The intracellular chloride ion channel protein CLIC1 undergoes a redox-controlled structural transition.

Most proteins adopt a well defined three-dimensional structure; however, it is increasingly recognized that some proteins can exist with at least two stable conformations. Recently, a class of intracellular chloride ion channel proteins (CLICs) has been shown to exist in both soluble and integral membrane forms. The structure of the soluble form of CLIC1 is typical of a soluble glutathione S-transferase superfamily protein but contains a glutaredoxin-like active site.

Macrophage inhibitory cytokine 1 reduces cell adhesion and induces apoptosis in prostate cancer cells.

Macrophage inhibitory cytokine 1 (MIC-1), a divergent member of the transforming growth factor-beta superfamily, is linked to the pathogenesis of cancer. To delineate possible roles for MIC-1 in prostate cancer, a number of prostate epithelial cell lines have been studied, including PZ-HPV-7, DU-145, PC-3, and LNCaP cells. Factors regulating the production of MIC-1 protein by these cells and some of the effects of MIC-1 on them were investigated.

Recombinant CLIC1 (NCC27) assembles in lipid bilayers via a pH-dependent two-state process to form chloride ion channels with identical characteristics to those observed in Chinese hamster ovary cells expressing CLIC1.

CLIC1 (NCC27) is an unusual, largely intracellular, ion channel that exists in both soluble and membrane-associated forms. The soluble recombinant protein can be expressed in Escherichia coli, a property that has made possible both detailed electrophysiological studies in lipid bilayers and an examination of the mechanism of membrane integration. Soluble E.