The Δ33-35 Mutant α-Domain Containing β-Domain-Like M3S9 Cluster Exhibits the Function of α-Domain with M4S11 Cluster in Human Growth Inhibitory Factor
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 i...
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| Format: | Article |
| Language: | English |
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Wiley
2010-01-01
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| Series: | Bioinorganic Chemistry and Applications |
| Online Access: | http://dx.doi.org/10.1155/2010/294169 |
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| author | Qingui Bao Zhichun Ding Zhong-Xian Huang Xiangshi Tan |
| author_facet | Qingui Bao Zhichun Ding Zhong-Xian Huang Xiangshi Tan |
| author_sort | Qingui Bao |
| collection | DOAJ |
| description | 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 Δ33-35 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. |
| format | Article |
| id | doaj-art-82ef34133eb04a54b162de3131a0e278 |
| institution | Kabale University |
| issn | 1565-3633 1687-479X |
| language | English |
| publishDate | 2010-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Bioinorganic Chemistry and Applications |
| spelling | doaj-art-82ef34133eb04a54b162de3131a0e2782025-02-03T01:28:00ZengWileyBioinorganic Chemistry and Applications1565-36331687-479X2010-01-01201010.1155/2010/294169294169The Δ33-35 Mutant α-Domain Containing β-Domain-Like M3S9 Cluster Exhibits the Function of α-Domain with M4S11 Cluster in Human Growth Inhibitory FactorQingui Bao0Zhichun Ding1Zhong-Xian Huang2Xiangshi Tan3Institute of Biomedical Science, Fudan University, 220 Handan Road, Shanghai 200433, ChinaDepartment of Chemistry, Fudan University, Shanghai 200433, ChinaDepartment of Chemistry, Fudan University, Shanghai 200433, ChinaInstitute of Biomedical Science, Fudan University, 220 Handan Road, Shanghai 200433, ChinaNeuronal 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 Δ33-35 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.http://dx.doi.org/10.1155/2010/294169 |
| spellingShingle | Qingui Bao Zhichun Ding Zhong-Xian Huang Xiangshi Tan The Δ33-35 Mutant α-Domain Containing β-Domain-Like M3S9 Cluster Exhibits the Function of α-Domain with M4S11 Cluster in Human Growth Inhibitory Factor Bioinorganic Chemistry and Applications |
| title | The Δ33-35 Mutant α-Domain Containing β-Domain-Like M3S9 Cluster Exhibits the Function of α-Domain with M4S11 Cluster in Human Growth Inhibitory Factor |
| title_full | The Δ33-35 Mutant α-Domain Containing β-Domain-Like M3S9 Cluster Exhibits the Function of α-Domain with M4S11 Cluster in Human Growth Inhibitory Factor |
| title_fullStr | The Δ33-35 Mutant α-Domain Containing β-Domain-Like M3S9 Cluster Exhibits the Function of α-Domain with M4S11 Cluster in Human Growth Inhibitory Factor |
| title_full_unstemmed | The Δ33-35 Mutant α-Domain Containing β-Domain-Like M3S9 Cluster Exhibits the Function of α-Domain with M4S11 Cluster in Human Growth Inhibitory Factor |
| title_short | The Δ33-35 Mutant α-Domain Containing β-Domain-Like M3S9 Cluster Exhibits the Function of α-Domain with M4S11 Cluster in Human Growth Inhibitory Factor |
| title_sort | δ33 35 mutant α domain containing β domain like m3s9 cluster exhibits the function of α domain with m4s11 cluster in human growth inhibitory factor |
| url | http://dx.doi.org/10.1155/2010/294169 |
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