Effects of urea on actin-activated Mg2+-ATPase of requiem shark myosin

Kanoh, Satoshi; Niwa, Eiji; Osaka, Yoshiki; Watabe, Shugo

doi:10.1016/s0305-0491(99)00025-5

Cited by 9 publications

(10 citation statements)

References 39 publications

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“…In previous investigations, myofibrils from requiem shark fast skeletal muscle showed urea‐resistibility for Ca 2+ ‐ and Mg 2+ ‐ATPase activities 14 . A high resistibility against urea in actin‐activated Mg 2+ ‐ATPase of requiem shark myosin was partly accounted for by its stable interaction with actin 18 . Furthermore, the α‐helical structure of requiem shark myosin was highly resistant to urea 23 .…”

Section: Introductionmentioning

confidence: 92%

“…Yancey and Somero 20 suggested that the primary sequence of A 4 ‐LDH from marine elasmobranch fish is altered so that its structure is resistant to high concentrations of urea. Marine elasmobranch myofibrils also have resistant properties to urea 15–19,21,22 . In previous investigations, myofibrils from requiem shark fast skeletal muscle showed urea‐resistibility for Ca 2+ ‐ and Mg 2+ ‐ATPase activities 14 .…”

Section: Introductionmentioning

confidence: 95%

“…The other strategy is to develop protein structures that are resistant to urea 5,13,14 . Proteins from marine elasmobranch fish have been reported to function even in physiological concentrations of urea 13–19 without methylamines. Yancey and Somero 20 suggested that the primary sequence of A 4 ‐LDH from marine elasmobranch fish is altered so that its structure is resistant to high concentrations of urea.…”

Section: Introductionmentioning

confidence: 99%

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Effects of urea and trimethylamine-N-oxide on ATPase of requiem shark myofibril and its constituents

et al. 2001

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The effects of trimethylamine‐N‐oxide (TMAO) on the urea‐resistibility of requiem shark myofibrils were investigated, using Ca2+‐ and Mg2+‐ATPase activities as a parameter. Both activities were hardly changed or activated up to 0.6 M urea. In contrast, the two activities both decreased to less than 50% in the presence of TMAO up to 0.5 M. When measured at a 2 : 1 molar ratio of urea and TMAO, Ca2+‐ and Mg2+‐ATPase activities were similar to those in the presence of TMAO alone, indicating that TMAO reduced the urea‐resistibility of myofibrils. Myosin, the most abundant protein in myofibrils, from requiem shark exhibited the effects of urea and TMAO on its Ca2+‐ATPase activity, which was primarily similar to those of myofibrils. However, Ca2+‐ATPase activities in the coexistence of urea and TMAO for actomyosin reconstituted from requiem shark myosin and chicken F‐actin were approximately average of those measured independently in the presence of either urea or TMAO alone. Carp myofibrils, reconstituted actomyosin and myosin, which were used as teleost references, all showed a tendency in the effects of urea and TMAO on Ca2+‐ATPase activities that was similar to those of requiem shark counterparts.

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Section: Introductionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

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Effects of urea and trimethylamine-N-oxide on ATPase of requiem shark myofibril and its constituents

et al. 2001

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“…Similarly, activity of myosin ATPase from requiem shark (Triakis scyllia) is just as sensitive to urea as is carp myosin, but sensitivity is eliminated by actin binding (Kanoh et al, 1999). See Yancey (2005) for other examples.…”

Section: Osmolyte Properties: Inorganic Ions Versus Compatible Solutesmentioning

confidence: 99%

Co-evolution of proteins and solutions: protein adaptation versus cytoprotective micromolecules and their roles in marine organisms

Yancey

Siebenaller

2015

Journal of Experimental Biology

128

116

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Organisms experience a wide range of environmental factors such as temperature, salinity and hydrostatic pressure, which pose challenges to biochemical processes. Studies on adaptations to such factors have largely focused on macromolecules, especially intrinsic adaptations in protein structure and function. However, micromolecular cosolutes can act as cytoprotectants in the cellular milieu to affect biochemical function and they are now recognized as important extrinsic adaptations. These solutes, both inorganic and organic, have been best characterized as osmolytes, which accumulate to reduce osmotic water loss. Singly, and in combination, many cosolutes have properties beyond simple osmotic effects, e.g. altering the stability and function of proteins in the face of numerous stressors. A key example is the marine osmolyte trimethylamine oxide (TMAO), which appears to enhance water structure and is excluded from peptide backbones, favoring protein folding and stability and counteracting destabilizers like urea and temperature. Co-evolution of intrinsic and extrinsic adaptations is illustrated with high hydrostatic pressure in deep-living organisms. Cytosolic and membrane proteins and G-protein-coupled signal transduction in fishes under pressure show inhibited function and stability, while revealing a number of intrinsic adaptations in deep species. Yet, intrinsic adaptations are often incomplete, and those fishes accumulate TMAO linearly with depth, suggesting a role for TMAO as an extrinsic 'piezolyte' or pressure cosolute. Indeed, TMAO is able to counteract the inhibitory effects of pressure on the stability and function of many proteins. Other cosolutes are cytoprotective in other ways, such as via antioxidation. Such observations highlight the importance of considering the cellular milieu in biochemical and cellular adaptation.

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“…The urea resistibility of marine elasmobranch myofibrillar proteins against inactivation of ATPase activity has been argued. [4][5][6][7] For example, it was shown in our previous investigation that a high resistibility of actinactivated Mg 2+ -ATPase activity of shark myosin against urea is partly accounted for by its stable interaction with actin. 4 The objective of the present study was to measure the surface hydrophobicity of requiem shark myosin as well as those of its subfragment-1 (S1) and rod at various urea concentrations, and to compare the results obtained with those of carp counterparts for a better understanding of the mechanisms involved in structural changes of the myosin molecule by urea.…”

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confidence: 98%