II. Aplysia brasiliana neurons R3-R14

Primary structure of the myoactive histidine-rich basic peptide and its prohormone

Susan L. Knock, Gregg T. Nagle, Cheng Yie Lin, David J. McAdoo, Alexander Kurosky

    Research output: Contribution to journalArticle

    4 Citations (Scopus)

    Abstract

    Neurons R3-R14 of the marine mollusc Aplysia are model neuroendocrine cells thought to regulate cardiovascular activity in vivo. The cells express a gene encoding three peptides-peptides I, II and the histidine-rich basic peptide (HRBP)-each of which has been chemically characterized in Aplysia californica. In the studies presented here, HRBP and its prohormone (proHRBP) were purified from A. brasiliana abdominal ganglion extracts by reversed-phase high-performance liquid chromatography and characterized by amino acid compositional and sequence analyses. ProHRBP was an 85-residue peptide whose sequence was: NH2-Glu-Glu-Val-Phe-Asp-Asp-Thr-Asp- Val-Gly-Asp-Glu-Leu-Thr-Asn-Ala-Leu-Glu-Ser-Val-Leu-Thr-Asp-Leu-Lys-Asp-Lys-Arg-Asp-Ala-Glu-Glu-Pro-Ser-Ala-Phe-Met- Thr-Arg-Leu-Arg-Arg-Gln-Val-Ala-Gln-Met-His-Ile-Trp-Arg-Ala-Val-Asn-His-Asp-Arg-His-His-Ser-Thr-Gly-Ser-Gly-Arg-His- Ser-Arg-Phe-Leu-Thr-Arg-Asn-Arg-Tyr-Arg-Tyr-Gly-Gly-Gly-His-Leu-Ser-Asp-Ala-COOH. It differed from A. californica pro-HRBP at seven of the 85 positions. Compositional and sequence analyses demonstrated that A. brasiliana HRBP was a 43-residue peptide corresponding to residues 43 through 85 of proHRBP, and that a significant proportion of the isolated peptide possessed a blocked NH2 terminus. Although this sequence differed from that of A. californica HRBP at five of 43 residues, the two peptides were approximately equipotent in inducing contractions of A. californica crop muscle in vitro, suggesting that the substituted residues may not be critical for biological activity.

    Original languageEnglish (US)
    Pages (from-to)859-867
    Number of pages9
    JournalPeptides
    Volume10
    Issue number4
    DOIs
    StatePublished - 1989

    Fingerprint

    Aplysia
    Histidine
    Neurons
    Peptides
    Molluscs
    Neuroendocrine Cells
    Gene encoding
    Mollusca
    Protein Sequence Analysis
    High performance liquid chromatography
    Reverse-Phase Chromatography
    Bioactivity
    Ganglia
    Crops
    Sequence Analysis
    Muscle
    High Pressure Liquid Chromatography

    Keywords

    • Amino acid sequence
    • Aplysia brasiliana
    • Histidine-rich basic peptide
    • Molluscan neuropeptide
    • Precursor peptide
    • R3-R14 neurons

    ASJC Scopus subject areas

    • Biochemistry
    • Endocrinology
    • Physiology
    • Cellular and Molecular Neuroscience

    Cite this

    II. Aplysia brasiliana neurons R3-R14 : Primary structure of the myoactive histidine-rich basic peptide and its prohormone. / Knock, Susan L.; Nagle, Gregg T.; Lin, Cheng Yie; McAdoo, David J.; Kurosky, Alexander.

    In: Peptides, Vol. 10, No. 4, 1989, p. 859-867.

    Research output: Contribution to journalArticle

    Knock, Susan L. ; Nagle, Gregg T. ; Lin, Cheng Yie ; McAdoo, David J. ; Kurosky, Alexander. / II. Aplysia brasiliana neurons R3-R14 : Primary structure of the myoactive histidine-rich basic peptide and its prohormone. In: Peptides. 1989 ; Vol. 10, No. 4. pp. 859-867.
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    AU - Lin, Cheng Yie

    AU - McAdoo, David J.

    AU - Kurosky, Alexander

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    Y1 - 1989

    N2 - Neurons R3-R14 of the marine mollusc Aplysia are model neuroendocrine cells thought to regulate cardiovascular activity in vivo. The cells express a gene encoding three peptides-peptides I, II and the histidine-rich basic peptide (HRBP)-each of which has been chemically characterized in Aplysia californica. In the studies presented here, HRBP and its prohormone (proHRBP) were purified from A. brasiliana abdominal ganglion extracts by reversed-phase high-performance liquid chromatography and characterized by amino acid compositional and sequence analyses. ProHRBP was an 85-residue peptide whose sequence was: NH2-Glu-Glu-Val-Phe-Asp-Asp-Thr-Asp- Val-Gly-Asp-Glu-Leu-Thr-Asn-Ala-Leu-Glu-Ser-Val-Leu-Thr-Asp-Leu-Lys-Asp-Lys-Arg-Asp-Ala-Glu-Glu-Pro-Ser-Ala-Phe-Met- Thr-Arg-Leu-Arg-Arg-Gln-Val-Ala-Gln-Met-His-Ile-Trp-Arg-Ala-Val-Asn-His-Asp-Arg-His-His-Ser-Thr-Gly-Ser-Gly-Arg-His- Ser-Arg-Phe-Leu-Thr-Arg-Asn-Arg-Tyr-Arg-Tyr-Gly-Gly-Gly-His-Leu-Ser-Asp-Ala-COOH. It differed from A. californica pro-HRBP at seven of the 85 positions. Compositional and sequence analyses demonstrated that A. brasiliana HRBP was a 43-residue peptide corresponding to residues 43 through 85 of proHRBP, and that a significant proportion of the isolated peptide possessed a blocked NH2 terminus. Although this sequence differed from that of A. californica HRBP at five of 43 residues, the two peptides were approximately equipotent in inducing contractions of A. californica crop muscle in vitro, suggesting that the substituted residues may not be critical for biological activity.

    AB - Neurons R3-R14 of the marine mollusc Aplysia are model neuroendocrine cells thought to regulate cardiovascular activity in vivo. The cells express a gene encoding three peptides-peptides I, II and the histidine-rich basic peptide (HRBP)-each of which has been chemically characterized in Aplysia californica. In the studies presented here, HRBP and its prohormone (proHRBP) were purified from A. brasiliana abdominal ganglion extracts by reversed-phase high-performance liquid chromatography and characterized by amino acid compositional and sequence analyses. ProHRBP was an 85-residue peptide whose sequence was: NH2-Glu-Glu-Val-Phe-Asp-Asp-Thr-Asp- Val-Gly-Asp-Glu-Leu-Thr-Asn-Ala-Leu-Glu-Ser-Val-Leu-Thr-Asp-Leu-Lys-Asp-Lys-Arg-Asp-Ala-Glu-Glu-Pro-Ser-Ala-Phe-Met- Thr-Arg-Leu-Arg-Arg-Gln-Val-Ala-Gln-Met-His-Ile-Trp-Arg-Ala-Val-Asn-His-Asp-Arg-His-His-Ser-Thr-Gly-Ser-Gly-Arg-His- Ser-Arg-Phe-Leu-Thr-Arg-Asn-Arg-Tyr-Arg-Tyr-Gly-Gly-Gly-His-Leu-Ser-Asp-Ala-COOH. It differed from A. californica pro-HRBP at seven of the 85 positions. Compositional and sequence analyses demonstrated that A. brasiliana HRBP was a 43-residue peptide corresponding to residues 43 through 85 of proHRBP, and that a significant proportion of the isolated peptide possessed a blocked NH2 terminus. Although this sequence differed from that of A. californica HRBP at five of 43 residues, the two peptides were approximately equipotent in inducing contractions of A. californica crop muscle in vitro, suggesting that the substituted residues may not be critical for biological activity.

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    KW - Molluscan neuropeptide

    KW - Precursor peptide

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