Three classes of filaments in cardiac differentiation

Rash, John E.; Biesele, John J.; Gey, George O.

doi:10.1016/s0022-5320(70)90171-1

Cited by 72 publications

(22 citation statements)

References 87 publications

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“…17-20). (26)(27)(28). Morphologically, the area of the fascia adherens was considered as the terminal Z line and it was assumed that these two structures are biochemically related (26)(27)(28).…”

Section: Discussionmentioning

confidence: 99%

“…(26)(27)(28). Morphologically, the area of the fascia adherens was considered as the terminal Z line and it was assumed that these two structures are biochemically related (26)(27)(28). In developing skeletal or in heart muscle cells, Z lines are quite frequently seen to originate from intercellular desmosomes or from electron dense membrane continuations of such areas which resemble morphologically the electron-dense material of the fascia adherens (26,27,29 (30).…”

Section: Discussionmentioning

confidence: 99%

“…Morphologically, the area of the fascia adherens was considered as the terminal Z line and it was assumed that these two structures are biochemically related (26)(27)(28). In developing skeletal or in heart muscle cells, Z lines are quite frequently seen to originate from intercellular desmosomes or from electron dense membrane continuations of such areas which resemble morphologically the electron-dense material of the fascia adherens (26,27,29 (30). On the basis of this morphological evidence, the assumption was made that the electron-dense material found in association with the muscle Z lines and the muscle intercellular junctions are biochemically related and share at least one structural component (12,(26)(27)(28) The role of the actin that copurifies with desmin in the structure of 100 A filaments is presently unknown.…”

Section: Discussionmentioning

confidence: 99%

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Immunological characterization of the subunit of the 100 A filaments from muscle cells.

Lazarides¹,

Hubbard²

1976

Proc. Natl. Acad. Sci. U.S.A.

367

189

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We report the immunological characterization of the subunit of the intermediate sized (100 A) filaments from muscle cells. The protein as isolated from smooth muscle (chicken gizzard) has an apparent molecular weight of 50,000. It is insoluble in buffers that solubilize myosin and the majority of actin, but becomes soluble in the presence of urea. Under a variety of experimental conditions, that include the presence of 8 M urea, this new protein comigrates with actin during purification studies. The two proteins can be separated from each other by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, and antibodies have been elicited against the 50,000 dalton protein purified by using this technique. These antibodies crossreact with the partially purified protein in urea, but show no detectable cross reaction with actin or myosin. Indirect immunofluorescence reveals that in skeletal muscle this protein is found in close association with the Z lines of the sarcomeres and extends between the Z lines of adjacent myofibrils; it is also associated with filamentous structures that run along the length of a muscle fiber both in close association with the plasma membrane and between myofibrils. These filaments appear to connect myofibrils to each other or to the plasma membrane at the level of their Z lines. In heart muscle, the protein shows the same distribution as in skeletal muscle. In addition, it is found intimately associated with intercalated disks and areas of membrane interaction between laterally associated heart muscle cells. The ). The cytoplasm of both developing and adult smooth muscle cells contains a great number of these filaments which comprise a class distinct from the actin and myosin filaments that are involved in cellular contraction (12, 13). These filaments are known to insert characteristically into desmosome-like structures associated with membrane which are somehow involved in maintaining a strong cell to cell interaction between smooth muscle cells (14). We used smooth muscle as a representative differentiated cell system for the isolation and characterization of the subunit of the 100 A filaments. In this paper, we report its immunological characterization from this type of muscle, and use indirect immunofluorescence to probe its localization in smooth, skeletal, and cardiac muscle cells. MATERIALS AND METHODS Antibody Preparation. Analytical and preparative slab gel electrophoresis with 12.5% gels was performed according to the discontinuous Tris-glycine system of Laemmli (15). The 50,000 molecular weight protein (desmin), for immunization, was purified from the 8 M urea extract of smooth muscle (see legend to Fig. if), by introducing as a final purification step preparative sodium dodecyl sulfate (NaDodSO4)/slab gel electrophoresis (refs. 16 and 17; see Results). After preparative electrophoresis of the 8 M urea extract (Fig. if), the gels were stained for 15 min in 0.25% Coomassie brilliant blue, made up in 50% methanol (vol/vol) and 7.5% acetic acid (...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Immunological characterization of the subunit of the 100 A filaments from muscle cells.

Lazarides¹,

Hubbard²

1976

Proc. Natl. Acad. Sci. U.S.A.

367

189

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“…Numerous investigators have demonstrated free thick filaments that have a marked similarity to synthetic myosin filaments (HUXLEY, 1963) in developing muscle cells (FISCHMAN, 1967;KELLY, 1969;RASH et al, 1970;LEMANSKI, 1973; Longitudinal section of the somitic muscle cells of a 6.5 hr ascidian embryo. Numerous free, short filaments and thinner filamentous structures (seen as amorphous in this micrograph) are aggregated (Ag).…”

Section: Discussionmentioning

confidence: 99%

“…Little evidence for the successive processes of such deposition has been presented in vjvo, however, although the presence of free thick filaments was reported in chick skeletal (FISCHMAN, 1967) and cardiac ( RASH et al, 1970) Free filaments thinner than the thick myosin filaments in developing muscle cells have been assumed to be thin actin filaments (HAY, 1963;ALLEN and PEPE, 1965;PRZYBYLSKI and BLUMBERC, 1966;FISCHMAN, 1967;OBINATA et al, 1967;SHIMADA et al, 1967;MANASEK, 1968), developing thick myosin filaments (HEUSON- STIENNON, 1965;FIRKET, 1967) or a mixture of these (HAY, 1965;TERAKADO, 1968TERAKADO, , 1972.…”

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confidence: 99%

Fine Structure and Size Distribution of Free Thick Filaments in Early Fibrillogenesis of Ascidian Tadpole

Terakado¹

1975

Dev Growth Differ

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The development and the size distribution of free thick filaments which accumulate in the early stages of myofibril formation in somitic myoblasts of the ascidian tadpole were studied by electron microscopy. Such filaments appeared in the cell cortex but, rather dominantly, the aggregates of these thick filaments and filamentous structures were observed in the interior of the cell. The aggregate consisted of some of the following elements: filamentous structures (20-60 A in diameter); free thick filaments (60-220 A); dense Z-band precursor materials; bundles of thick (140-160 A) and thin (60-70 A) filaments; and ribosomal clusters. The free thick filaments were variable in diameter and showed long lateral projections (300 -600 A) and tapered ends.The variation curve in diameter of the free thick filaments indicates a continuous size distribution, suggesting the continuous growth of these filaments by polymerization of myosin molecules. Free thick filaments thicker than myosin filaments which were found within myofibrils were present; their significance is discussed in relation to myosin filament formation.

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Expression of the smooth-muscle proteins α-smooth-muscle actin and calponin, and of the intermediate filament protein desmin are parameters of cardiomyocyte maturation in the prenatal rat heart

Ya¹,

Markman²,

Wagenaar³

et al. 1997

Anat. Rec.

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The results indicate that alpha-SMA, calponin, and desmin are involved in the myofibrillar development in rat heart. The presence of spatiotemporal differences in the expression of these proteins reveals regional differences in the developmental timing of cardiomyocyte maturation. The maturation process extends from the compact myocardium in the IVS to the left and right ventricular free walls, whereas the atrioventricular junction, the ventricular trabeculae, and developing ventricular conduction system show a relatively slow maturation. Smooth-muscle proteins may contribute to the slow shortening speed that is characteristic of the embryonic myocardium.

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Three classes of filaments in cardiac differentiation

Cited by 72 publications

References 87 publications

Immunological characterization of the subunit of the 100 A filaments from muscle cells.

Immunological characterization of the subunit of the 100 A filaments from muscle cells.

Fine Structure and Size Distribution of Free Thick Filaments in Early Fibrillogenesis of Ascidian Tadpole

Expression of the smooth-muscle proteins α-smooth-muscle actin and calponin, and of the intermediate filament protein desmin are parameters of cardiomyocyte maturation in the prenatal rat heart

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