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Sequence of an intestinal cDNA encoding human motilin precursor.
1Division of Metabolism and Clinical Nutrition, Kyoto University School of Medicine, Japan.
FEBS Letters
|October 19, 1987
Summary
Researchers isolated a human motilin precursor cDNA, revealing a novel processing site at Lys-Lys. This finding advances understanding of human motilin (motilin) precursor maturation and its gastrointestinal functions.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- Motilin is a gastrointestinal peptide hormone regulating motility.
- The precursor structure and processing of human motilin were not fully elucidated.
Purpose of the Study:
- To isolate and characterize the cDNA encoding the human motilin precursor.
- To determine the amino acid sequence and processing sites of human motilin.
Main Methods:
- cDNA library screening using synthetic oligonucleotide probes.
- Amino acid sequence prediction from cDNA.
- Comparison with porcine motilin sequence.
Main Results:
- Isolated a cDNA clone for the human motilin precursor (115 amino acids).
- Predicted human motilin sequence is identical to porcine motilin.
- Identified a novel proteolytic processing site at Lys-Lys in the precursor.
Conclusions:
- The human motilin precursor contains a signal peptide, motilin sequence, and C-terminal peptide.
- Human motilin processing at Lys-Lys is a newly discovered mechanism.
- This research provides insights into motilin biogenesis and regulation.