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PubMed1979

A new structural protein located in the Z lines of chicken skeletal muscle.

A new structural protein was purified from a prolonged 0.6 M KI extract of residues of chicken skeletal myofibrils, from which myosin, actin, and some other proteins had been removed. The protein had a chain weight of 55,000. The indirect immunofluorescence technique using antiserum against the 55,000 dalton protein revealed that the protein was exclusively located in the Z lines of a myofibril. The new protein formed lattice structures in vitro which were similar to those observed in the Z lines in situ.

Animals↗

PubMed1979

Myosin from striated adductor muscle of Chlamys nipponensis akazara.

Myosin was isolated from striated adductor muscle of Akazara shell-fish, and purified on DEAE-Sephadex A50. The sedimentation constant (s 20,2 0 W) and the intrinsic viscosity, [eta] of Akazara myosin thus purified were estimated to be 6.6 S and 2.10 dl/g, respectively. In many respects, Akazara myosin was similar to scallop myosin. (1) Only one size of light-chain component (17,000 daltons) was detectable in SDS-gel electrophoresis of Akazara myosin, but two types of light-chain component were seen in urea-gel electrophoresis; these were equivalent to EDTA-light chain and SH-light chain of scallop myosin. The molar ratio of heavy chain (206,000 daltons), EDTA-light chain, and SH-light chain in Akazara myosin was estimated, from the staining densities of gel-electrophoretic bands, to be approximately 1 : 1 : 1. (2) EDTA-washing procedure removed EDTA-light chain only, causing desensitization of Akazara myosin. EDTA-light chain isolated from Akazara myofibrils was able to resensitize EDTA-washed Akazara myosin. Akazara myosin, however, was found to be different from scallop myosin in two important properties: (1) complete removal of EDTA-light chains was required to achieve a complete loss of calcium sensitivity, and full resensitization was attained on recombination of EDTA-light chains with desensitized myosin prepared essentially free from EDTA-light chains. (2) EDTA-light chains isolated from Akazara myofibrils show a calcium-induced UV absorption difference spectrum.

Adenosine Triphosphatases↗

PubMed1981

Eu-actinin, a new structural protein of the Z-line of striated muscles.

A new protein component of the Z-line of striated muscles was isolated from chicken breast muscle. This protein has been designated as eu-actinin because of its close similarity in polypeptide molecular weight to actin. Eu-actinin was extracted from myosin-removed myofibrils at low ionic strength at pH 6.5 and purified by column chromatography on Sepharose 4B and DEAE-cellulose. Although the polypeptide molecular weight of eu-actinin measured by SDS-polyacrylamide gel electrophoresis is similar to that of actin, other physico-chemical properties of eu-actinin definitely differ from those of actin. The isoelectric point of eu-actinin was more acidic than that of actin. The amino acid composition of eu-actinin was found to be different from that of actin or those of other muscle structural proteins. The results of analytical gel filtration on Sepharose 4B indicated that eu-actinin forms dimers through non-covalent bonding under aqueous conditions. Eu-actinin has a low axial asymmetry under low-salt conditions, as judged from its intrinsic viscosity ([eta] = 6.4 ml/g for the dimer state) and exhibits a tendency to undergo self-association with increasing ionic strength. Interactions of eu-actinin with other muscle proteins were examined by the affinity column technique. It was shown that eu-actinin binds to actin and alpha-actinin. Eu-actinin exhibited strong seeding ability for the polymerization of actin. Antibody to eu-actinin was raised in a goat and purified by affinity chromatography. The specific antibody against eu-actinin did not form precipitine lines with actin or alpha-actinin. Immunofluorescence studies revealed that eu-actinin is localized at the Z-line of myofibrils. The FITC-conjugated antibody to eu-actinin also stained the Z-lines of rabbit skeletal muscle and chicken cardiac muscle. Therefore, it was concluded that eu-actinin is a new, ubiquitous constituent of Z-lines of striated muscles.

Actinin↗

PubMed1981

Connectin, an elastic protein of muscle. Effects of proteolytic enzymes in situ.

The effects of various proteolytic enzymes on the high molecular weight protein (connectin) present in a direct sodium dodecyl sulfate extract of myofibrils from chicken breast muscle were studied in detail. To keep the high molecular weight proteins intact, myofibrils had to be prepared in the presence of EGTA. Trypsin, chymotrypsin, papain, and nagarse readily hydrolyzed connectin (doublet band of titin) and the band 3 protein (N2-line protein). Pepsin did not attack connectin, but digested the band 3 protein and myosin. Calcium-activated neutral proteinase hydrolyzed the band 3 protein, leaving connectin intact. On the other hand, serine protease digested connectin but not the band 3 protein.

Animals↗

PubMed1981

A new 220,000 dalton protein located in the Z lines of vertebrate skeletal muscle.

A new protein with a chain weight of approximately 220,000 was isolated from 0.6 M KI extracts of I-Z-I brushes of rabbit and chicken skeletal muscles, using (NH4)2SO4 precipitation and three column chromatographic procedures in succession. It was only possible to separate the high molecular weight protein from actin and alpha-actinin in the presence of 6 M urea or 0.1% sodium dodecyl sulfate (SDS). The purified protein migrated as a single band on SDS gel electrophoresis. The amino acid composition of the 220,000 dalton protein was distinct from any known proteins found in myofibrils, e.g., alpha-actinin and actin binding protein (ABP; filamin). An indirect immunofluorescence technique revealed that the new protein was exclusively located in the Z lines of myofibrils of chicken breast muscle. There is, however, a possibility that the 220,000 dalton protein is identical with synemin recently isolated from chicken gizzard (Granger, B.L. and Lazarides, E. (1980) Cell 22, 727).

Amino Acids↗

PubMed1982

A myofibrillar component that modifies the actin-myosin interaction in postrigor skeletal muscle.

A protein component that modified the interaction between actin and myosin was released from myofibrils on Ca2+-treatment, accompanying the weakening of Z disks. For its release 10(-4) M Ca2+ was required. The presence of the component facilitated the dissociation of thin and thick filaments from myofibrils and delayed superprecipitation of reconstituted actomyosin, independently of Ca2+ concentration. The component is probably a constituent of Z disks. In postmortem muscle, it is possible that the component is released from Z disks with an increased concentration of Ca2+, and that it weakens rigor linkages formed between actin and myosin, giving rise to lengthening of rigor-shortened sarcomeres.

Actins↗

PubMed1983

Preparation of native connectin from chicken breast muscle.

Connectin, an elastic protein of striated muscle, was isolated in a native state from chicken breast muscle. Myofibrils were well washed with 5 mM NaHCO3 and extracted with 0.1 M sodium phosphate buffer, pH 5.6. After washing with water, myofibrils were extracted with 0.1 M phosphate buffer, pH 6.6. The filtrate contained native connectin. The yield of connectin was as high as 200 mg, starting from 50 g of muscle. Since connectin had been isolated only in a denatured state before, the new preparation method enables investigation of possible interactions of connectin with other myofibrillar structural proteins.

Amino Acids↗

PubMed1984

Connectin content and its post-mortem changes in fish muscle.

Connectin was isolated from fish dorsal myofibrils by an SDS-gel filtration method and estimated to account for approximately 13% of the total myofibrillar proteins. There was no significant difference in the amount of connectin among seven fish species but rabbit skeletal myofibrils contained a slightly higher content (16%) of connectin. The high molecular weight connectins from carp and rabbit both showed a doublet band, consisting of bands 1 and 2, on SDS-polyacrylamide gel electrophoresis using a large-pore gel. However, rabbit band 1 (a component of the connectin doublet) was found to migrate more slowly than carp band 1. During post-mortem ageing of the muscles, it was observed that the band 1 component rapidly disappeared with a concomitant increase in band 2 component and then the band 2 component was transformed slowly into faster migrating components. These results suggest that post-mortem ageing has qualitatively similar effects on the submolecular compositions of carp and rabbit connectins. However, the apparent rate of disappearance of the band 1 component was considerably higher in carp muscle than that in rabbit muscle.

Animals↗

PubMed1990

Morphological and biochemical examination of Cosmos 1887 rat heart tissue: Part I--Ultrastructure.

Morphological changes were observed in the left ventricle of rat heart tissue from animals flown on the Cosmos 1887 biosatellite for 12.5 days. These tissues were compared to the synchronous and vivarium control hearts. While many normal myofibrils were observed, others exhibited ultrastructural alterations, i.e., damaged and irregular-shaped mitochondria and generalized myofibrillar edema. Analysis of variance (ANOVA) of the volume density data revealed a statistically significant increase in glycogen and a significant decrease in mitochondria compared to the synchronous and vivarium controls. Point counting indicated an increase in lipid and myeloid bodies and a decrease in microtubules, but these changes were not statistically significant. In addition, the flight animals exhibited some patchy loss of protofibrils (actin and myosin filaments) and some abnormal supercontracted myofibrils that were not seen in the controls. This study was undertaken to gain insight into the mechanistic aspects of cardiac changes in both animals and human beings as a consequence of space travel (1). Cardiac hypotrophy and fluid shifts have been observed after actual or simulated weightlessness and raise concerns about the functioning of the heart and circulatory system during and after travel in space (2-4).

Actins↗

PubMed2004

A novel mechanism of regulation of cardiac contractility by mitochondrial functional state.

It is generally considered that mitochondria regulate cardiac cell contractility by providing ATP for cellular ATPases and by participating in Ca2+ homeostasis. However, other possible mechanisms by which mitochondria can influence contractility have been largely overlooked. Here, we demonstrate that inhibition of the mitochondrial electron transport chain strongly increases Ca2+-dependent and independent isometric force development in rat ventricular fibers with selectively permeabilized sarcolemma. This effect is unrelated to the ATP-generating activity of mitochondria or Ca2+ homeostasis. Furthermore, various conditions that increase K+ accumulation in the mitochondrial matrix (activation of ATP- or Ca2+-dependent K+ channels as well as inhibition of the K+ efflux pathway via the K+/H+ exchanger) induce a similar mechanical response. Modulators of mitochondrial function that augment isometric force also cause swelling of mitochondria in the vicinity of myofibrils in situ, as shown by confocal microscopy. Osmotic compression of intracellular structures abolishes the effect of mitochondria-induced force modulation, suggesting a mechanical basis for the interaction between the organelles. These findings suggest a novel mechanism for cellular regulation of myofibrillar function, whereby increases in mitochondrial volume can impose mechanical constraints inside the cell, leading to an increase in force developed by myofibrils.

Adenosine Triphosphate↗

PubMed1997

Myofibrillar myopathy. III. Abnormal expression of cyclin-dependent kinases and nuclear proteins.

The pathological process in myofibrillar myopathy (MFM) (previously also referred to as "desmin storage" or "intermediate filament myopathy") results in dissolution of myofibrils, accumulation of products of the degradative process, and abnormal ectopic expression of desmin, dystrophin, gelsolin, NCAM, and N-terminal components of beta-amyloid precursor protein. We now demonstrate that the abnormal fiber regions in MFM immunoreact strongly for (a) CDC2 kinase, the mitotic kinase that phosphorylates and disassembles intermediate filaments; (b) cyclin-dependent kinases CDK2, CDK4, and CDK7, which are involved in regulation of the cell cycle; (c) lamin B, which normally supports the inner nuclear membrane; and (d) the nuclear matrix associated protein. The normal muscle fiber lies in a terminally differentiated state and is refractory to reentry into the cell cycle. The abnormal expression of multiple cyclin-dependent kinases in the terminally differentiated muscle fiber implies inappropriate activation of positive regulators of mitosis and may signal a mitotic catastrophe. The dissolution of myofibrils may be due to hyperphosphorylation occurring during this event.

Adult↗

PubMedDate not supplied

Fine structure of muscle in human disuse atrophy: significance of proximal muscle involvement in muscle disorders.

The universal occurrence of weakness of skeletal musculature on disuse, however produced, and the paucity of published reports on the fine structural changes in human disuse atrophy, prompted the present investigation. The quadriceps muscle of a leg immobilized in plaster cast (for fracture) and of the opposite non-immobilized limb was biopsied in four adult males, after periods of immobilization from 50 to 75 days. These 8 muscle specimens were examined for histopathological changes, and muscle fibre diameters were measured by micrometry from paraffin sections. The histograms revealed a larger proportion of small fibres (less than 20 micron) and a smaller proportion of large fibres (greater than 40 micron) in the immobilized limb compared to the opposite. Thus, light microscopy showed only atrophic changes. This was confirmed by electronmicroscopy, where atrophy of few to several muscle fibres was seen in the form of loss of myofibrils, collapse and folding of the basement membrane and prominence of glycogen or muscle nuclei. The atrophic change was more severe in the immobilized limbs, but it was also noticeable in all the non-immobilized limbs. Degenerative changes, especially disorganization and breakdown of myofibrils, and fragmentation of plasma membrane, were also seen in occasional atrophied muscle fibres, again more frequently in the immobilized limb. Lipofuscin was often found accumulated in muscle fibres and occasionally in endothelial cells of intramuscular blood vessels; the latter showed prominent pinocytotic vesicles or thickened basement membrane. It is concluded that both atrophy and degeneration of fibres of proximal muscles can occur as non-specific consequences of disuse of the limb in man, that degeneration is a latter and more severe change, that muscles even of the non-immobilized leg are subjected to disuse atrophy during bed-rest, and that the proximal muscles in man seem to have a natural susceptibility to atrophy and degeneration in any muscular disorders.

Adult↗

PubMed1983

A new myofibrillar protein characteristic of type I human skeletal muscle fibres.

Analysis of a single human type I (slow-twitch) skeletal muscle fibres by two-dimensional gel electrophoresis shows that they contain a specific protein of subunit Mr 34 x 10(3) and pI 6.0, 6.1 and 6.2 (three spots) which is absent from type IIA and IIB muscle fibres. This type I protein is located in the I-band of isolated myofibrils as demonstrated by the indirect immunofluorescence using specific antisera against the denatured form of type I protein. Type I protein could only be extracted from myofibrils with high salt solutions (0.6-1 M KCl), conditions which also coextract actin and myosin, demonstrating its firm attachment. Rat and cat type I muscle fibres as well as the slow-tonic fibres from chicken anterior latissimus dorsi also contained a protein homologous to the human type I protein. The human type I protein was found to be different from the known regulatory and contractile muscle proteins by electrophoretic and immunological criteria, and may therefore be a new myofibrillar protein in type I muscle fibres.

Animals↗

PubMed1984

Assay of ATP synthesis using single giant mitochondria.

Two assays of the capacity of single giant mitochondria or mitoplasts to phosphorylate ATP from Pi and ADP have been developed. One depends on the placement of a single mitochondrion next to a glycerinated myofibril, by micromanipulation. With the appropriate controls, contraction of the myofibril serves as an indication of ATP synthesis. The other assay similarly requires the isolation of one single mitochondrion but the assay of ATP synthesized uses the luciferin-luciferase reaction with a conventional photometric system. With the latter, we found that either impalement with microelectrodes or electrophoretic microinjection of two dyes, Lucifer Yellow CH or pyranine , into the inner space have no effect on the phosphorylative capacity of mitochondria or mitoplasts. The electric potential across the mitochondrial membrane was monitored during the assay and found to be small and generally positive inside.

Adenosine Triphosphate↗

PubMed1997

Identification of the regions on the M110 subunit of protein phosphatase 1M that interact with the M21 subunit and with myosin.

We have previously isolated a form of protein phosphatase-1 (PP1M) from avian smooth muscle myofibrils that is composed of the catalytic subunit of PP1 (PP1C) bound to an M-complex consisting of 110-kDa (M110) and 21-kDa (M21) subunits. The interaction of PP1C with an N-terminal region of the M110 subunit enhances the dephosphorylation of myosin and suppresses the dephosphorylation of other substrates [Alessi, D. R., MacDougall, L. K., Sola, M. M., Ikebe, M. & Cohen, P. (1992) Eur. J. Biochem. 210, 1023-1035; Chen, Y. H., Chen, M. X., Alessi, D. R., Campbell, D. G., Shanahan, C., Cohen, P. & Cohen, P. T. W. (1994) FEBS Lett. 356, 51-56; Johnson, D. F., Moorhead, G., Caudwell, F. B., Cohen, P., Chen, Y. H., Chen, M. X. & Cohen, P. T. W. (1996) Eur. J. Biochem. 239, 317-325]. In this paper, we establish that PP1M accounts for nearly all the myosin phosphatase activity in myofibrils, that the M110 and M21 subunits are present at similar concentrations in the myofibrillar fraction, and that these subunits are entirely bound to PP1. We demonstrate that the M21 subunit does not interact with PP1C, but with the C-terminal 72 residues of the M110 subunit, a region which is 43% identical to residues 87-161 of the M21 subunit. A fragment of the M21 subunit, M21-(M1-L146), which lacks the C-terminal leucine zipper, also bound to the M110 subunit, but two other fragments M21-(M1-E110) and M21-(E110-K186) did not. The M110 and M21 subunits were both found to be myosin-binding proteins. The C-terminal 291 residues of the M110 subunit, but not the C-terminal 72 residues, bound to myosin, but the N-terminal fragments M110-(M1-E309) and M110-(M1-S477) did not. Thus, the region of the M110 subunit that stimulates the dephosphorylation of myosin by PP1C is distinct from the region that targets PP1M to myosin. Remarkably, each myosin dimer was capable of binding about 20 mol M21 subunit and many of the M21-binding sites were located in the myosin rod domain. The potential significance of this observation is discussed.

Amino Acid Sequence↗

PubMed1969

Enzymic properties of myosin in fast and slow twitch muscles of the cat following cross-innervation.

1. Following cross-innervation of the cat flexor digitorum longus muscle (F.D.L., fast-twitch) and soleus muscle (slow-twitch) the isometric twitch speed of the F.D.L. muscle decreases while the contraction time of soleus increases. The tetanus-twitch ratio of soleus is also increased.2. Myosin or myofibrils from normal or self-reinnervated fast-twitch muscles of the cat split adenosine triphosphate (ATP) more rapidly than myosin or myofibrils from slow twitch muscles.3. Following cross-innervation the myosin and myofibrillar ATPase activity of flexor digitorum longus muscle falls, to become nearly equal to that of normal or self-reinnervated soleus muscle. The ATPase activity of cross-innervated soleus muscle increases only slightly.

Adenosine Triphosphatases↗

PubMed1990

Ca2+ release from the sarcoplasmic reticulum of barnacle myofibrillar bundles initiated by photolysis of caged Ca2+.

1. Ca2(+)-induced Ca2+ release (CICR) from the sarcoplasmic reticulum was measured by isometric tension recording from barnacle myofibrillar bundles. Laser-induced photolysis of the caged calcium molecule, nitr-5, was used to generate a rapid jump in free Ca2+ (within 1 ms) at the site of the sarcoplasmic reticulum, thus overcoming delays due to Ca2+ diffusion from the bathing solution. 2. The method consisted of equilibrating a myofibrillar bundle (100 micrograms diameter) in a solution containing 0.1 mM-nitr-5 (initial pCa 6.8-6.6) and then exposing it to a UV laser pulse. The resulting phasic contraction had an amplitude of up to 100% maximum tension (P0) in some preparations and a mean half-time for the rise of tension of 2.3 s at 12 degrees C. Longer half-times were obtained at low pulse energies. 3. Pre-treatment of the myofibrillar bundles with ryanodine (10(-4) M) or the detergent Triton X-100 abolished a large part of the phasic contraction, confirming its dependence on SR Ca2+ release. The small tonic response which remained had a shorter rise half-time than the Ca2(+)-induced Ca2+ release response and was attributed to direct activation of the myofibrils by Ca2+ released from the nitr-5. 4. The size of the photolytic Ca2+ jump was estimated from the amplitude of the fast tension component. By increasing the laser pulse energy or the initial Ca2+ loading of the nitr-5, the post-photolysis pCa was varied from 6.7 to 6.0; the CICR response increased in size over this pCa range. 5. Direct activation of Triton-treated myofibrils by photolysis of 2.0 mM-nitr-5 (initial pCa 6.4) gave contractions of up to 100% P0 and a mean rise half-time of 164 ms at 12 degrees C (n = 9 for contractions greater than 40% P0). Both the amplitude and the rate of these contractions were dependent on the laser pulse energy. 6. The Ca2(+)-induced Ca2+ release responses obtained with nitr-5 photolysis were significantly slower than the fastest rate of tetanus development which has been recorded from intact fibres of barnacle muscle (mean half-time = 177 ms at 12 degrees C). This could mean that either Ca2(+)-induced Ca2+ release is less efficient in isolated myofibrillar bundles than in intact fibres or that Ca2(+)-induced Ca2+ release is not the primary Ca2+ releasing mechanism in excitation-contraction coupling in barnacle muscle.

Animals↗

PubMed1967

Transverse tubule apertures in mammalian myocardial cells: surface array.

The technique of " freezeetching" tissues for electron microscopy has permitted observation of the external apertures of the transverse tubules. The apertures appear on the cell surface in approximately parallel rows, which can be interpreted as corresponding longitudinally to the spaces between the myofibrils and transversely to the Z regions of the myofibrils.

Animals↗