粘虫蛾飞行肌的发育：超微结构特征分析

应用电子显微镜对正常条件下饲养的0-16日龄粘虫Mythimna separata (Walker)雌蛾飞行肌超微结构的研究结果表明：肌原纤维直径。线粒体和横管的体积分量均随蛾龄的增加而增加,到7日龄达到最大值以后又随蛾龄的增加而下降;但是,肌节长度则随蛾龄的增加而缩短,到7日龄达到最短后又随蛾龄的增加而延长,从而使整条发育曲线呈“V”字形;肌原纤维和肌质网体积分量变化不大或无规律可寻;二位体在发育初期和未期的比例较高,而三位体在4和7口龄比例较高;肌丝排列从0～7日龄均是有序的,肌动蛋白丝(细丝)和肌球蛋白丝(粗丝)的数量比为3：1,粗丝的数量变化也不大,每根肌原纤维约有600根。但从10日龄开始肌丝排列出现紊乱,细丝全部消失,粗丝降解、数量减少了30%,从而使肌原纤维留下一片片的空白。根据这些结果,把7日龄前的飞行肌发育过程视为生长过程,而把10日龄后的视作降解过程。最后对粘虫蛾飞行肌与卵巢发育及其飞行能力变化的关系进行了讨论。     

粘虫蛾飞行肌超微结构的研究

应用电子显微镜对粘虫雌蛾Mythimna separata(Walker)飞行(背纵)肌的研究结果表明,其肌原纤维由500-700根肌球蛋白丝(粗丝)组成,每根粗丝由6根肌动蛋白丝(细丝)环绕排列成六角形,每根细丝精确地位于两根粗丝间1/2处,从而使粗丝和细丝的比为1：3。肌节较短,长度约2.2-2.6μm。肌原纤维之间充满着线粒体和横管。每个肌节约有线粒体三个,横管二根。线粒体约占肌纤维体积的40%,而横管为7%。每根横管准确地位于肌节的1/4、3/4处,或Z线和中膈的中央,并与肌质网交接形成二位体(dyads)或三位体(triads)。肌质网相当不发达,约占肌纤维体积的2.5%。但其分布很有特色,即除了紧贴于肌原纤维周围的由单层液泡组成的肌质网以外,在中膈处还有一层横穿于肌原纤维的肌质网。和其它同步飞行肌的结构和功能分析比较的结果还表明,粘虫蛾飞行肌具有较善于飞行的结构。     

Cardiac myocytes' dynamic contractile behavior differs depending on heart segment

Cardiac myocytes originating from different parts of the heart exhibit varying morphology and ultrastructure. However, the difference in their dynamic behavior is unclear. We examined the contraction of cardiac myocytes originating from the apex, ventricle, and atrium, and found that their dynamic behavior, such as amplitude and frequency of contraction, differs depending on the heart segment of origin. Using video microscopy and high‐precision image correlation, we found that: (1) apex myocytes exhibited the highest contraction rate (～17 beats/min); (2) ventricular myocytes exhibited the highest contraction amplitude (～5.2 micron); and (3) as myocyte contraction synchronized, their frequency did not change significantly, but the amplitude of contraction increased in apex and ventricular myocytes. In addition, as myocyte cultures mature they formed contractile filaments, further emphasizing the difference in myocyte dynamics is persistent. These results suggest that the dynamic behavior (in addition to static properties) of myocytes is dependent on their segment of origin. Biotechnol. Bioeng. 2013; 110: 628–636. © 2012 Wiley Periodicals, Inc.     

Skeletal muscle design to meet functional demands

Skeletal muscles are length- and velocity-sensitive force producers, constructed of a vast array of sarcomeres. Muscles come in a variety of sizes and shapes to accomplish a wide variety of tasks. How does muscle design match task performance? In this review, we outline muscle''s basic properties and strategies that are used to produce movement. Several examples are provided, primarily for human muscles, in which skeletal muscle architecture and moment arms are tailored to a particular performance requirement. In addition, the concept that muscles may have a preferred sarcomere length operating range is also introduced. Taken together, the case is made that muscles can be fine-tuned to perform specific tasks that require actuators with a wide range of properties.     

Stretch-induced growth of blowfly muscle

The expansion of the adult blowfly after it has emerged from the puparium was accompanied by an increase in the length of the longitudinal and tergo-sternal flight muscles by 26% and of the tergo-trochanteral leg muscle by 30%. The increases in muscle length were accompanied by similar increases in sarcomere length. Over the 2 hr between emergence and expansion the activity of the actomyosin ATPase increased by over 3 fold and the amount of actomyosin per thorax increased by 3 fold. Ligaturing the proboscis of the newly-emerged fly prevented the expansion of the fly, prevented the increase in the length of the muscles and sarcomeres and the increase in actomyosin activity and quantity. Stretching is proposed as the stimulus inducing increases in the length of the thick and thin filaments.     

Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin

Sarcomeric filament proteins display extraordinary properties in terms of protein length and mechanical elasticity, requiring specific anchoring and assembly mechanisms. To establish the molecular basis of terminal filament assembly, we have selected the sarcomeric M-band protein myomesin as a prototypic filament model. The crystal structure of the myomesin C-terminus, comprising a tandem array of two immunoglobulin (Ig) domains My12 and My13, reveals a dimeric end-to-end filament of 14.3 nm length. Although the two domains share the same fold, an unexpected rearrangement of one beta-strand reveals how they are evolved into unrelated functions, terminal filament assembly (My13) and filament propagation (My12). The two domains are connected by a six-turn alpha-helix, of which two turns are void of any interactions with other protein parts. Thus, the overall structure of the assembled myomesin C-terminus resembles a three-body beads-on-the-string model with potentially elastic properties. We predict that the found My12-helix-My13 domain topology may provide a structural template for the filament architecture of the entire C-terminal Ig domain array My9-My13 of myomesin.     

Alternative S2 hinge regions of the myosin rod differentially affect muscle function, myofibril dimensions and myosin tail length

Muscle myosin heavy chain (MHC) rod domains intertwine to form alpha-helical coiled-coil dimers; these subsequently multimerize into thick filaments via electrostatic interactions. The subfragment 2/light meromyosin "hinge" region of the MHC rod, located in the C-terminal third of heavy meromyosin, may form a less stable coiled-coil than flanking regions. Partial "melting" of this region has been proposed to result in a helix to random-coil transition. A portion of the Drosophila melanogaster MHC hinge is encoded by mutually exclusive alternative exons 15a and 15b, the use of which correlates with fast (hinge A) or slow (hinge B) muscle physiological properties. To test the functional significance of alternative hinge regions, we constructed transgenic fly lines in which fast muscle isovariant hinge A was switched for slow muscle hinge B in the MHC isoforms of indirect flight and jump muscles. Substitution of the slow muscle hinge B impaired flight ability, increased sarcomere lengths by approximately 13% and resulted in minor disruption to indirect flight muscle sarcomeric structure compared with a transgenic control. With age, residual flight ability decreased rapidly and myofibrils developed peripheral defects. Computational analysis indicates that hinge B has a greater coiled-coil propensity and thus reduced flexibility compared to hinge A. Intriguingly, the MHC rod with hinge B was approximately 5 nm longer than myosin with hinge A, consistent with the more rigid coiled-coil conformation predicted for hinge B. Our study demonstrates that hinge B cannot functionally substitute for hinge A in fast muscle types, likely as a result of differences in the molecular structure of the rod, subtle changes in myofibril structure and decreased ability to maintain sarcomere structure in indirect flight muscle myofibrils. Thus, alternative hinges are important in dictating the distinct functional properties of myosin isoforms and the muscles in which they are expressed.     

Fiber architecture of the extensors of the hindlimb in semiterrestrial and arboreal guenons

Fiber architecture of the extensor musculature of the knee and ankle is examined in two African guenon species—the semiterrestrial Cercopithecus aethiops, and the arboreal C. ascanius. Using histologic and microscopic techniques to measure lengths of sarcomeres, the original lengths of muscle fasciculi and angles of pinnation in quadriceps femoris and triceps surae are reconstructed from direct measurements on cadavers. Calculations of reduced physiological cross-sectional area, mass/predicted effective tetanic tension, maximum excursion, and tendon length/fasciculus + tendon lengths are correlated to preferred locomotor modalities in the wild. For both species, greater morphological differences occur among the bellies of quadriceps femoris—rectus femoris, vastus intermedius, v. lateralis, and v. medialis—than among the bellies of triceps surae—gastrocnemius lateralis, g. medialis, plantaris, and soleus. With regard to quadriceps femoris, few differences occur between species. Interspecific differences in the triceps surae indicate (1) redirection of muscle force to accommodate arboreality in which the substrate is less than body width; (2) muscles more suited for velocity in the semiterrestrial vervets; and (3) muscles used more isotonically in vervets and more isometrically in red-tailed monkeys. The inherent flexibility of muscle may be preadaptive to a primary species shift in locomotor modality until the bony morphology is able to adapt through natural selection. © 1996 Wiley-Liss, Inc.     

Cardiac sarcomere mechanics in health and disease

The sarcomere is the fundamental structural and functional unit of striated muscle and is directly responsible for most of its mechanical properties. The sarcomere generates active or contractile forces and determines the passive or elastic properties of striated muscle. In the heart, mutations in sarcomeric proteins are responsible for the majority of genetically inherited cardiomyopathies. Here, we review the major determinants of cardiac sarcomere mechanics including the key structural components that contribute to active and passive tension. We dissect the molecular and structural basis of active force generation, including sarcomere composition, structure, activation, and relaxation. We then explore the giant sarcomere-resident protein titin, the major contributor to cardiac passive tension. We discuss sarcomere dynamics exemplified by the regulation of titin-based stiffness and the titin life cycle. Finally, we provide an overview of therapeutic strategies that target the sarcomere to improve cardiac contraction and filling.