J. Biol. Chem., Vol. 263, Issue 2, 980-987, Jan, 1988
Fibril-forming collagens in lamprey
J Kelly, S Tanaka, T Hardt, EF Eikenberry and B Brodsky
Department of Biochemistry, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway 08854.
Five types of collagen with triple-helical regions approximately 300 nm in
length were found in lamprey tissues which show characteristic D- periodic
collagen fibrils. These collagens are members of the fibril forming family
of this primitive vertebrate. Lamprey collagens were characterized with
respect to solubility, mobility on sodium dodecyl sulfate-polyacrylamide
gel electrophoresis, carboxylmethyl-cellulose chromatography, peptide
digestion patterns, composition, susceptibility to vertebrate collagenase,
thermal stability, and segment long spacing- banding pattern. Comparison
with fibril-forming collagens in higher vertebrates (types I, II, III, V,
and XI) identified three lamprey collagens as types II, V, and XI. Both
lamprey dermis and major body wall collagens had properties similar to type
I but not the typical heterotrimer composition. Dermis molecules had only
alpha 1(I)-like chains, while body wall molecules had alpha 2(I)-like
chains combined with chains resembling lamprey type II. Neither collagen
exhibited the interchain disulfide linkages or solubility properties of
type III. The conservation of fibril organization in type II/type XI
tissues in contrast to the major developments in type I and type III
tissues after the divergence of lamprey and higher vertebrates is
consistent with these results. The presence of type II and type I-like
molecules as major collagens and types V and XI as minor collagens in the
lamprey, and the differential susceptibility of these molecules to
vertebrate collagenase is analogous to the findings in higher vertebrates.
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