Pharmacological Characterization and Investigation of N-Terminal Loop Amino Acids of Adrenomedullin 2 That Are Important for Receptor Activation
| Autor: | Paul W. R. Harris, Hala Musa, Michael L. Garelja, Erica R. Hendrikse, Harriet A. Watkins, Margaret A. Brimble, Debbie L. Hay |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences 030302 biochemistry & molecular biology Disulfide bond Receptors Cell Surface Peptide hormone Biochemistry Terminal loop Amino acid Loop (topology) Adrenomedullin 03 medical and health sciences Adrenomedullin 2 chemistry COS Cells Chlorocebus aethiops Cyclic AMP Animals Humans Amino Acid Sequence Receptor Receptor activation hormones hormone substitutes and hormone antagonists |
| Zdroj: | Biochemistry. 58:3468-3474 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/acs.biochem.9b00571 |
| Popis: | Adrenomedullin 2 (AM2) is a peptide hormone with potent effects in the cardiovascular system. The N-terminal disulfide loop of AM2 is thought to be important for interacting with its receptors to initiate a signaling response. However, the relative contribution of each amino acid within this region is currently unknown. Thus, the region was investigated using an alanine scanning approach. Two AM2 peptides (AM2-47 and AM2-40) were directly compared at the CGRP, AM |
| Databáze: | OpenAIRE |
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