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Purification, structural characterization, and cardiovascular activity of cod bradykinins
1Department of Zoophysiology, University of Göteborg, Sweden.
The American Journal of Physiology
|February 1, 1997
Summary
Researchers identified two bradykinin (BK) peptides in Atlantic cod. The peptide cod [Arg0]BK significantly increased cod blood pressure and heart rate, indicating unique receptor interactions and catecholamine involvement.
Area of Science:
- Comparative physiology
- Marine biology
- Biochemistry
Background:
- Bradykinin (BK) is a peptide hormone involved in various physiological processes, including blood pressure regulation.
- Understanding BK receptor subtypes and their functions across different species is crucial for comparative pharmacology.
Purpose of the Study:
- To identify and characterize bradykinin peptides in Atlantic cod (Gadus morhua).
- To investigate the physiological effects of these peptides on cardiovascular parameters in cod.
- To compare the binding properties of cod BK receptors with mammalian subtypes.
Main Methods:
- Plasma incubation with trypsin to generate peptides.
- Synthesis of identified cod bradykinin peptides.
- Intra-arterial injections into conscious cod to measure ventral aortic pressure and heart rate.
- Administration of pharmacological agents (prasozin, enalapril) to assess mediating pathways.
Main Results:
- Two peptides, [Trp5,Leu8]bradykinin (cod BK) and [Arg0,Trp5,Leu8]bradykinin (cod [Arg0]BK), were identified.
- Cod [Arg0]BK demonstrated potent pressor and heart rate increasing effects, approximately 10 times more potent than cod BK.
- Mammalian BK and cod des-Arg9,[Arg0]BK had no significant cardiovascular effects.
- The pressor response to cod [Arg0]BK was modulated by prasozin and enalapril, suggesting involvement of catecholamines but not the renin-angiotensin system.
Conclusions:
- Atlantic cod possess unique bradykinin peptides and receptors distinct from mammalian B1 and B2 subtypes.
- Cod [Arg0]BK elicits significant cardiovascular responses in cod, mediated partly by catecholamines.
- These findings contribute to understanding the evolution and diversity of the kinin-peptide system in vertebrates.