DNase I interactions with filaments of skeletal muscles

Zimmer, Danna B.; Goldstein, M. A.

doi:10.1007/bf01767262

Cited by 10 publications

(5 citation statements)

References 25 publications

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“…The lengths and diameters of the Z band filaments observed in the reconstruction are consistent with known Z band components. The axial filaments have an F-actin core (Yamaguchi et al, 1983b;Zimmer and Goldstein, 1987a), and in the Z band appear to be covered by et-actinin (Tokuyasu et al, 1981;Zimmer and Goldstein, 1987b). The N10-nm diameter of the axial filaments in our reconstruction is consistent with this axial filament structure.…”

Section: Discussionsupporting

confidence: 73%

Three-dimensional structure of the Z band in a normal mammalian skeletal muscle.

Schroeter

Bretaudiere

Sass

et al. 1996

The Journal of Cell Biology

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Abstract. The three-dimensional structure of the vertebrate skeletal muscle Z band reflects its function as the muscle component essential for tension transmission between successive sarcomeres. We have investigated this structure as well as that of the nearby I band in a normal, unstimulated mammalian skeletal muscle by tomographic three-dimensional reconstruction from electron micrograph tilt series of sectioned tissue.The three-dimensional Z band structure consists of interdigitating axial filaments from opposite sarcomeres connected every 18 _+ 12 nm (mean _+ SD) to one to four cross-connecting Z-filaments. Most often, the cross-connecting Z-filaments are observed to meet the axial filaments in a fourfold symmetric arrangement. The substantial variation in the spacing between cross-connecting Z-filament to axial filament connection points suggests that the structure of the Z band is not determined solely by the arrangement of a-actinin to actin-binding sites along the axial filament. The cross-connecting filaments bind to or form a "relaxed interconnecting body" halfway between the axial filaments. This filamentous body is parallel to the Z band axial filaments and is observed to play an essential role in generating the small square lattice pattern seen in electron micrographs of unstimulated muscle cross sections. This structure is absent in cross sections of the Z band from muscles fixed in rigor or in tetanus, suggesting that the Z band lattice must undergo dynamic rearrangement concomitant with crossbridge binding in the A band.

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Section: Discussionsupporting

confidence: 73%

Three-dimensional structure of the Z band in a normal mammalian skeletal muscle.

Schroeter

Bretaudiere

Sass

et al. 1996

The Journal of Cell Biology

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“…Various other components have been localized to the Z-disc: a 220-kDa protein [153], Z-nin 12201, Z-protein [163], amorphin [37] which appears to be identical to phosphorylase b [142], zeugmatin [134], Cap Z, a barbed-end actin-capping protein [32], which is identical to p-actinin 198, 1441 and a 95-kDa protein that is released from myofibrils treated with DNase I, but which is not a-actinin by immunological criteria [277]. Cap Z is composed of two subunits of 32 kDa and 36 kDa and binds selectively to the (+) ends of actin filaments.…”

Section: The Z-discmentioning

confidence: 99%

The cytoskeletal lattice of muscle cells

Small¹,

Fürst²,

Thornell³

1993

EJB Reviews

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By modulating the level of structural organization of two primary components, actin and myosin, nature has devised a wide range of actin-based motile systems. At one extreme is the cross-striated muscle cell with its highly ordered and stable arrangement of filaments, specialised for rapid contractions. And at the other are non-muscle cells, like fibroblasts and amoebae, whose dynamic protrusive movements depend on the continual growth and breakdown of less organised actin filament arrays coupled, in some way, with the shearing of monomeric, tailless myosin molecules.Left to their own devices, in vitro, actin and myosin filaments can form contractile threads [268] but these are poorly organized and inefficient. Order in contractile assemblies must therefore be brought about by other components, accessory molecules, whose function is to link filaments with each other and with the cell membrane. In order to characterise such accessory molecules and gain insight into assembly principles, efforts have been mainly concentrated on vertebrate skeletal muscle. This system has been favoured, first, because it readily facilitates a combined biochemical and microscopic approach and, second, because early data (reviewed in [261 I) had already pointed to the existence in the sarcomere of structural material distinct from the contractile elements. Results accumulated over the last decade or so from skeletal muscle, together with complementary data from other systems, has now led to the recognition of a complex structural lattice in muscle cells; included in this lattice is an organised membrane skeleton whose components may play roles in maintaining sarcomere integrity. The purpose ofthis review is to survey recent advances in our understanding of the organisation and function of this structural lattice. The starting point is skeletal muscle but we shall also analyse cardiac and smooth muscle as well as other muscle types for which relevant information is available. Previous reviews of this subject have been presented by Obinata et al. [164], Wang [261], Maruyama [139], Price [181] and Trinick [239, 2401. CROSS-STRIATED MUSCLEIt is notable that the first indications of the existence of a structural lattice in striated muscle came in parallel with the discovery of the actin-and myosin-based sliding filament

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“…The anti-alpha-actinin Fab fragments used in this study were prepared from the same sera as those used previously in the analysis of DNAse extracts (Zimmer and Goldstein, 1987). Antibodies were raised in sheep against denatured alpha-actinin (Fuller et al, 19751, and an IgG fraction was isolated from the serum by ammonium sulfate fractionation (Fehay and Terry, 1978).…”

Section: Anti-alpha-actinin Generation and Purificationmentioning

confidence: 99%

Immunolocalization of Alpha‐Actinin in Adult Chicken Skeletal Muscles

Zimmer

Goldstein

1987

J. Elec. Microsc. Tech.

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Electron microscopy, Immunolabeling, Skeletal muscle KEY WORDS ABSTRACTImmunoelectron microscopy techniques were used to localize alpha-actinin within the Z lattice of adult skeletal muscles. Analysis of electron micrographs by direct visualization demonstrated that anti-alpha-actinin Fab fragments bound throughout the Z lattice. A low-resolution scanning densitometry technique was developed to quantitate the visual increase in the density of the Z lattice. These techniques did not allow determination of the particular component of the Z lattice, amorphous matrix, axial filaments, or cross-connecting filaments with which the antibody was associated. Therefore, additional techniques, including direct measurement of filament diameters and optical diffraction, were utilized in determining which components of the Z lattice bound anti-alpha-actinin Fab fragments. These analyses suggest that the antibody binding is distributed evenly throughout the lattice, along the filaments, and between them and is confined to the region of double overlap of the ends of the thin filaments.

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DNase I interactions with filaments of skeletal muscles

Cited by 10 publications

References 25 publications

Three-dimensional structure of the Z band in a normal mammalian skeletal muscle.

Three-dimensional structure of the Z band in a normal mammalian skeletal muscle.

The cytoskeletal lattice of muscle cells

Immunolocalization of Alpha‐Actinin in Adult Chicken Skeletal Muscles

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