EXPRESSION AND ACTION OF THE CARDIOINHIBITORY PEPTIDE, DROSOPHILA MYOSUPPRESSIN (DMS)

R. NICHOLS ~§ (P), J. MCCORMICK §, M. DICKERSON §, K. PAISLEY §

Depts of ~Biological Chemistry, and § Biology, University of Michigan, Ann Arbor, Michigan, USA 48109-1048,

Although Drosophila has served as a versatile experimental organism for developmental neurobiology little is known about the action of neuropeptides due to the lack of structure data, antisera specific to individual neuropeptides, and bioassays. We have isolated TDVDHVFLRFamide, Drosophila myosuppressin or dromyosuppressin (DMS), generated sequence-specific antisera to DMS, and established in vivo and in vitro assays to study the cardioinhibitory action of DMS.
Myosuppressin peptides, isolated from several organisms, have a high degree of structure identity. Only the N-terminal amino acid residue differs between EDVDHVFLRFamide or leuco- myosuppressin, LMS, isolated from cockroach and PDVDHVFLRFamide or SchistoFLRFamide, isolated from locust. Antisera raised to TDVDHV were used to determine the expression pattern of DMS at all stages of development. DMS immunoreactive material is present in neural and gastrointestinal tissue. Immunoreactive projections from neurons in the superior protocerebrum impinge on the anterior of the dorsal vessel. We have determined that serotonin increases Drosophila heart rate. A mixture of serotonin and DMS has an additive effect suggesting that the two substances act through different mechanisms. The action of DMS is suppressed in potassium channels mutants and in the presence of potassium channel blockers, supporting the conclusion that the regulation of heart rate involves potassium channels. Supported by NSF and AHA/MI.