Characterization and localization of α-connectin (titin 1): An elastic protein isolated from rabbit skeletal muscle

Kimura, Sumiko; Matsuura, Tetsu; Ohtsuka, Satoshi; Nakauchi, Yuni; Matsuno, Akira; Maruyama, Kosçak

doi:10.1007/bf01738426

Cited by 50 publications

(29 citation statements)

References 41 publications

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“…This second band is assumed to be a proteolytic fragment of T1; however the presence of this fragment in the literature seems to be independent of the muscle sample preparation procedures (Wang et al 1991;Horowits 1992;Fry et al 1997). In addition, the estimated molecular weights of these two proteins have been reported at several different values independent of migration distance, leading to some confusion (Kimura et al 1992;Granzier and Wang 1993;Weicker 1997). This investigation followed procedures outlined by Granzier and Wang (1993) to ensure proteolytic activity was kept to a minimum.…”

Section: Discussionmentioning

confidence: 98%

Characteristics of titin in strength and power athletes

McBride¹,

Triplett-McBride²,

Davie

et al. 2003

Eur J Appl Physiol

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The purpose of this investigation was to identify characteristics of the muscle protein titin in different athletic populations with increased levels of strength and power relative to non-athletes. Subjects fell into one of four groups: (1) non-athletes (NA) ( n=5), (2) weightlifters (WL) (n=5), (3) powerlifters (PL) (n=5), (4) sprinters (S) (n=5). A one repetition maximum in the squat exercise was performed to assess strength. In addition, countermovement vertical jump trials were performed to assess power capabilities. Peak power (W(peak)) was calculated for the vertical jumps from force plate measurements. From gel electrophoresis analyses of muscle samples, titin-1 (T1) and titin-2 (T2) protein bands were identified, quantified and expressed relative to each other. In addition the relative mobility (R(f)) of T1 and T2 was determined as an estimate of molecular weight. The NA group [%T1=47.8 (5.1), %T2=52.2 (5.1), mean (SE)] had lower T1 and higher T2 percentages than WL [%T1=62.3 (6.6), %T2=37.7 (6.6)], PL [%T1=66.8 (5.0), %T2=33.2 (5.0)] and S [%T1=65.9 (4.9), %T2=34.1 (4.9)] groups (P< or =0.10, preliminary investigation into titin and exercise justifies more liberal alpha level). No significant differences were found in R(f) of T1 or T2 between the groups. This investigation has shown that there is a differential expression of titin protein bands in competitive athletes with increased levels of strength and power in comparison to untrained non-athletic individuals. Some relationships between titin characteristics and athletic performance were observed; however, no conclusions can be made based on these data as to the contribution of titin to strength or power capabilities.

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Section: Discussionmentioning

confidence: 98%

Characteristics of titin in strength and power athletes

McBride¹,

Triplett-McBride²,

Davie

et al. 2003

Eur J Appl Physiol

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“…An SDS-PAGE (SDS-polyacrylamide gel electrophoresis) analysis of myofibrils was made following Kimura et al [18]. Calpain-and trypsin-treated myofibrils used for SDS-PAGE were prepared under the same proteolytic conditions employed for preparing calpain-and trypsin-treated myofibrils used for AFM experiments.…”

Section: Preparation Of Myofibrilsmentioning

confidence: 99%

Transverse Stiffness of Myofibrils of Skeletal and Cardiac Muscles Studied by Atomic Force Microscopy

et al. 2006

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Abstract:The transverse stiffness of single myofibrils of skeletal and cardiac muscles was examined by atomic force microscopy. The microscopic images of both skeletal and cardiac myofibrils in a rigor state showed periodical striation patterns separated by Z-bands, which is characteristic of striated muscle fibers. However, sarcomere patterns were hardly distinguishable in the stiffness distributions of the relaxed myofibrils of skeletal and cardiac muscles. Myofibrils in a rigor state were significantly stiff compared with those in a relaxed state, and in each state, cardiac myofibrils were significantly stiffer compared with skeletal myofibrils. By proteolytic digestions of sarcomere components of myofibrils, it was suggested that cardiac myofibrils are laterally stiffer than skeletal myofibrils because Z-bands, connectin (titin) filament networks, and other components of sarcomere structures for the former myofibrils are stronger than those for the latter.

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“…SDS-PAGE analysis of myofibril preparations was made following the method of Kimura et al (1992) as detailed in Akiyama et al (2006). Myofibril preparations were dissolved in an SDS solution and an aliquot of the solution was applied to a gradient gel (2.5-12%).…”

Section: Preparations Of Myofibrilsmentioning

confidence: 99%

Mechanical Strength of Sarcomere Structures of Skeletal Myofibrils Studied by Submicromanipulation

Kayamori

Miyake

Akiyama

et al. 2006

Cell Struct. Funct.

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ABSTRACT. The mechanical strength of sarcomere structures of skeletal muscle was studied by rupturing single myofibrils of rabbit psoas muscle by submicromanipulation techniques. Microbeads coated with α-actinin were attached to the surface of myofibrils immobilized to coverslip. By use of either optical tweezers or atomic force microscope, the attached beads were captured and detached from the myofibrils. During the detachment of the beads, the actin filaments bound specifically to the beads were peeled off from the bulk structures of myofibrils, thus rupturing the peripheral components of the myofibrils bound to the actin filaments. By analyzing the ruptures thus produced in various myofibril preparations, it was found that the sarcomere structure of myofibrils is maintained by numerous molecular components having the mechanical strength sufficient to sustain the contractile force produced by the actomyosin system. The present techniques could be applied to study the mechanical strength of cellular organelles containing actin filaments as their component.

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Characterization and localization of α-connectin (titin 1): An elastic protein isolated from rabbit skeletal muscle

Cited by 50 publications

References 41 publications

Characteristics of titin in strength and power athletes

Characteristics of titin in strength and power athletes

Transverse Stiffness of Myofibrils of Skeletal and Cardiac Muscles Studied by Atomic Force Microscopy

Mechanical Strength of Sarcomere Structures of Skeletal Myofibrils Studied by Submicromanipulation

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