Identification of the spinal degradation products and inhibition of adenylate cyclase by recombinant rat galanin message-associated peptide
| Autor: | Siv Andell-Jonsson, Tamas Bartfai |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Male
Receptors Neuropeptide Molecular Sequence Data Gene Expression Adenylate kinase Neuropeptide Galanin Peptide Biology Binding Competitive Second Messenger Systems Cyclase Rats Sprague-Dawley Cellular and Molecular Neuroscience chemistry.chemical_compound Endocrinology Cyclic AMP Escherichia coli Animals Protein Precursors Cyclic GMP DNA Primers chemistry.chemical_classification Forskolin Sequence Homology Amino Acid Endocrine and Autonomic Systems Cell Membrane Colforsin General Medicine Peptide Fragments Recombinant Proteins Rats Spinal Cord Neurology chemistry Biochemistry Adenylyl Cyclase Inhibitors Second messenger system Receptors Galanin Cyclase activity Adenylyl Cyclases |
| Zdroj: | Neuropeptides. 32:191-196 |
| ISSN: | 0143-4179 |
| DOI: | 10.1016/s0143-4179(98)90037-3 |
| Popis: | In rat preprogalanin, galanin is C-terminally flanked by a 60 amino acid long peptide: galanin message-associated peptide (GMAP). GMAP sequences in different species show high degree of homology, suggesting a biological role. However, the study of the physiological and pharmacological actions of this peptide have been hampered by lack of availability of this large peptide, its fragments and well-characterized antibodies to GMAP. This study report the production of GMAP in Escherichia coli and the use of the recombinant peptide to define its degradation products in the spinal cord. The GMAP fragments formed upon incubation of GMAP with membranes of lumbar spinal cord were identified by sequencing and were also produced by solid phase synthesis for studies on second messenger systems. Furthermore, the study demonstrates that GMAP inhibits forskolin stimulated adenylate cyclase activity in a concentration dependent manner, while GMAP and its synthetic fragments did not affect cGMP level. |
| Databáze: | OpenAIRE |
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