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Complete primary structure of human collagen alpha 1 (V) chain
K Takahara1, Y Sato, K Okazawa
1Biotechnology Research Laboratories, Takara Shuzo Co., Shiga, Japan.
The Journal of Biological Chemistry
|July 15, 1991
Summary
Researchers isolated human collagen alpha 1(V) chain cDNA clones, revealing unique structural features and evolutionary divergence from other fibrillar collagens. This study enhances understanding of collagen V
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Collagen V (alpha 1(V)) is a fibrillar collagen crucial for tissue structure.
- Understanding its genetic and structural properties is key to comprehending collagen biology.
Purpose of the Study:
- To isolate and characterize cDNA clones encoding human collagen alpha 1(V) prepropeptide.
- To elucidate the structural features and evolutionary relationships of the alpha 1(V) collagen chain.
Main Methods:
- Isolation and sequencing of cDNA clones encoding human collagen alpha 1(V) prepropeptide.
- Bioinformatic analysis of the deduced amino acid sequence, including domain identification and homology searches.
Main Results:
- The human alpha 1(V) prepropeptide (1838 amino acids) contains a signal peptide, a large N-terminal noncollagenous region, a collagenous domain, and a C-terminal noncollagenous region.
- The N-terminal noncollagenous region shows homology to laminin A chain but lacks a conserved cysteine-rich domain found in other collagens.
- The collagenous domain exhibits high homology (82%) to alpha 1(XI) collagen, while codon usage patterns resemble type IV collagen, suggesting distinct evolutionary origins.
Conclusions:
- The alpha 1(V) chain shares characteristics with fibrillar collagens like alpha 1(XI) but possesses unique structural and evolutionary features.
- The distinct codon usage of alpha 1(V) cDNA compared to other fibrillar collagens implies a separate evolutionary trajectory for the alpha 1(V) gene.