The Δ33-35 mutant α-domain containing β-domain-like M 3S9 cluster exhibits the function of α-domain with M4S11 cluster in human growth inhibitory factor

Xiangshi Tan, Qingui Bao, Zhichun Ding, Zhong Xian Huang

Research output: Contribution to journalArticle

Abstract

Neuronal growth inhibitory factor (GIF), also known as metallothionein (metallothionein-3), impairs the survival and neurite formation of cultured neurons. It is known that the α-β domain-domain interaction of hGIF is crucial to the neuron growth inhibitory bioactivity although the exact mechanism is not clear. Herein, the β(MT3)-β(MT3) mutant and the hGIF-truncated Δ33-35 mutant were constructed, and their biochemical properties were characterized by pH titration, EDTA, and DTNB reactions. Their inhibitory activity toward neuron survival and neurite extension was also examined. We found that the Δ 33-35 mutant α-domain containing β-domain-like M3S9 cluster exhibits the function of α-domain with M4S11 cluster in hGIF. These results showed that the stability and solvent accessibility of the metal-thiolate cluster in β-domain is very significant to the neuronal growth inhibitory activity of hGIF and also indicated that the particular primary structure of α-domain is pivotal to domain-domain interaction in hGIF.

Original languageEnglish (US)
Article number294169
JournalBioinorganic Chemistry and Applications
Volume2010
DOIs
StatePublished - Jun 18 2010

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Neurons
Neurites
Dithionitrobenzoic Acid
Metallothionein
Growth
Bioactivity
Titration
Edetic Acid
Metals
Survival
growth inhibitory factor

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Inorganic Chemistry

Cite this

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title = "The Δ33-35 mutant α-domain containing β-domain-like M 3S9 cluster exhibits the function of α-domain with M4S11 cluster in human growth inhibitory factor",
abstract = "Neuronal growth inhibitory factor (GIF), also known as metallothionein (metallothionein-3), impairs the survival and neurite formation of cultured neurons. It is known that the α-β domain-domain interaction of hGIF is crucial to the neuron growth inhibitory bioactivity although the exact mechanism is not clear. Herein, the β(MT3)-β(MT3) mutant and the hGIF-truncated Δ33-35 mutant were constructed, and their biochemical properties were characterized by pH titration, EDTA, and DTNB reactions. Their inhibitory activity toward neuron survival and neurite extension was also examined. We found that the Δ 33-35 mutant α-domain containing β-domain-like M3S9 cluster exhibits the function of α-domain with M4S11 cluster in hGIF. These results showed that the stability and solvent accessibility of the metal-thiolate cluster in β-domain is very significant to the neuronal growth inhibitory activity of hGIF and also indicated that the particular primary structure of α-domain is pivotal to domain-domain interaction in hGIF.",
author = "Xiangshi Tan and Qingui Bao and Zhichun Ding and Huang, {Zhong Xian}",
year = "2010",
month = "6",
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doi = "10.1155/2010/294169",
language = "English (US)",
volume = "2010",
journal = "Bioinorganic Chemistry and Applications",
issn = "1565-3633",
publisher = "Hindawi Publishing Corporation",

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AU - Tan, Xiangshi

AU - Bao, Qingui

AU - Ding, Zhichun

AU - Huang, Zhong Xian

PY - 2010/6/18

Y1 - 2010/6/18

N2 - Neuronal growth inhibitory factor (GIF), also known as metallothionein (metallothionein-3), impairs the survival and neurite formation of cultured neurons. It is known that the α-β domain-domain interaction of hGIF is crucial to the neuron growth inhibitory bioactivity although the exact mechanism is not clear. Herein, the β(MT3)-β(MT3) mutant and the hGIF-truncated Δ33-35 mutant were constructed, and their biochemical properties were characterized by pH titration, EDTA, and DTNB reactions. Their inhibitory activity toward neuron survival and neurite extension was also examined. We found that the Δ 33-35 mutant α-domain containing β-domain-like M3S9 cluster exhibits the function of α-domain with M4S11 cluster in hGIF. These results showed that the stability and solvent accessibility of the metal-thiolate cluster in β-domain is very significant to the neuronal growth inhibitory activity of hGIF and also indicated that the particular primary structure of α-domain is pivotal to domain-domain interaction in hGIF.

AB - Neuronal growth inhibitory factor (GIF), also known as metallothionein (metallothionein-3), impairs the survival and neurite formation of cultured neurons. It is known that the α-β domain-domain interaction of hGIF is crucial to the neuron growth inhibitory bioactivity although the exact mechanism is not clear. Herein, the β(MT3)-β(MT3) mutant and the hGIF-truncated Δ33-35 mutant were constructed, and their biochemical properties were characterized by pH titration, EDTA, and DTNB reactions. Their inhibitory activity toward neuron survival and neurite extension was also examined. We found that the Δ 33-35 mutant α-domain containing β-domain-like M3S9 cluster exhibits the function of α-domain with M4S11 cluster in hGIF. These results showed that the stability and solvent accessibility of the metal-thiolate cluster in β-domain is very significant to the neuronal growth inhibitory activity of hGIF and also indicated that the particular primary structure of α-domain is pivotal to domain-domain interaction in hGIF.

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