Biochemical mechanisms of calcium mobilisation induced by mastoparan and chimeric hormone-mastoparan constructs

Clare L. Longland; Mokdad Mezna; Ülo Langel; Mattias Hällbrink; Ursel Soomets; Mark Wheatley; Francesco Michelangeli; John Howl

doi:10.1016/S0143-4160(98)90086-0

Biochemical mechanisms of calcium mobilisation induced by mastoparan and chimeric hormone-mastoparan constructs

Clare L. Longland, Mokdad Mezna, Ülo Langel, Mattias Hällbrink, Ursel Soomets, Mark Wheatley, Francesco Michelangeli, John Howl

Research output: Contribution to journal › Article › peer-review

32 Citations (Scopus)

Abstract

Ca²⁺ efflux, Ca²⁺-ATPase, and membrane permeability measurements were used to investigate the biochemical mechanisms of Ca²⁺ release induced by mastoparan (MP) and the chimeric hormone-Mp constructs incorporating galanin (galparan) or vasopressin antagonist (M375 and M391) moieties. Comparative studies utilised preparations of porcine cerebellar microsomes and rabbit skeletal muscle sarcoplasmic reticulum (SR), MP and chimeric peptides galparan, M375 and M391 induce Ca²⁺ release over a range of concentrations from 0.3-10 μM. Comparison of MP and three chimeric, N-terminal extended, constructs indicates that N-terminal extension modifies the biological properties of MP, producing changes in efficacy which are enzyme-isoform-specific. Biochemical studies indicate that the chimeric analogues and MP inhibit Ca²⁺-ATPases and directly activate the ryanodine receptor (RyR) to release Ca²⁺ from both heavy SR (HSR) and microsomes. The same peptides have no effect on the InsP₃ receptor (InsP₃,R), Other actions that include modest changes in membrane permeability may also contribute to the Ca²⁺-mobilising action of MP and chimeric constructs.

Original language	English
Pages (from-to)	27-34
Number of pages	8
Journal	Cell Calcium
Volume	24
Issue number	1
DOIs	https://doi.org/10.1016/S0143-4160(98)90086-0
Publication status	Published - Jul 1998
Externally published	Yes

Funding

We would like to thank the BBSRC for a PhD studentship to CLL. In addition, we would also like to thank the Wellcome trust, The Swedish Institute and Swedish Research Council for Natural Sciences for financial support.

ASJC Scopus subject areas

Physiology
Molecular Biology
Cell Biology

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title = "Biochemical mechanisms of calcium mobilisation induced by mastoparan and chimeric hormone-mastoparan constructs",

abstract = "Ca2+ efflux, Ca2+-ATPase, and membrane permeability measurements were used to investigate the biochemical mechanisms of Ca2+ release induced by mastoparan (MP) and the chimeric hormone-Mp constructs incorporating galanin (galparan) or vasopressin antagonist (M375 and M391) moieties. Comparative studies utilised preparations of porcine cerebellar microsomes and rabbit skeletal muscle sarcoplasmic reticulum (SR), MP and chimeric peptides galparan, M375 and M391 induce Ca2+ release over a range of concentrations from 0.3-10 μM. Comparison of MP and three chimeric, N-terminal extended, constructs indicates that N-terminal extension modifies the biological properties of MP, producing changes in efficacy which are enzyme-isoform-specific. Biochemical studies indicate that the chimeric analogues and MP inhibit Ca2+-ATPases and directly activate the ryanodine receptor (RyR) to release Ca2+ from both heavy SR (HSR) and microsomes. The same peptides have no effect on the InsP3 receptor (InsP3,R), Other actions that include modest changes in membrane permeability may also contribute to the Ca2+-mobilising action of MP and chimeric constructs.",

author = "Longland, \{Clare L.\} and Mokdad Mezna and {\"U}lo Langel and Mattias H{\"a}llbrink and Ursel Soomets and Mark Wheatley and Francesco Michelangeli and John Howl",

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AU - Longland, Clare L.

AU - Mezna, Mokdad

AU - Langel, Ülo

AU - Hällbrink, Mattias

AU - Soomets, Ursel

AU - Wheatley, Mark

AU - Michelangeli, Francesco

AU - Howl, John

PY - 1998/7

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N2 - Ca2+ efflux, Ca2+-ATPase, and membrane permeability measurements were used to investigate the biochemical mechanisms of Ca2+ release induced by mastoparan (MP) and the chimeric hormone-Mp constructs incorporating galanin (galparan) or vasopressin antagonist (M375 and M391) moieties. Comparative studies utilised preparations of porcine cerebellar microsomes and rabbit skeletal muscle sarcoplasmic reticulum (SR), MP and chimeric peptides galparan, M375 and M391 induce Ca2+ release over a range of concentrations from 0.3-10 μM. Comparison of MP and three chimeric, N-terminal extended, constructs indicates that N-terminal extension modifies the biological properties of MP, producing changes in efficacy which are enzyme-isoform-specific. Biochemical studies indicate that the chimeric analogues and MP inhibit Ca2+-ATPases and directly activate the ryanodine receptor (RyR) to release Ca2+ from both heavy SR (HSR) and microsomes. The same peptides have no effect on the InsP3 receptor (InsP3,R), Other actions that include modest changes in membrane permeability may also contribute to the Ca2+-mobilising action of MP and chimeric constructs.

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Biochemical mechanisms of calcium mobilisation induced by mastoparan and chimeric hormone-mastoparan constructs

Abstract

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ASJC Scopus subject areas

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