Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1980 Aug 15;190(2):229–237. doi: 10.1042/bj1900229

Studies on the assembly of the rat lens capsule. Biosynthesis of a cross-linked collagenous component of high molecular weight.

J G Heathcote, A J Bailey, M E Grant
PMCID: PMC1162086  PMID: 7470049

Abstract

1. Intact rat lenses in tissue culture synthesize hydroxy[3H]proline-containing polypeptides of apparent mol.wt. approx. 180000, which become assembled into aggregates of higher molecular weight with time. 2. Both the 180000-mol.wt. species and the aggregates are components of the deoxycholate-insoluble base-membrane matrix. 3. Formation of the high-molecular-weight aggregate is accompanied by the biosynthesis of the reducible hydroxylysine-derived cross-link hydroxylysino-5-oxo-norleucine. 4. Hydroxylysino-5-oxonorleucine and dehydrohydroxylysinonorleucine are the major reducible cross-links present in intact foetal and 1-month-old calf lens capsules.

Full text

PDF
236

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bailey A. J., Robins S. P., Balian G. Biological significance of the intermolecular crosslinks of collagen. Nature. 1974 Sep 13;251(5471):105–109. doi: 10.1038/251105a0. [DOI] [PubMed] [Google Scholar]
  2. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  3. Cheah K. S., Grant M. E., Jackson D. S. Translation of embryonic-chick tendon procollagen messenger ribonucleic acid in two cell-free protein-synthesizing systems. Biochem J. 1979 Jul 15;182(1):81–93. doi: 10.1042/bj1820081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Crouch E., Bornstein P. Characterization of a type IV procollagen synthesized by human amniotic fluid cells in culture. J Biol Chem. 1979 May 25;254(10):4197–4204. [PubMed] [Google Scholar]
  5. Fisher R. F., Wakely J. The elastic constants and ultrastructural organization of a basement membrane (lens capsule). Proc R Soc Lond B Biol Sci. 1976 Jun 30;193(1113):335–358. doi: 10.1098/rspb.1976.0051. [DOI] [PubMed] [Google Scholar]
  6. Harwood R., Merry A. H., Woolley D. E., Grant M. E., Jackson D. S. The disulphide-bonded nature of procollagen and the role of the extension peptides in the assembly of the molecule. Biochem J. 1977 Feb 1;161(2):405–418. doi: 10.1042/bj1610405. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Heathcote G., Sear C. H., Grant M. E. Studies on the assembly of the rat lens capsule. Biosynthesis and partial characterization of the collagenous components. Biochem J. 1978 Oct 15;176(1):283–294. doi: 10.1042/bj1760283. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Howard B. V., Macarak E. J., Gunson D., Kefalides N. A. Characterization of the collagen synthesized by endothelial cells in culture. Proc Natl Acad Sci U S A. 1976 Jul;73(7):2361–2364. doi: 10.1073/pnas.73.7.2361. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hudson B. G., Spiro R. G. Fractionation of glycoprotein components of the reduced alkylated renal glomerular basement membrane. J Biol Chem. 1972 Jul 10;247(13):4239–4247. [PubMed] [Google Scholar]
  10. Hudson B. G., Spiro R. G. Studies on the native and reduced alkylated renal glomerular basement membrane. Solubility, subunit size, and reaction with cyanogen bromide. J Biol Chem. 1972 Jul 10;247(13):4229–4238. [PubMed] [Google Scholar]
  11. Juva K., Prockop D. J. Modified procedure for the assay of H-3-or C-14-labeled hydroxyproline. Anal Biochem. 1966 Apr;15(1):77–83. doi: 10.1016/0003-2697(66)90249-1. [DOI] [PubMed] [Google Scholar]
  12. Kefalides N. A., Alper R., Clark C. C. Biochemistry and metabolism of basement membranes. Int Rev Cytol. 1979;61:167–228. doi: 10.1016/s0074-7696(08)61998-1. [DOI] [PubMed] [Google Scholar]
  13. Kefalides N. A., Cameron J. D., Tomichek E. A., Yanoff M. Biosynthesis of basement membrane collagen by rabbit corneal endothelium in vitro. J Biol Chem. 1976 Feb 10;251(3):730–733. [PubMed] [Google Scholar]
  14. Kefalides N. A. Structure and biosynthesis of basement membranes. Int Rev Connect Tissue Res. 1973;6:63–104. doi: 10.1016/b978-0-12-363706-2.50008-8. [DOI] [PubMed] [Google Scholar]
  15. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  16. Laskey R. A., Mills A. D. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem. 1975 Aug 15;56(2):335–341. doi: 10.1111/j.1432-1033.1975.tb02238.x. [DOI] [PubMed] [Google Scholar]
  17. Meezan E., Hjelle J. T., Brendel K., Carlson E. C. A simple, versatile, nondisruptive method for the isolation of morphologically and chemically pure basement membranes from several tissues. Life Sci. 1975 Dec 1;17(11):1721–1732. doi: 10.1016/0024-3205(75)90119-8. [DOI] [PubMed] [Google Scholar]
  18. Moczar M., Moczar E., Robert L. Structural glycoprotein from the media of pig aorta. Aggregation of the S-carboxamidomethyl subunits. Biochimie. 1977;59(2):141–151. doi: 10.1016/s0300-9084(77)80285-x. [DOI] [PubMed] [Google Scholar]
  19. Robins S. P., Bailey A. J. The chemistry of the collagen cross-links. The mechanism of stabilization of the reducible intermediate cross-links. Biochem J. 1975 Aug;149(2):381–385. doi: 10.1042/bj1490381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Robins S. P., Shimokomaki M., Bailey A. J. The chemistry of the collagen cross-links. Age-related changes in the reducible components of intact bovine collagen fibres. Biochem J. 1973 Apr;131(4):771–780. doi: 10.1042/bj1310771. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Tanzer M. L., Kefalides N. A. Collagen crosslinks: occurrence in basement membrane collagens. Biochem Biophys Res Commun. 1973 Apr 2;51(3):775–780. doi: 10.1016/0006-291x(73)91382-x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES