Structure and biological activity of glucagon and glucagon-like peptide from a primitive bony fish, the bowfin (Amia calva)
| Autor: | J M Conlon, J H Youson, T P Mommsen |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
endocrine system
medicine.medical_specialty Glycogenolysis Molecular Sequence Data Glucagon-Like Peptides Biochemistry Glucagon chemistry.chemical_compound Glucagon-Like Peptide 1 Internal medicine medicine Animals Humans Amino Acid Sequence Bowfin Tyrosine Pancreas Molecular Biology Peptide sequence chemistry.chemical_classification Sequence Homology Amino Acid biology Glycogen digestive oral and skin physiology Fishes Cell Biology biology.organism_classification Peptide Fragments Amino acid Endocrinology Liver chemistry Peptides hormones hormone substitutes and hormone antagonists Research Article |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2950857 |
| Popis: | The bowfin, Amia calva (order Amiiformes) occupies an important position in phylogeny as a surviving representative of a group of primitive ray-finned fishes from which the present-day teleosts may have evolved. Glucagon and glucagon-like peptide (GLP) were isolated from an extract of bowfin pancreas and their primary structures determined. Bowfin glucagon shows only four amino acid substitutions compared with human glucagon, and bowfin glucagon was equipotent and equally effective as human glucagon in stimulation of glycogenolysis in dispersed hepatocytes from a teleost fish, the copper rockfish, Sebastes caurinus. In contrast, bowfin GLP shows 15 amino acid substitutions and three amino acid deletions compared with the corresponding region of human GLP-1-(7-37)-peptide. In particular, the bowfin peptide contains an N-terminal tyrosine residue rather than the N-terminal histidine residue found in all other glucagon-related peptides so far characterized. Bowfin GLP stimulated glycogenolysis in rockfish hepatocytes, but was 3-fold less effective and 23-fold less potent than human GLP-1-(7-37)-peptide. We speculate that selective mutations in the GLP domain of bowfin preproglucagon may be an adaptive response to the previously demonstrated low biological potency of bowfin insulin. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|