Back to Search
Start Over
Amino-acid sequence and cell-adhesion activity of a fibril-forming collagen from the tube worm Riftia pachyptila living at deep sea hydrothermal vents
- Source :
- European Journal of Biochemistry. 210:839-847
- Publication Year :
- 1992
- Publisher :
- Wiley, 1992.
-
Abstract
- We have determined the amino acid sequence of the α chain of a fibril-forming collagen from the body wall of the marine invertebrate Riftia pachyptila (vestimentifera) by Edman degradation. The pepsin-solubilized collagen chain consists of a 1011-residue triple-helical domain and short remnants of N- and C-telopeptides. The triple-helical sequence showed one imperfection of the collagen Gly-Xaa-Yaa triplet repeat structure due to a Gly Ala substitution. This imperfection imperfection is correlated to a prominent kink in the molecule observed by electron microscopy. No strong sequence similarity was found with the fibril-forming vertebrate collagen types I-III, V and XI except for the invariant Gly residues. However, one of the two consensus cross-linking sequences was well conserved. The Riftia collagen shared with the vertebrate collagens many post-translational modifications. About 50% of the Pro and Lys residues are found in the Yaa position and were extensively hydroxylated to 4-hydroxyproline (4Hyp) and hydroxylysine (Hyl). A few proline residues in Xaa position were partially hydroxylated to either 4Hyp or 3Hyp. Despite the low sequence similarity, Riftia collagen was a potent adhesion substrate for two human cell lines. Cell adhesion could be inhibited by antibodies against the integrin β1 subunit but not by RGD peptides. This biological activity is apparently conserved in fibril-forming collagens of distantly related species but does not require the two RGD sequences present in Riftia collagen.
- Subjects :
- Edman degradation
Macromolecular Substances
Protein subunit
Molecular Sequence Data
Biological activity
Adhesion
Biology
Invertebrates
Biochemistry
Peptide Fragments
Hydroxylysine
chemistry.chemical_compound
chemistry
Cell Adhesion
Animals
Seawater
Amino Acid Sequence
Collagen
Cyanogen Bromide
Proline
Cell adhesion
Cell Adhesion Molecules
Protein Processing, Post-Translational
Peptide sequence
Subjects
Details
- ISSN :
- 14321033 and 00142956
- Volume :
- 210
- Database :
- OpenAIRE
- Journal :
- European Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....24c00a6eaeb0a893bb1cf8fc70e28f05