Collagen fibril structure in lamprey.
X-ray diffraction and electron microscopy are used to compare the molecular and higher order structure of collagen fibrils in three tissues of the lamprey: the dermis, perinotochord and notochord sheath. These lamprey tissues are known to contain five distinct genetic types of fibrillar collagen. The modes of axial and lateral packing of collagen molecules in fibrils of the lamprey tissues demonstrate the three major motifs seen in higher vertebrate D-periodic collagen fibrils. In particular, lamprey dermis was found to have a decreased D period resulting from a molecular tilt that is seen in skins of higher vertebrates. Our results suggest the molecular-packing motifs for collagen fibrils were in place at the dawn of vertebrate evolution and have been conserved since. In contrast, the diameters of fibrils and their spatial orientation in lamprey tissues do not in general, correspond to features found in mammalian tissues. Only for lamprey notochord is there a strong similarity, with fibril diameters and organization closely resembling those seen in type II tissues of higher vertebrates. This suggests that for all tissues except those with type II collagen, higher level organization of fibrils evolved along with the diversification of vertebrates.
Brodsky
B
B
Department of Biochemistry, UMDNJ-Robert Wood Johnson Medical School, Piscataway 08854.
BelBruno
K C
KC
Hardt
T A
TA
Eikenberry
E F
EF
D000818:Animals; D003094:Collagen / Q000737:chemistry / Q000648:ultrastructure*; D003238:Connective Tissue / Q000737:chemistry / Q000648:ultrastructure*; D007798:Lampreys / Q000033:anatomy & histology* / Q000378:metabolism; D008854:Microscopy, Electron; D009672:Notochord / Q000648:ultrastructure; D012867:Skin / Q000648:ultrastructure; D014961:X-Ray Diffraction
D003094:Collagen