Purification and primary structure of the neuropeptide egg-laying hormone of
            <i>Aplysia californica</i>

Chiu, Arlene Y.; Hunkapiller, Michael W.; Heller, E.; Stuart, Duncan K.; Hood, Leroy; Strumwasser, Felix

doi:10.1073/pnas.76.12.6656

Cited by 149 publications

(69 citation statements)

References 16 publications

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“…Amino acid alignment of msP 355a with ELH. The regions of msP 355a sequence identity with ELH are outlined; the full sequence of ELH (Chiu et al 1979) is presented for clarity. Allowing one gap in each sequence, 11 of 17 amino acids are identical (boxed); if no gaps are allowed, 9 of 17 amino acids are identical.…”

Section: Discussionmentioning

confidence: 99%

“…One match was found for the msP 355a amino acid sequence, with egg-laying hormone (ELH) of the mollusc Aplysia californica (the California seahare). ELH is a 36-amino-acid peptide neurohormone which is involved in eliciting stereotyped postmating behavior in Aplysia (Chiu et al 1979). The similarity hes in the stretch from amino acids 121 to 137 of msP 355a, in which 11 out of 17 amino acids are identical to those in the stretch from amino acid 2 to 18 of ELH, allowing for a single amino acid gap in each sequence (Fig.…”

Section: Msp 355a Has Amino Acid Sequence Similarity To Aplysia Egg-lmentioning

confidence: 99%

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Structure and expression of a Drosophila male accessory gland gene whose product resembles a peptide pheromone precursor.

Monsma

Wolfner²

1988

Genes Dev.

137

109

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The accessory gland of male insects is a genital tissue that secretes many components of the ejaculatory fluid, some of which affect the female's receptivity to courtship and her rate of oviposition. We have examined the structure and expression of two tightly linked genes that are expressed exclusively in the male accessory glands of adult Drosopbila melanogaster. The two genes are transcribed from the same strand of DNA, and are separated by 20 bases. Both genes are regulated by the sex determination hierarchy and are expressed in the absence of germ cells. Immunological analysis reveals the protein products of at least one of these genes in the secretion of the accessory gland. The proteins are transferred to the female fly during copulation and are rapidly altered in the female genital tract. The predicted sequence of one protein has features of a peptide hormone precursor, and a region in which 11 of 17 amino acids are identical to egg-laying hormone (ELH) of the California sea hare, Aplysia califomica.

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Section: Discussionmentioning

confidence: 99%

Section: Msp 355a Has Amino Acid Sequence Similarity To Aplysia Egg-lmentioning

confidence: 99%

Structure and expression of a Drosophila male accessory gland gene whose product resembles a peptide pheromone precursor.

Monsma

Wolfner²

1988

Genes Dev.

137

109

View full text Add to dashboard Cite

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“…Previous studies defined the primary sequence of ELH (Chiu et al, 1979), the acidic peptide (Scheller et al, 1983), and a-BCP . From the precursor structure we predicted additional cleavages that would give rise to peptides we called the fi-, y-, and &BCPs.…”

Section: Discussionmentioning

confidence: 99%

“…These neurons send secretory processes primarily into the sheath surrounding the ganglion and the pleural abdominal connectives. At least 2 biologically active peptides, ELH and a-bag cell peptide (cu-BCP), have been purified from bag cell extracts (Chiu et al, 1979;Mayeri et al, 1985;Sigvardt et al, 1986). Furthermore, bag cell discharge leads to a stereotyped egg-laying behavior with multiple separate components (Arch and Smock, 1977).…”

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confidence: 99%

Proteolytic processing of the Aplysia egg-laying hormone and R3-14 neuropeptide precursors

Newcomb¹,

Scheller²

1987

J. Neurosci.

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A number of animal behaviors are influenced by the actions of neuropeptides that arise from the processing of complex protein precursors. In this report we investigate the proteolytic processing of neuropeptide precursors expressed in the Aplysia californica bag cells, which govern egg-laying, and neurons R3–14, which mediate aspects of cardiac output. Peptides were purified by fractionation on 2 high- pressure liquid chromatography systems followed by determination of amino acid compositions. Most of these compositions are indicative of processing products derived from the egg-laying hormone (ELH) and R3–14 precursors by cleavage at basic residues. We characterized 9 peptides that arise from the ELH precursor by cleavage of the signal sequence, as well as 7 out of 8 dibasic residues and at least 1 single Arg residue. The peptides range in size from 5 to about 60 amino acids. The R3–14 neuropeptide precursor is cleaved at 2 internal dibasic residues in addition to the signal sequence, resulting in 3 peptides. Shortened forms of several peptides probably result from amino- and carboxy- terminal peptidase action. It is likely that the complex mixtures of neuropeptides arising from these single protein precursors are co- secreted.

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“…We chose to follow the appearance of AP and ELH as indicators of the final stages of precursor processing because they are known to be transported by a colchicine-sensitive process and secreted in response to depolarization (Arch, 1972a;Arch et al, 1976bKupfermann, 1972Loh et al, 1975;Stuart et al, 1980). Moreover, because of their relatively high leucine content (Chiu et al, 1979;Scheller et al, 1983) and dissimilar isoelectric points (Arch et al, 1976a), radiolabeling and isoelectric focusing give clear indications of their presence in samples of interest (e.g., Fig. 1, top).…”

Section: Our Initial Experimentsmentioning

confidence: 99%

Neuropeptide routing in the bag cells: kinetic differences in the appearance of newly labeled peptides in transport and secretion

Arch¹,

Linstedt²,

Whitney³

et al. 1986

J. Neurosci.

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The bag cell neurons of Aplysia synthesize and secrete several peptides. Some of these, in addition to the egg-laying hormone (ELH), are strongly implicated in the various alterations of central neuronal activity that accompany an electrical discharge of the bag cells. Thus, the secreted peptides appear to play a variety of roles in the animal's physiology. We have been interested in the intracellular mechanisms that precede peptide secretion from the bag cells because of the evidence that most, if not all, of these peptides are derived from a common precursor. Our objective has been to determine if presumed products of this precursor are processed coordinately following their synthesis. We have concentrated on two peptides (ELH and the acidic peptide, AP) because they are most easily identified in our analytical systems. On pulse-chase radiolabeling of the cells in vitro, we found that labeled AP appears before labeled ELH in axonal transport. This observation is not easily accounted for by the assumption, taken from studies of other peptide-secreting cells, that a precursor to both peptides is loaded into secretory granules before further processing ensues. Since the initial disproportion in the representation of the peptides in transport is no longer detectable at long chase times (18 and 24 hr), we examined the possibilities that ELH production is delayed relative to that of AP or that AP is degraded more rapidly than ELH. No evidence was found for either process. The disproportion between the newly labeled peptides in transport was evident on analysis of the medium bathing bag cells depolarized after 24 hr of chase.(ABSTRACT TRUNCATED AT 250 WORDS)

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Purification and primary structure of the neuropeptide egg-laying hormone of Aplysia californica

Cited by 149 publications

References 16 publications

Structure and expression of a Drosophila male accessory gland gene whose product resembles a peptide pheromone precursor.

Structure and expression of a Drosophila male accessory gland gene whose product resembles a peptide pheromone precursor.

Proteolytic processing of the Aplysia egg-laying hormone and R3-14 neuropeptide precursors

Neuropeptide routing in the bag cells: kinetic differences in the appearance of newly labeled peptides in transport and secretion

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