Abstract
It has been proved in three rodent species that in the insoluble collagen fraction which accumulates in skin collagen with age of the two categories of collagen present (collagen type I and collagen type II), their proportion alters in favour of collagen type I with the advancing age. Since it has also been shown that collagen type I is less resistant towards proteolytic cleavage than is collagen type III its accumulation can be explained either by rapidly advancing cross-linking of this collagen type or more likely by different proteosynthesis. The second alternative is preferred since a step-wise polymerization of collagen type III was also observed. No information revealing to what extent the lysine derived cross-linked can combine both collagen types is at present available. On the basis of this information the rapid decrease in insoluble collagen in very early ontogeny (rats below 8 weeks of age) is explained.
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