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J. Biochem, 1980, Vol. 87, No. 4 1037-1041
© 1980 Japanese Biochemical Society

research-article

The Effect of Temperature on a "History" Phenomenon in Collagen Fibril Formation In Vitro

Evidence for Multiple Processes in Nucleation

Toshihiko HAYASHI

Department of Tissue Physiology, Medical Research Institute, Tokyo Medical and Dental University Kandasurugadai, Chiyoda-ku, Tokyo 101

Collagen fibril formation in vitro has been explained by resolving the process into nucleation and growth. The collagen fibrils formed in vitro at 37°C from pepsin-treated calf skin collagen went back into solution with no turbidity. The redissolved solution showed a faster formation of the fibrils upon reincubation at 37°C than a solution not subjected to the prior formation of the fibrils. This "history" phenomenon can be explained by assuming the presence of aggregates which did not dissociate into monomers. The history phenomenon was also observed at 29°C, where the time for the nucleation (which was quite distinct from the growth step) was much longer than at 37°C. Only the nucleation, not the growth step, became faster after previous formation of the fibrils. However, the nucleation time was not shortened beyond a certain limit either by prolonged incubation of the fibrils or by increased concentration of collagen. The collagen solution obtained by dissolution of the fibrils formed in vitro at 37°C did not show faster nucleation upon incubation at 29°C but rather retardation. The solution obtained by dissolution of the fibrils formed at 29°C also failed to show faster formation of the fibrils upon incubation at 37°C. The findings suggest that aggregates possibly remaining in the redissolved solution did not necessarily function as nuclei. The structure of the aggregates or the function of nuclei has a temperature specificity. Nucleation in collagen fibril formation in vitro involves at least two different processes; aggregation of monomers and conversion of the aggregates into nuclei.


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R. Jakobsen, L. Brown, T. Hutson, D. Fink, and A Veis
Intermolecular interactions in collagen self-assembly as revealed by Fourier transform infrared spectroscopy
Science, June 17, 1983; 220(4603): 1288 - 1290.
[Abstract] [PDF]


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