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Primary structure of human pepsinogen C gene
T Hayano1, K Sogawa, Y Ichihara
1Department of Biochemistry, Japanese Foundation for Cancer Research, Tokyo.
The Journal of Biological Chemistry
|January 25, 1988
Summary
Researchers isolated the human pepsinogen C gene, revealing its structure and evolutionary link to other aspartic proteinases. This finding aids in understanding gene expression and the origins of this enzyme family.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Pepsinogen C is a key enzyme in digestion.
- Understanding its gene structure provides insights into proteinase evolution.
Purpose of the Study:
- To isolate and characterize the complete human pepsinogen C gene.
- To analyze its nucleotide sequences and flanking regions.
- To infer evolutionary relationships with other aspartic proteinases.
Main Methods:
- Isolation of the human pepsinogen C gene from a cosmid genomic library.
- Determination of nucleotide sequences of exons and flanking regions.
- Bioinformatic analysis of the predicted amino acid sequence.
Main Results:
- The complete human pepsinogen C gene was successfully isolated.
- Nucleotide sequences of exons and 5'/3'-flanking regions were determined.
- The gene structure is compatible with other aspartic proteinases, suggesting a common ancestor.
- The predicted amino acid sequence includes a signal peptide, activation peptide, and mature pepsin.
Conclusions:
- The human pepsinogen C gene shares fundamental organization with other aspartic proteinases.
- Genes for aspartic proteinases likely evolved from a common ancestral gene.
- The study provides a basis for investigating eukaryotic gene expression and regulatory elements within the pepsinogen C gene promoter.