahey, E. Helton, M. Ketteman, A. Madan, S. Rodrigues, A. Sanchez, M. Whiting, A. Madan, A.C. Young, Y. Shevchenko, G.G. Bouffard, R.W. Blakesley, J.W. Touchman, E.D. Green, M.C. Dickson, A.C. Rodriguez, J. Grimwood, J. Schmutz, R.M. Myers, Y.S. Butterfield, M.I. Krzywinski, U. Skalska, D.E. Smailus, A. Schnerch, J.E. Schein, S.J. Jones and M.A. Marra. 2002. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci., U.S.A., 99, 16899-16903
  26. Su, M.W., H.R. Suzuki, J.J. Bieker, M. Solursh and F. Ramirez. 1991. Expression of two nonallelic type II procollagen genes during Xenopus laevis embryogenesis is characterized by stage-specific production of alternatively spliced transcripts. J. Cell Biol., 115, 565-575 https://doi.org/10.1083/jcb.115.2.565
  27. Vaughan, L., M. Mendler, S. Huber, P. Bruckner, K.H. Winterhalter, M.I. Irwin and R. Mayne. 1988. D-periodic distribution of collagen type IX along cartilage fibrils. J. Cell Biol., 106, 991-997 https://doi.org/10.1083/jcb.106.3.991
  28. von der Mark, K. and H. von der Mark. 1977. Immunological and biochemical studies of collagen type transition during in vitro chrondrogenesis of chick limb mesodermal cells. J. Cell Biol., 73, 736-747 https://doi.org/10.1083/jcb.73.3.736
  29. Yan, Y.L., K. Hatta, B. Riggleman and J.H. Postlethwait. 1995. Expression of a type II collagen gene in the zebrafish embryonic axis. Dev. Dyn., 203, 363-376 https://doi.org/10.1002/aja.1002030308