CHARACTERIZATION OF AN ANTISERUM AGAINST AN ACHETAKININ-I ANALOG AND ITS USE FOR THE LOCALIZATION OF CULEKININ DEPOLARIZING PEPTIDE-II IN THE MOSQUITO, CULEX-SALINARIUS
Fl. Clottens et al., CHARACTERIZATION OF AN ANTISERUM AGAINST AN ACHETAKININ-I ANALOG AND ITS USE FOR THE LOCALIZATION OF CULEKININ DEPOLARIZING PEPTIDE-II IN THE MOSQUITO, CULEX-SALINARIUS, Regulatory peptides, 49(2), 1993, pp. 145-157
ELISA experiments revealed that an antiserum raised against an achetak
inin-analog could specifically detect the recently isolated Culekinin
Depolarizing Peptide (CDP)-II from the mosquito, Culex salinarius. The
characterization indicated that two different epitopes in the C-termi
nal region of achetakinin I and CDP-II are recognized. One epitope is
the -F-Y-region, the other is the -P-W-region. Among the peptides isol
ated from C. salinarius, the antiserum reacts only with CDP-II. Pre-ab
sorption tests of the antiserum with CDP-II in immunohistological stai
nings abolished the reaction, while tests with pre-immune sera did not
cause any immunopositive reactions. In the mosquito head ganglia, imm
unoreactive neurons were detected in the pars lateralis, the optic lob
e and the suboesophageal ganglion. Although some immunopositive axons
extended into the nervi corporis cardiacii II, no immunoreactivity was
observed in the retrocerebral complex. In the thoracic ganglia, immun
oreactive neurons were found in the pro-, meso- and metathoracic neuro
meres. No immunoreactivity was found elsewhere. With this study we dem
onstrate that CDP-II, isolated from a whole body extract, is truly a n
europeptide, and the data suggest that its function is neuromodulating
or neurotransmitting rather than neurohormonal.