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Fibril-forming collagens in lamprey
1Department of Biochemistry, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway 08854.
The Journal of Biological Chemistry
|January 15, 1988
Summary
Lamprey vertebrates possess five collagen types, including fibril-forming collagens analogous to higher vertebrates. These findings reveal conserved collagen structures and functions in primitive vertebrates.
Area of Science:
- Biochemistry
- Evolutionary Biology
- Molecular Biology
Background:
- Collagen is a crucial structural protein in vertebrates, with various types forming distinct fibrils.
- Lampreys, as primitive vertebrates, offer insights into the evolution of collagen structures.
Purpose of the Study:
- To characterize the collagen types found in lamprey tissues.
- To compare lamprey collagens with those of higher vertebrates and understand evolutionary relationships.
Main Methods:
- Solubility and SDS-PAGE analysis.
- Carboxymethyl-cellulose chromatography and peptide digestion.
- Collagenase susceptibility, thermal stability, and segment long spacing (SLS) banding pattern analysis.
Main Results:
- Identified three lamprey collagens as types II, V, and XI.
- Lamprey dermis and body wall collagens showed type I-like properties but lacked typical heterotrimer composition.
- Dermis molecules contained alpha 1(I)-like chains; body wall molecules had alpha 2(I)-like chains and type II-like chains.
Conclusions:
- Lamprey collagens include types II, V, XI (minor), and type I-like molecules (major).
- Fibril organization conservation in type II/XI tissues contrasts with type I and III developments in higher vertebrates.
- Differential collagenase susceptibility in lampreys mirrors findings in higher vertebrates, suggesting functional conservation.