Vallee B L
Center for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Boston, MA 02115, USA.
Neurochem Int. 1995 Jul;27(1):23-33. doi: 10.1016/0197-0186(94)00165-q.
Since its discovery in 1957 metallothionein (MT) has remained a protein in search of a function. After 40 years of frustrating efforts, three areas of research point to its zinc cluster structure as the basis of its functional potential: (1) the regulation of MT gene expression by zinc-dependent transcription factors, (2) neuronal growth inhibition in brain, and (3) interactions with glutathione and zinc proteins.
自1957年被发现以来，金属硫蛋白（MT）一直是一种有待明确功能的蛋白质。经过40年令人沮丧的研究，三个研究领域表明其锌簇结构是其潜在功能的基础：（1）锌依赖性转录因子对MT基因表达的调控，（2）大脑中神经元生长的抑制，以及（3）与谷胱甘肽和锌蛋白的相互作用。
