Co-localization of the adipokinetic hormones I and II in the same glandular cells and in the same secretory granules of corpus cardiacum of Locusta migratoria and Schistocerca gregaria

Diederen, J. H. B.; Maas, Huub; Pel, HJ; Schooneveld, H.; Jansen, W. F.; Vullings, H. G. B.

doi:10.1007/bf00215522

Cited by 47 publications

(17 citation statements)

References 22 publications

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“…This suggests that the secretory granules have a higher content of AAP I sequences and thus AKH I than AAP II sequences and AKH II, and that the ICGs contain more AKH I prohormone than AKH II prohormone. This agrees with the findings of Diederen et al (1987) as far as the AKHs in the secretory granules are concerned, and also with the data of Oudejans et al (1993) showing that the corpora cardiaca contain more AKH I than AKH II. The immunoreactivity for AAP I and AAP II tended to be stronger in older animals than in younger animals, which suggests that older animals contain more (pro)hormone than younger animals, reflecting the fact that the older the locusts, the higher the AKH content of the glands (Oudejans et al 1993).…”

Section: Discussionsupporting

confidence: 93%

“…Since the processing of the prohormones of the AKHs also most probably occurs in the secretory granules (O'Shea and Rayne 1992), immunocytochemical detection of the AAP sequences in these granules implies the corresponding AKHs are present as well. The co-localization of AKH I and AKH II in the secretory granules has already been established by Diederen et al (1987) by means of immunocytochemistry with antisera against these two peptide hormones. Our results show that these granules also contain AAP I and AAP II sequences.…”

Section: Discussionmentioning

confidence: 99%

“…The AKH III prohormone shows almost no homology with the former two and there are no indications that dimerization between the prohormone for AKH III and those for AKH I and AKH II can occur (Oudejans et al 1991;Bogerd et al 1995). AKH I and AKH II have been shown to be co-localized in the same secretory granules and the same ICGs of the locust adipokinetic cells (Diederen et al 1987). Both AKH I and AKH II are known to be released into the haemolymph shortly after the onset of flight and regulate the mobilization of lipid and carbohydrate from the locust fat body (Orchard and Lange 1983;Beenakkers et al 1985).…”

Section: Introductionmentioning

confidence: 94%

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Differential location of peptide hormones in the secretory pathway of insect adipokinetic cells

Harthoorn

Diederen

Oudejans

et al. 1999

Cell and Tissue Research

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Immunoreactivity of granules containing secretory material in the adipokinetic cells of the insect Locusta migratoria was studied using antisera specific for the adipokinetic hormone-associated peptides (AAP) I, II and III. Immunocytochemical detection of these associated peptides represents a new strategy for studying the intracellular location of the adipokinetic hormones and their prohormones. Fixation with 2% glutaraldehyde and 2% formaldehyde with low-temperature embedding in Lowicryl HM20 allowed highly selective immunogold labelling of both secretory and intracisternal granules. All three associated peptides were co-localized in secretory granules. This indicates that also all three adipokinetic hormones can be co-localized in these granules, which was confirmed by experiments in which, after secretory stimulation, adipokinetic hormone III was released from the adipokinetic cells together with adipokinetic hormones I and II. The immunopositivity of the intracisternal granules was similar to that of the secretory granules, although with the exception that the intracisternal granules did not show any specific reaction with anti-AAP III. The presence of AAP I and AAP II in intracisternal granules indicates that these granules only function as stores of adipokinetic prohormones I and II and not of adipokinetic prohormone III. The observed differences in storage in intracisternal granules among the three adipokinetic prohormones suggest differences in physiological significance of the three adipokinetic hormones in L. migratoria.

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Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 94%

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Differential location of peptide hormones in the secretory pathway of insect adipokinetic cells

Harthoorn

Diederen

Oudejans

et al. 1999

Cell and Tissue Research

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“…An interesting example of cellular co-localization of related peptides is constituted by the locust metabolic hormones designated the adipokinetic hormones (AKHs). In Locusta migratoria, these are derived from three different precursors (Bogerd et al 1995), and yet, they are co-localized in the same glandular cells of the corpora cardiaca (Diederen et al 1987;Harthoorn et al 1999).…”

Section: Introductionmentioning

confidence: 99%

Neuronal co-localization of different isoforms of tachykinin-related peptides (LemTRPs) in the cockroach brain

Nässel

Winther

2002

Cell and Tissue Research

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Seven isoforms of tachykinin-related peptides (TRPs) have been isolated from the brain of the cockroach Leucophaea maderae. These peptides (LemTRP-1, 2, and 5-9) share the C-terminal sequence GFX(1)GX(2)Ramide (where X(1) and X(2) are variable residues). In order to determine the neuronal distribution of several of these LemTRP isoforms, we raised antisera to their variable N-termini. Antisera to LemTRP-1, 2, 3, 7, and 8 were utilized for immunocytochemistry on cryostat sections of the L. maderae brain. As expected, the gut peptide LemTRP-3 was not detected in the brain, and the antisera to LemTRP-1, 2, and 7 labeled the same sets of neurons in different regions of the brain. These neurons could also be labeled with antisera raised to the more conserved C-termini of LemTRP-1 and the locust TRP LomTK-I. The antiserum to LemTRP-8 predominantly labeled a set of neurons distinct from that seen with any other N- or C-terminus-directed antisera, suggesting that it recognizes epitope(s) other than known insect TRPs. Our findings indicate that at least three of the LemTRPs are always co-localized in neurons of the L. maderae brain. We have also been able to show that LemTRP-2, which is an N-terminally extended form (17-mere) of LemTRP-1 with a dibasic putative cleavage site, is transported throughout the processes of the neurons in the same manner as LemTRP-1 and 7. Thus, LemTRP-2 may be released with the other shorter LemTRPs. This is the first investigation of LemTRP distribution in the cockroach central nervous system utilizing antisera to native peptides.

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“…Locust adipokinetic cells producing AKHs in CC contain two types of secretory granules (Diederen et al, 1987(Diederen et al, , 2002. Processed AKHs are either stored or prepared for release by exocytosis in the regular secretory granules, which have a diameter of about 300 nm.…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization, tissue distribution, and ultrastructural localization of adipokinetic hormones in the CNS of the firebug Pyrrhocoris apterus (Heteroptera, Insecta)

Kodrı́k¹,

Stašková²,

Jedličková³

et al. 2015

General and Comparative Endocrinology

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Co-localization of the adipokinetic hormones I and II in the same glandular cells and in the same secretory granules of corpus cardiacum of Locusta migratoria and Schistocerca gregaria

Cited by 47 publications

References 22 publications

Differential location of peptide hormones in the secretory pathway of insect adipokinetic cells

Differential location of peptide hormones in the secretory pathway of insect adipokinetic cells

Neuronal co-localization of different isoforms of tachykinin-related peptides (LemTRPs) in the cockroach brain

Molecular characterization, tissue distribution, and ultrastructural localization of adipokinetic hormones in the CNS of the firebug Pyrrhocoris apterus (Heteroptera, Insecta)

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