Different architectures of the collagen fibril: morphological aspects and functional implications.
Several tissues known to contain collagen fibrils with a 'helical' arrangement were studied by t.e.m. and freeze-fracture. In all the tissues examined, the diameter of the collagen fibrils appeared to be tissue-specific and fairly constant within the same tissue. No statistical differences, on the contrary, were detectable in the coiling angle which appeared similar in all the tissues and independent of both diameter and age of the fibril. Rat tail tendon was also examined under the same technical conditions and showed collagen fibrils of large and very heterogeneous diameter and with a consistent 'straight' arrangement. These data seem to suggest that the 'helical' and 'straight' arrangements may actually identify different types of collagen fibrils. The authors discuss the possible functional significance of these arrangements and present two hypotheses on the three-dimensional structure of the 'helical' fibril.
Raspanti
M
M
Istituto di Anatomia Umana, Bologna, Italy.
Ottani
V
V
Ruggeri
A
A
D000818:Animals; D001011:Aorta / Q000737:chemistry; D002417:Cattle; D003094:Collagen / Q000737:chemistry* / Q000648:ultrastructure; D005614:Freeze Fracturing; D008854:Microscopy, Electron; D008958:Models, Molecular; D009900:Optic Nerve / Q000737:chemistry; D011487:Protein Conformation; D051381:Rats; D012867:Skin / Q000737:chemistry; D013623:Tail; D013710:Tendons / Q000737:chemistry
D003094:Collagen