NEM-HMM serves as a specific probe for actomyosin interactions, demonstrating tight binding to actin and inhibition of actomyosin-dependent contractile processes without affecting microtubule or cilia functions.
May enable selective actomyosin probing in models; leaves open cardiac translation.
Treatment of rabbit skeletal muscle heavy meromyosin (HMM) with the sulfhydryl reagent N-ethylmaleimide (NEM) produces a species of HMM which remains tightly bound to actin in the presence of MgATP. NEM-HMM forms characteristic "arrowhead" complexes with actin which persist despite rinses with MgATP. NEM-HMM inhibits the actin activation of native HMM-ATPase activity, the superprecipitation of actomyosin, the contraction of glycerinated muscle myofibrils, and the contraction of cytoplasmic strands of the soil amoeba Chaos carolinensis. However, NEM-HMM does not interfere with in vitro microtubule polymerization or beating of demembranated cilia.
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Meeusen et al. (1979) studied this question.
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