Study on structure-property-reactivity-function relationship of human neuronal growth inhibitory factor (hGIF)

Zhi-Chun Ding, Qi Zheng, Bin Cai, Feng Yun Ni, Wen Hao Yu, Xing Chen Teng, Yuan Gao, Fang Liu, Dong Chen, Yang Wang, Hou Ming Wu, Hong Zhe Sun, Ming Jie Zhang, Xiang Shi Tan, Zhong Xian Huang

Research output: Contribution to journalShort survey

11 Citations (Scopus)

Abstract

Human metallothionein-3 (hMT3), also named as human neuronal growth inhibitory factor (hGIF), can inhibit the outgrowth of embryonic cortical neurons in the presence of brain extracts. In order to systematically study the structure-property-reactivity-function relationship of hGIF, our laboratory designed a series of mutants and studied their structure, property, reactivity and functions by a series of chemical and biological tools including UV spectroscopy, CD spectroscopy, NMR, chemical reaction and primary neuronal culture assays. In summary, we concluded that the bioactivity of hGIF was regulated by multiple factors, including the 6 CPCP 9 motif, an additional threonine insert at sequence position 5, domain-domain interactions, the structure and stability of the metal-thiolate cluster and the linker. Our studies provide more and more evidences which revealed that the bioactivity of hGIF is mainly related to the essential metal release and its characteristic conformation.

Original languageEnglish (US)
Pages (from-to)1965-1972
Number of pages8
JournalJournal of Inorganic Biochemistry
Volume102
Issue number11
DOIs
StatePublished - Nov 1 2008

Fingerprint

Bioactivity
Metals
Threonine
Ultraviolet spectroscopy
Nuclear magnetic resonance spectroscopy
Neurons
Conformations
Chemical reactions
Assays
Brain
Spectrum Analysis
Magnetic Resonance Spectroscopy
growth inhibitory factor

Keywords

  • Cell bioassay
  • Metallothionein (MT)
  • Mutation
  • Neuronal growth inhibitory factor (GIF)
  • Structure-function relationship

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Study on structure-property-reactivity-function relationship of human neuronal growth inhibitory factor (hGIF). / Ding, Zhi-Chun; Zheng, Qi; Cai, Bin; Ni, Feng Yun; Yu, Wen Hao; Teng, Xing Chen; Gao, Yuan; Liu, Fang; Chen, Dong; Wang, Yang; Wu, Hou Ming; Sun, Hong Zhe; Zhang, Ming Jie; Tan, Xiang Shi; Huang, Zhong Xian.

In: Journal of Inorganic Biochemistry, Vol. 102, No. 11, 01.11.2008, p. 1965-1972.

Research output: Contribution to journalShort survey

Ding, Z-C, Zheng, Q, Cai, B, Ni, FY, Yu, WH, Teng, XC, Gao, Y, Liu, F, Chen, D, Wang, Y, Wu, HM, Sun, HZ, Zhang, MJ, Tan, XS & Huang, ZX 2008, 'Study on structure-property-reactivity-function relationship of human neuronal growth inhibitory factor (hGIF)', Journal of Inorganic Biochemistry, vol. 102, no. 11, pp. 1965-1972. https://doi.org/10.1016/j.jinorgbio.2008.07.007
Ding, Zhi-Chun ; Zheng, Qi ; Cai, Bin ; Ni, Feng Yun ; Yu, Wen Hao ; Teng, Xing Chen ; Gao, Yuan ; Liu, Fang ; Chen, Dong ; Wang, Yang ; Wu, Hou Ming ; Sun, Hong Zhe ; Zhang, Ming Jie ; Tan, Xiang Shi ; Huang, Zhong Xian. / Study on structure-property-reactivity-function relationship of human neuronal growth inhibitory factor (hGIF). In: Journal of Inorganic Biochemistry. 2008 ; Vol. 102, No. 11. pp. 1965-1972.
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AU - Yu, Wen Hao

AU - Teng, Xing Chen

AU - Gao, Yuan

AU - Liu, Fang

AU - Chen, Dong

AU - Wang, Yang

AU - Wu, Hou Ming

AU - Sun, Hong Zhe

AU - Zhang, Ming Jie

AU - Tan, Xiang Shi

AU - Huang, Zhong Xian

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AB - Human metallothionein-3 (hMT3), also named as human neuronal growth inhibitory factor (hGIF), can inhibit the outgrowth of embryonic cortical neurons in the presence of brain extracts. In order to systematically study the structure-property-reactivity-function relationship of hGIF, our laboratory designed a series of mutants and studied their structure, property, reactivity and functions by a series of chemical and biological tools including UV spectroscopy, CD spectroscopy, NMR, chemical reaction and primary neuronal culture assays. In summary, we concluded that the bioactivity of hGIF was regulated by multiple factors, including the 6 CPCP 9 motif, an additional threonine insert at sequence position 5, domain-domain interactions, the structure and stability of the metal-thiolate cluster and the linker. Our studies provide more and more evidences which revealed that the bioactivity of hGIF is mainly related to the essential metal release and its characteristic conformation.

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