I. Aplysia californica neurons R3-R14

Primary structure of the myoactive histidine-rich basic peptide and peptide I

Gregg Thomas Nagle, Susan L. Knock, Sherry D. Painter, James E. Blankenship, Richard R. Fritz, Alexander Kurosky

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The R3-R14 neurons of the marine mollusc Aplysia are neuroendocrine cells that express a gene encoding peptides I, II and histidine-rich basic peptide (HRBP), a myoactive peptide that excites Aplysia heart and enhances gut motility in vitro. Peptide II has been chemically characterized (35), but the complete primary structures of peptide I and HRBP have not been established by amino acid sequence analysis. HRBP, peptide I, and the prohormone (proHRBP) were therefore purified from acid extracts of Aplysia californica neural tissue using sequential gel filtration and reversed-phase high-performance liquid chromatography and chemically characterized. Amino acid sequence analysis demonstrated that HRBP was a 43-residue peptide whose sequence was: <Glu-Val-Ala-Gln-Met-His-Val-Trp-Arg-Ala-Val-Asn-His-Asp-Arg-Asn-His-Gly-Thr-Gly-Ser-Gly-Arg-His-Gly-Arg-Phe-Leu-Ile-Arg-Asn- Arg-Tyr-Arg-Tyr-Gly-Gly-Gly-His-Leu-Ser-Asp-Ala-COOH. Compositional and sequence analyses of peptide I and proHRBP demonstrated that peptide I was a 26-residue peptide with the following sequence: NH 2 -Glu-Glu-Val-Phe-Asp-Asp-Thr-Asp-Val-Gly-Asp-Glu-Leu-Thr-Asn-Ala-Leu-Glu-Ser-Val-Leu-Thr-Asp-Phe-Lys-Asp-COOH. These results demonstrated that the pro-HRBP sequence predicted by nucleotide sequence analysis of a cDNA clone (24) was in fact synthesized in R3-R14 neurons. Hydrophilicity and hydrophobicity profiles of preproHRBP, combined with charge distribution profiles and predictive secondary structural analysis, showed that cleavage at dibasic sequences was strongly associated with peaks of hydrophilicity in α-helical regions of the preprohormone.

Original languageEnglish (US)
Pages (from-to)849-857
Number of pages9
JournalPeptides
Volume10
Issue number4
DOIs
StatePublished - Jan 1 1989
Externally publishedYes

Fingerprint

Aplysia
Histidine
Neurons
Peptides
Hydrophobic and Hydrophilic Interactions
Protein Sequence Analysis
Hydrophilicity
Sequence Analysis
peptide I
Molluscs
Amino Acids
Neuroendocrine Cells
Gene encoding
Mollusca
Charge distribution
High performance liquid chromatography
Reverse-Phase Chromatography
Hydrophobicity
Structural analysis
Gel Chromatography

Keywords

  • Amino acid sequence
  • Aplysia californica
  • Histidine-rich basic peptide
  • Molluscan neuropeptide
  • Peptide I
  • R3-R14 neurons

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

Cite this

I. Aplysia californica neurons R3-R14 : Primary structure of the myoactive histidine-rich basic peptide and peptide I. / Nagle, Gregg Thomas; Knock, Susan L.; Painter, Sherry D.; Blankenship, James E.; Fritz, Richard R.; Kurosky, Alexander.

In: Peptides, Vol. 10, No. 4, 01.01.1989, p. 849-857.

Research output: Contribution to journalArticle

Nagle, Gregg Thomas ; Knock, Susan L. ; Painter, Sherry D. ; Blankenship, James E. ; Fritz, Richard R. ; Kurosky, Alexander. / I. Aplysia californica neurons R3-R14 : Primary structure of the myoactive histidine-rich basic peptide and peptide I. In: Peptides. 1989 ; Vol. 10, No. 4. pp. 849-857.
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abstract = "The R3-R14 neurons of the marine mollusc Aplysia are neuroendocrine cells that express a gene encoding peptides I, II and histidine-rich basic peptide (HRBP), a myoactive peptide that excites Aplysia heart and enhances gut motility in vitro. Peptide II has been chemically characterized (35), but the complete primary structures of peptide I and HRBP have not been established by amino acid sequence analysis. HRBP, peptide I, and the prohormone (proHRBP) were therefore purified from acid extracts of Aplysia californica neural tissue using sequential gel filtration and reversed-phase high-performance liquid chromatography and chemically characterized. Amino acid sequence analysis demonstrated that HRBP was a 43-residue peptide whose sequence was: <Glu-Val-Ala-Gln-Met-His-Val-Trp-Arg-Ala-Val-Asn-His-Asp-Arg-Asn-His-Gly-Thr-Gly-Ser-Gly-Arg-His-Gly-Arg-Phe-Leu-Ile-Arg-Asn- Arg-Tyr-Arg-Tyr-Gly-Gly-Gly-His-Leu-Ser-Asp-Ala-COOH. Compositional and sequence analyses of peptide I and proHRBP demonstrated that peptide I was a 26-residue peptide with the following sequence: NH 2 -Glu-Glu-Val-Phe-Asp-Asp-Thr-Asp-Val-Gly-Asp-Glu-Leu-Thr-Asn-Ala-Leu-Glu-Ser-Val-Leu-Thr-Asp-Phe-Lys-Asp-COOH. These results demonstrated that the pro-HRBP sequence predicted by nucleotide sequence analysis of a cDNA clone (24) was in fact synthesized in R3-R14 neurons. Hydrophilicity and hydrophobicity profiles of preproHRBP, combined with charge distribution profiles and predictive secondary structural analysis, showed that cleavage at dibasic sequences was strongly associated with peaks of hydrophilicity in α-helical regions of the preprohormone.",
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AU - Knock, Susan L.

AU - Painter, Sherry D.

AU - Blankenship, James E.

AU - Fritz, Richard R.

AU - Kurosky, Alexander

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N2 - The R3-R14 neurons of the marine mollusc Aplysia are neuroendocrine cells that express a gene encoding peptides I, II and histidine-rich basic peptide (HRBP), a myoactive peptide that excites Aplysia heart and enhances gut motility in vitro. Peptide II has been chemically characterized (35), but the complete primary structures of peptide I and HRBP have not been established by amino acid sequence analysis. HRBP, peptide I, and the prohormone (proHRBP) were therefore purified from acid extracts of Aplysia californica neural tissue using sequential gel filtration and reversed-phase high-performance liquid chromatography and chemically characterized. Amino acid sequence analysis demonstrated that HRBP was a 43-residue peptide whose sequence was: <Glu-Val-Ala-Gln-Met-His-Val-Trp-Arg-Ala-Val-Asn-His-Asp-Arg-Asn-His-Gly-Thr-Gly-Ser-Gly-Arg-His-Gly-Arg-Phe-Leu-Ile-Arg-Asn- Arg-Tyr-Arg-Tyr-Gly-Gly-Gly-His-Leu-Ser-Asp-Ala-COOH. Compositional and sequence analyses of peptide I and proHRBP demonstrated that peptide I was a 26-residue peptide with the following sequence: NH 2 -Glu-Glu-Val-Phe-Asp-Asp-Thr-Asp-Val-Gly-Asp-Glu-Leu-Thr-Asn-Ala-Leu-Glu-Ser-Val-Leu-Thr-Asp-Phe-Lys-Asp-COOH. These results demonstrated that the pro-HRBP sequence predicted by nucleotide sequence analysis of a cDNA clone (24) was in fact synthesized in R3-R14 neurons. Hydrophilicity and hydrophobicity profiles of preproHRBP, combined with charge distribution profiles and predictive secondary structural analysis, showed that cleavage at dibasic sequences was strongly associated with peaks of hydrophilicity in α-helical regions of the preprohormone.

AB - The R3-R14 neurons of the marine mollusc Aplysia are neuroendocrine cells that express a gene encoding peptides I, II and histidine-rich basic peptide (HRBP), a myoactive peptide that excites Aplysia heart and enhances gut motility in vitro. Peptide II has been chemically characterized (35), but the complete primary structures of peptide I and HRBP have not been established by amino acid sequence analysis. HRBP, peptide I, and the prohormone (proHRBP) were therefore purified from acid extracts of Aplysia californica neural tissue using sequential gel filtration and reversed-phase high-performance liquid chromatography and chemically characterized. Amino acid sequence analysis demonstrated that HRBP was a 43-residue peptide whose sequence was: <Glu-Val-Ala-Gln-Met-His-Val-Trp-Arg-Ala-Val-Asn-His-Asp-Arg-Asn-His-Gly-Thr-Gly-Ser-Gly-Arg-His-Gly-Arg-Phe-Leu-Ile-Arg-Asn- Arg-Tyr-Arg-Tyr-Gly-Gly-Gly-His-Leu-Ser-Asp-Ala-COOH. Compositional and sequence analyses of peptide I and proHRBP demonstrated that peptide I was a 26-residue peptide with the following sequence: NH 2 -Glu-Glu-Val-Phe-Asp-Asp-Thr-Asp-Val-Gly-Asp-Glu-Leu-Thr-Asn-Ala-Leu-Glu-Ser-Val-Leu-Thr-Asp-Phe-Lys-Asp-COOH. These results demonstrated that the pro-HRBP sequence predicted by nucleotide sequence analysis of a cDNA clone (24) was in fact synthesized in R3-R14 neurons. Hydrophilicity and hydrophobicity profiles of preproHRBP, combined with charge distribution profiles and predictive secondary structural analysis, showed that cleavage at dibasic sequences was strongly associated with peaks of hydrophilicity in α-helical regions of the preprohormone.

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