Disulfide-linked S100β dimers and signal transduction

Steven W. Barger; Sandra R. Wolchok; Linda J. Van Eldik

doi:10.1016/0167-4838(92)90043-D

Disulfide-linked S100β dimers and signal transduction

Steven W. Barger
, Sandra R. Wolchok
, Linda J. Van Eldik

Producción científica: Article › revisión exhaustiva

114 Citas (Scopus)

Resumen

S100β is a calcium-binding protein with neurotrophic and mitogenic activities, both of which may be mediated by the protein's ability to stimulate an increase in intracellular free calcium ([Ca²⁺]). These extracellular trophic activities of S100β require a disulfide-linked, dimeric form of the protein. In this chapter, we present a minireview on the current state of knowledge concerning extracellular functions of S100β, with emphasis on the potential relevance of these activities to neuropathological disorders. We also report a simplified procedure for preparation of pharmacological amounts of biologically active S100β dimers, based on the finding that formation of disulfide-linked S100β dimers can be stimulated by the presence of calcium or lipid.

Idioma original	English
Páginas (desde-hasta)	105-112
Número de páginas	8
Publicación	BBA - Protein Structure
Volumen	1160
N.º	1
DOI	https://doi.org/10.1016/0167-4838(92)90043-D
Estado	Published - nov 10 1992

Nota bibliográfica

Funding Information:
These studies were supported in part by National Institutes of Health grants NS29215 and AG10208, and Biomedical Research Support Grant RR05424. We thank Drs. Thomas Lukas, Stefan Strack and D. Martin Watterson for helpful discussions during the course of these studies and Dr. Fridolin Sulser for the use of the laser densitometer. We are also grateful to Drs. J. Oliver Mclntyre and Sidney Fleischer for the gifts of phospholipids and advice concerning their preparation and use. Finally, the help of Dr. Stefan Strack and Ms. Jessica Taylor with some of the lipid studies is gratefully acknowledged.

Financiación

These studies were supported in part by National Institutes of Health grants NS29215 and AG10208, and Biomedical Research Support Grant RR05424. We thank Drs. Thomas Lukas, Stefan Strack and D. Martin Watterson for helpful discussions during the course of these studies and Dr. Fridolin Sulser for the use of the laser densitometer. We are also grateful to Drs. J. Oliver Mclntyre and Sidney Fleischer for the gifts of phospholipids and advice concerning their preparation and use. Finally, the help of Dr. Stefan Strack and Ms. Jessica Taylor with some of the lipid studies is gratefully acknowledged.

Financiadores	Número del financiador
National Institutes of Health (NIH)	RR05424, NS29215
National Institute on Aging	P01AG010208

ASJC Scopus subject areas

Molecular Biology
Structural Biology
Biophysics
Biochemistry

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title = "Disulfide-linked S100β dimers and signal transduction",

abstract = "S100β is a calcium-binding protein with neurotrophic and mitogenic activities, both of which may be mediated by the protein's ability to stimulate an increase in intracellular free calcium ([Ca2+]). These extracellular trophic activities of S100β require a disulfide-linked, dimeric form of the protein. In this chapter, we present a minireview on the current state of knowledge concerning extracellular functions of S100β, with emphasis on the potential relevance of these activities to neuropathological disorders. We also report a simplified procedure for preparation of pharmacological amounts of biologically active S100β dimers, based on the finding that formation of disulfide-linked S100β dimers can be stimulated by the presence of calcium or lipid.",

keywords = "Calcium, Disulfide, Growth factor, Lipid, Neurotrophic factor, S100",

author = "Barger, \{Steven W.\} and Wolchok, \{Sandra R.\} and \{Van Eldik\}, \{Linda J.\}",

note = "Funding Information: These studies were supported in part by National Institutes of Health grants NS29215 and AG10208, and Biomedical Research Support Grant RR05424. We thank Drs. Thomas Lukas, Stefan Strack and D. Martin Watterson for helpful discussions during the course of these studies and Dr. Fridolin Sulser for the use of the laser densitometer. We are also grateful to Drs. J. Oliver Mclntyre and Sidney Fleischer for the gifts of phospholipids and advice concerning their preparation and use. Finally, the help of Dr. Stefan Strack and Ms. Jessica Taylor with some of the lipid studies is gratefully acknowledged.",

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doi = "10.1016/0167-4838(92)90043-D",

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T1 - Disulfide-linked S100β dimers and signal transduction

AU - Barger, Steven W.

AU - Wolchok, Sandra R.

AU - Van Eldik, Linda J.

N1 - Funding Information: These studies were supported in part by National Institutes of Health grants NS29215 and AG10208, and Biomedical Research Support Grant RR05424. We thank Drs. Thomas Lukas, Stefan Strack and D. Martin Watterson for helpful discussions during the course of these studies and Dr. Fridolin Sulser for the use of the laser densitometer. We are also grateful to Drs. J. Oliver Mclntyre and Sidney Fleischer for the gifts of phospholipids and advice concerning their preparation and use. Finally, the help of Dr. Stefan Strack and Ms. Jessica Taylor with some of the lipid studies is gratefully acknowledged.

PY - 1992/11/10

Y1 - 1992/11/10

N2 - S100β is a calcium-binding protein with neurotrophic and mitogenic activities, both of which may be mediated by the protein's ability to stimulate an increase in intracellular free calcium ([Ca2+]). These extracellular trophic activities of S100β require a disulfide-linked, dimeric form of the protein. In this chapter, we present a minireview on the current state of knowledge concerning extracellular functions of S100β, with emphasis on the potential relevance of these activities to neuropathological disorders. We also report a simplified procedure for preparation of pharmacological amounts of biologically active S100β dimers, based on the finding that formation of disulfide-linked S100β dimers can be stimulated by the presence of calcium or lipid.

AB - S100β is a calcium-binding protein with neurotrophic and mitogenic activities, both of which may be mediated by the protein's ability to stimulate an increase in intracellular free calcium ([Ca2+]). These extracellular trophic activities of S100β require a disulfide-linked, dimeric form of the protein. In this chapter, we present a minireview on the current state of knowledge concerning extracellular functions of S100β, with emphasis on the potential relevance of these activities to neuropathological disorders. We also report a simplified procedure for preparation of pharmacological amounts of biologically active S100β dimers, based on the finding that formation of disulfide-linked S100β dimers can be stimulated by the presence of calcium or lipid.

KW - Calcium

KW - Disulfide

KW - Growth factor

KW - Lipid

KW - Neurotrophic factor

KW - S100

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U2 - 10.1016/0167-4838(92)90043-D

DO - 10.1016/0167-4838(92)90043-D

M3 - Article

C2 - 1420327

AN - SCOPUS:0026463640

SN - 0167-4838

VL - 1160

SP - 105

EP - 112

JO - BBA - Protein Structure

JF - BBA - Protein Structure

IS - 1

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Disulfide-linked S100β dimers and signal transduction

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Nota bibliográfica

Financiación

ASJC Scopus subject areas

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