Molecular structure and functional morphology of echinoderm collagen fibrils.
The collagenous tissues of echinoderms, which have the unique capacity to rapidly and reversibly alter their mechanical properties, resemble the collagenous tissues of other phyla in consisting of collagen fibrils in a nonfibrillar matrix. Knowledge of the composition and structure of their collagen fibrils and interfibrillar matrix is thus important for an understanding of the physiology of these tissues. In this report it is shown that the collagen molecules from the fibrils of the spine ligament of a sea-urchin and the deep dermis of a sea-cucumber are the same length as those from vertebrate fibrils and that they assemble into fibrils with the same repeat period and gap/overlap ratio as do those of vertebrate fibrils. The distributions of charged residues in echinoderm and vertebrate molecules are somewhat different, giving rise to segment-long-spacing crystallites and fibrils with different banding patterns. Compared to the vertebrate pattern, the banding pattern of echinoderm fibrils is characterized by greatly increased stain intensity in the c3 band and greatly reduced stain intensity in the a3 and b2 bands. The fibrils are spindle-shaped, possessing no constant-diameter region throughout their length. The shape of the fibrils is mechanically advantageous for their reinforcing role in a discontinuous fiber-composite material.
Trotter
J A
JA
Department of Anatomy, University of New Mexico School of Medicine, Albuquerque 87131.
Thurmond
F A
FA
Koob
T J
TJ
D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D004447:Echinodermata / Q000737:chemistry*; D008854:Microscopy, Electron; D015394:Molecular Structure; D012616:Sea Cucumbers; D012617:Sea Urchins
D003094:Collagen