Key result
Antifreeze polypeptides from the winter flounder effectively suppressed calcium and potassium currents in porcine granulosa cells, indicating a protein-protein interaction mechanism.
Why the study?
Do antifreeze polypeptides from the winter flounder suppress calcium and potassium currents in porcine granulosa cells?
Do antifreeze polypeptides from the winter flounder suppress calcium and potassium currents in porcine granulosa cells?
Antifreeze proteins from winter flounder possess a novel property of blocking calcium and potassium ion channels, suggesting a protein-protein interaction mechanism.
Answers are grounded in this paper and cite their sources.
No immediate clinical implications; extends preclinical evidence of antifreeze polypeptide effects on mammalian ion channels.
For the last two decades, the research on fish "antifreeze" proteins has focused exclusively on their ability to depress noncolligatively blood plasma freezing points, presumably by binding to ice crystals. We report evidence that antifreeze polypeptides from the winter flounder (Pseudopleuronectes americanus) have another special property, the ability to block ion channels. In experiments with porcine granulosa cells we show, using the patch-clamp technique in the whole cell configuration, that these proteins suppress effectively calcium and potassium currents. The results of dose-response studies indicate a protein-protein interaction mechanism.
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Rubinsky et al. (1992) studied this question. Antifreeze polypeptides from the winter flounder (Pseudopleuronectes americanus) was evaluated on Calcium and potassium currents. Antifreeze polypeptides from the winter flounder effectively suppressed calcium and potassium currents in porcine granulosa cells, indicating a protein-protein interaction mechanism.
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