Control of collagen fibril diameters in tissues.

It is proposed that radial growth of collagen fibrils, which takes place in all connective tissues to varying extents, according to the tensile stresses exerted on them, proceeds mainly by aggregation of protofibrils (approximately 10 nm) and existing fibrils. In young tissues, fibrils are prevented from making frequent intimate contacts which would lead to aggregation by abundant interfibrillar proteoglycan, that keeps the fibrils apart. Collagen fibrils are probably unable to fuse except when the molecules within them are packed in the same sense, i.e. fusing fibrils are parallel. The roughly equal numbers of parallel and antiparallel fibrils seen in several tissues must limit radial fibril growth in older tissues, where proteoglycan is usually less abundant. Possible origins of the balance of fibril polarities, which must be conserved after fibril nucleation on cell or non-cell templates, are analysed. The two controlling factors, ambient proteoglycan and fibril polarity, working against the tendency of fibrils to fuse, account for many features of the observed distributions of collagen fibril diameters in diverse tissues and at different ages.