Cross-Linking of Collagen

The formation of collagen cross-links is attributable to the presence of two aldehyde-containing amino acids which react with other amino acids in collagen to generate difunctional, trifunctional, and tetrafunctional cross-links. A necessary prerequisite for the development of these cross-links is that the collagen molecules be assembled in the naturally occurring fibrous polymer. Once this condition is met, cross-linking occurs in a spontaneous, progressive fashion. The chemical structures of the cross-links dictate that very precise intermolecular alignments must occur in the collagen polymer. This seems to be a function of each specific collagen because the relative abundance of the different cross-links varies markedly, depending upon the tissue of origin of the collagen.

[1]  E. J. Miller.  Collagen cross-linking: identification of two cyanogen bromide peptides containing sites of intermolecular cross-link formation in cartilage collagen. , 1971, Biochemical and biophysical research communications.

[2]  G. Martin,et al.  Collagen cross-linking. Enzymatic synthesis of lysine-derived aldehydes and the production of cross-linked components. , 1970, The Journal of biological chemistry.

[3]  M. Nimni,et al.  Identification of stable intermolecular crosslinks present in reconstituted native collagen fibers. , 1972, Biochemical and biophysical research communications.

[4]  P. Bornstein,et al.  The nature and location of intramolecular cross-links in collagen. , 1966, Proceedings of the National Academy of Sciences of the United States of America.

[5]  M. Glimcher,et al.  Comparative biochemistry of collagen crosslinks: reducible bonds in invertebrate collagens. , 1971, Biochimica et biophysica acta.

[6]  M. Nimni,et al.  Synthesis of aldehydes and their interactions during the in vitro aging of collagen. , 1971, Biochemistry.

[7]  P. Gallop,et al.  Collagen crosslinks: isolation of reduced N -hexosylhydroxylysine from borohydride-reduced calf skin insoluble collagen. , 1972, Archives of biochemistry and biophysics.

[8]  G. Mechanic,et al.  Isolation of peptides containing the cross-link, hydroxylysinonorleucine, from reconstituted collagen fibrils. , 1970, Biochemistry.

[9]  A. Bailey,et al.  Age-related changes in collagen: the identification of reducible lysine-carbohydrate condensation products. , 1972, Biochemical and biophysical research communications.

[10]  G. Martin,et al.  On the inhibition of lysyl oxidase by -aminopropionitrile. , 1972, Biochemical and biophysical research communications.

[11]  G. Mechanic.  Crosslinking of collagen in a heritable disorder of connective tissue: Ehlers-Danlos syndrome. , 1972, Biochemical and biophysical research communications.

[12]  A. Kang,et al.  The in vitro formation of intermolecular cross-links in chick skin collagen. , 1970, Biochemical and biophysical research communications.

[13]  M. Shimokomaki,et al.  Age related changes in the reducible cross‐links of collagen , 1971, FEBS letters.

[14]  A. Kang,et al.  In vitro formation of intermolecular crosslinks in chick skin collagen. II. Kinetics. , 1970, Biochemical and biophysical research communications.

[15]  M. Tanzer.  Intermolecular cross-links in reconstituted collagen fibrils. Evidence for the nature of the covalent bonds. , 1968, The Journal of biological chemistry.

[16]  A. J. Bailey.  Comparative studies on the nature of the crosslinks in the collagen of various fish tissues. , 1970, Biochimica et biophysica acta.

[17]  Andrea Szalavetz,et al.  Hungarian Academy of Sciences , 1952, Nature.

[18]  M. Tanzer.  Collagen reduction by sodium borohydride: effects of reconstitution, maturation and lathyrism. , 1968, Biochemical and biophysical research communications.

[19]  M. Nimni,et al.  Characterization of the aldehydes present on the cyanogen bromide peptides from mature rat skin collagen. , 1971, Biochemistry.

[20]  W. Traub,et al.  The chemistry and structure of collagen. , 1971, Advances in protein chemistry.

[21]  P. Gallop,et al.  Structure of two histidine-containing crosslinks from collagen. , 1973, The Journal of biological chemistry.

[22]  P. Gallop,et al.  The nature of crosslinking in collagens from mineralized tissues. , 1971, Biochemical and biophysical research communications.

[23]  A. Kang.  Studies on the location of intermolecular cross-links in collagen. Isolation of a CNBr peptide containing -hydroxylysinonorleucine. , 1972, Biochemistry.

[24]  P. Bornstein,et al.  The nature of the intramolecular cross-links in collagen. The separation and characterization of peptides from the cross-link region of rat skin collagen. , 1966, Biochemistry.

[25]  A. Bailey,et al.  Embryonic skin collagen. Replacement of the type of aldimine crosslinks during the early growth period , 1972, FEBS letters.

[26]  A. Shuttleworth,et al.  A comparison between the reducible intermolecular crosslinks of the collagens from mature dermis and young dermal scar tissue of the guinea pig. , 1972, Biochemical and biophysical research communications.

[27]  A. Bailey.  Comparative studies on the nature of the cross‐links stabilizing the collagen fibres of invertebrates, cyclostomes and elasmobranchs , 1971, FEBS letters.

[28]  R. Lent,et al.  The nature of the intramolecular cross-link in collagen. , 1969, Biochemical and biophysical research communications.

[29]  J. Gross.  Ihermal Denaturation of Collagen in the Dispersed and Solid State , 1964, Science.

[30]  A J Bailey,et al.  Isolation and structural identification of a labile intermolecular crosslink in collagen. , 1968, Biochemical and biophysical research communications.

[31]  G. Mechanic,et al.  Quantitative changes of bone collagen crosslinks and precursors in vitamin D deficiency. , 1972, Biochemical and biophysical research communications.