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Complete primary structure of human collagen type XIV (undulin)
M Bauer1, W Dieterich, T Ehnis
1Free University of Berlin, Klinkum Benjamin Franklin, Department of Gastroenterology, Germany.
Biochimica Et Biophysica Acta
|January 14, 1998
Summary
Researchers completed the human undulin cDNA sequence, confirming its identity as collagen type XIV. This finding reveals two distinct polyprotein variants with significant sequence similarity to chicken collagen type XIV.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- Undulin is a protein found in the human extracellular matrix.
- Its precise identity and relationship to other proteins have been under investigation.
Purpose of the Study:
- To complete the cDNA sequence of human undulin.
- To confirm the identity of undulin as collagen type XIV.
- To analyze the structural characteristics of the resulting protein variants.
Main Methods:
- cDNA sequencing
- Bioinformatic analysis of protein sequences
- Comparison with known collagen sequences
Main Results:
- A complete cDNA sequence for human undulin was obtained.
- Conclusive evidence was found identifying undulin as human collagen type XIV.
- Two polyprotein variants (1780 and 1796 amino acids) were identified.
- These variants showed 75% amino acid sequence identity to chicken collagen type XIV, particularly in the C-terminal NC1 domain.
Conclusions:
- Human undulin is identical to collagen type XIV.
- Alternative splicing or transcription start sites result in two distinct protein isoforms.
- The findings provide a comprehensive understanding of human collagen type XIV structure and its relationship to avian counterparts.