Structural and functional diversities of the Aplysia Mytilus inhibitory peptide-related peptides.
Aplysia Mytilus inhibitory peptide-related peptides (AMRPs) are multiple hexapeptides coded on a single precursor. By comparing the AMRP precursors of two species of Aplysia (Aplysia californica and Aplysia kurodai), we found that there are substantial numbers of species-specific AMRPs. We next compared the function of AMRPs on the anterior aorta between A. kurodai and Aplysia juliana. In A. juliana, AMRPs inhibited the contractile activity of the aorta (EC(50)=10(-9) to 10(-8)M), whereas the peptides had no obvious action in A. kurodai up to 10(-7)M. These results indicate that AMRPs are both structurally and functionally diverse neuropeptides even among closely related species.
Sasaki
Kosei
K
Graduate School of Science, Department of Biological Science, Hiroshima University, Kagamiyama 1-3-1, Japan.
Shimizu
Yoriko
Y
Abe
Genbu
G
Fujisawa
Yuko
Y
Morishita
Fumihiro
F
Matsushima
Osamu
O
Furukawa
Yasuo
Y
D000595:Amino Acid Sequence; D000818:Animals; D001011:Aorta / Q000187:drug effects / Q000502:physiology; D001048:Aplysia / Q000737:chemistry*; D001483:Base Sequence; D017931:DNA Primers; D008969:Molecular Sequence Data; D009119:Muscle Contraction / Q000187:drug effects; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology*; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D017931:DNA Primers; D010455:Peptides