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淡水甲壳类动物破坏螯虾爪部的皮肤短肌节和长肌节肌纤维最大激活特性的差异。

Differences in maximal activation properties of skinned short- and long-sarcomere muscle fibres from the claw of the freshwater crustacean Cherax destructor.

作者信息

West J M, Humphris D C, Stephenson D G

机构信息

Department of Zoology, La Trobe University, Bundoora, Victoria, Australia.

出版信息

J Muscle Res Cell Motil. 1992 Dec;13(6):668-84. doi: 10.1007/BF01738256.

Abstract

Single fibres of different sarcomere length at rest have been isolated from the claw muscle of the yabby (Cherax destructor), a decapod crustacean. Fibres of either long (SL > 6 microns) or short (SL < 4 microns) sarcomere length have been mechanically skinned and were maximally activated by Ca2+ and Sr2+ under various experimental conditions (ionic strength, in the presence of 2,3 butanedione monoxime (BDM)) to determine differences in their contractile properties. Isometric force was measured simultaneously with either myofibrillar MgATPase or fibre stiffness in both fibre types. The ultrastructure of individual long- and short-sarcomere fibres was also determined by electron microscopy. The long-sarcomere fibres developed greater tension (30.48 +/- 1.72 N cm-2) when maximally activated by Ca2+ compared with the short-sarcomere fibres (18.60 +/- 0.80 N cm-2). The difference in the maximum Ca(2+)-activated force can be explained by the difference in the amount of filament overlap between the two fibre types. The maximum Ca(2+)-activated myofibrillar MgATPase rate in the short-sarcomere fibres (1.60 +/- 0.27 mmol ATP l-1s-1) was higher, but not significantly different from the ATPase rate in fibres with long-sarcomeres (1.09 +/- 0.14 mmol ATP l-1s-1). As the concentration of myosin is estimated to be higher only by a factor of 1.22 in the short-sarcomere preparations there is no evidence to suggest that the myofibrillar MgATPase activity is different in the long- and short-sarcomere preparations. The maximum Ca(2+)-activated force (P0) of both short- and long-sarcomere fibres was quite insensitive to BDM compared with vertebrate muscle. Force decreased to 60.2 +/- 5.3% and 76.1 +/- 2.7% in the short- and long-sarcomere fibres respectively in the presence of 100 mmol l-1 BDM. The difference in the force depression between the long- and short-sarcomere fibres is statistically significant (p < 0.05). Fibre stiffness during maximum Ca(2+)-activation expressed as percentage maximum force per nm per half sarcomere was higher by a factor of 3.5 in short-sarcomere fibres than in long-sarcomere fibres suggesting that the compliance of the filaments in the long-sarcomere fibres is considerably higher than in the short-sarcomere fibres. Sr2+ could not activate the contractile apparatus to the same level as that seen by Ca2+ in either fibre type: the maximum Sr(2+)-activated force was (20 +/- 3%) and (63 +/- 3%) of the maximum Ca(2+)-activated force response in short- and long-sarcomere fibres, respectively.(ABSTRACT TRUNCATED AT 400 WORDS)

摘要

已从十足目甲壳动物亚比虾(Cherax destructor)的爪肌中分离出处于静息状态下不同肌节长度的单根肌纤维。已对肌节长度长(SL>6微米)或短(SL<4微米)的肌纤维进行了机械去膜处理,并在各种实验条件(离子强度、在2,3-丁二酮单肟(BDM)存在的情况下)下由Ca2+和Sr2+使其达到最大激活状态,以确定它们收缩特性的差异。在两种纤维类型中,等长力与肌原纤维MgATP酶或纤维硬度同时进行测量。还通过电子显微镜确定了单个长肌节和短肌节纤维的超微结构。与短肌节纤维(18.60±0.80N/cm2)相比,长肌节纤维在被Ca2+最大激活时产生更大的张力(30.48±1.72N/cm2)。两种纤维类型之间细丝重叠量的差异可以解释最大Ca(2+)激活力的差异。短肌节纤维中最大Ca(2+)激活的肌原纤维MgATP酶速率(1.60±0.27mmol ATP·l-1·s-1)较高,但与长肌节纤维中的ATP酶速率(1.09±0.14mmol ATP·l-1·s-1)无显著差异。由于估计短肌节制剂中肌球蛋白的浓度仅高1.22倍,因此没有证据表明长肌节和短肌节制剂中肌原纤维MgATP酶活性不同。与脊椎动物肌肉相比,短肌节和长肌节纤维的最大Ca(2+)激活力(P0)对BDM相当不敏感。在100mmol·l-1 BDM存在的情况下,短肌节和长肌节纤维中的力分别降至60.2±5.3%和76.1±2.7%。长肌节和短肌节纤维之间力降低的差异具有统计学意义(p<0.05)。最大Ca(2+)激活期间以每半肌节每纳米最大力的百分比表示的纤维硬度,短肌节纤维比长肌节纤维高3.5倍,这表明长肌节纤维中细丝的顺应性比短肌节纤维高得多。Sr2+不能将收缩装置激活到与任何一种纤维类型中Ca2+所见相同的水平:短肌节和长肌节纤维中最大Sr(2+)激活力分别为最大Ca(2+)激活力反应的(20±3%)和(63±3%)。(摘要截断于400字)

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