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PubMed1994

Cytoskeletal alterations in cultured cardiomyocytes following exposure to the lipid peroxidation product, 4-hydroxynonenal.

Damage to the cardiac myocyte sarcolemma following any of several pathological insults such as ischemia (anoxia) alone or followed by reperfusion (reoxygenation), is most apparent as progressive sarcolemmal blebbing, an event attributed by many investigators to a disruption in the underlying cytoskeletal scaffolding. Scanning electron microscopic observation of tissue cultured rat neonatal cardiomyocytes indicates that exposure of these cells to the toxic aldehyde 4-hydroxynonenal (4-HNE), a free radical-induced, lipid peroxidation product, results in the appearance of sarcolemmal blebs, whose ultimate rupture leads to cell death. Indirect immunofluorescent localization of a number of cytoskeletal components following exposure to 4-HNE reveals damage to several, but not all, key cytoskeletal elements, most notably microtubules, vinculin-containing costameres, and intermediate filaments. The exact mechanism underlying the selective disruption of these proteins cannot be ascertained at this time. Colocalization of actin indicated that whereas elements of the cytoskeleton were disrupted by increasing length of exposure to 4-HNE, neither the striated appearance of the myofibrils nor the lateral register of neighboring myofibrils was altered. Monitoring systolic and diastolic levels of intracellular calcium ([Ca2+]i) indicated that increases in [Ca2+]i occurred after considerable cytoskeletal changes had already taken place, suggesting that damage to the cytoskeleton, at least in early phases of exposure to 4-HNE, does not involve Ca(2+)-dependent proteases. However, 4-HNE-induced cytoskeletal alterations coincide with the appearance of, and therefore suggest linkage to, sarcolemmal blebs in cardiac myocytes. Although free radicals produced by reperfusion or reoxygenation of ischemic tissue have been implicated in cellular damage, these studies represent the first evidence linking cardiomyocyte sarcolemmal damage to cytoskeletal disruption produced by a free radical product.

Aldehydes↗
PubMed1995

Exogenous gelsolin binds to sarcomeric thin filaments without severing.

We have investigated the binding of gelsolin to thin myofilaments in situ and their stability against severing. Differentiated myotubes from chicken skeletal muscle containing cross-striated myofibrils were permeabilized with Triton X-100 and incubated with gelsolin. Immunofluorescence microscopy localized both endogenous and exogenous gelsolin in the I-Z-I-regions of the sarcomers. The staining pattern suggested a binding of the exogenous gelsolin along the entire length of the thin filaments. This binding was Ca2+ dependent, but gelsolin was not removed after subsequent addition of EGTA. The fluorescence staining for actin remained unchanged after gelsolin incubation, indicating that thin filaments in cross-striated myofibrils were resistant to the severing action of gelsolin, in contrast to the microfilaments in stress fibers. After extraction of the permeabilized cells with high ionic strength to remove tropomyosin and myosin, gelsolin still bound along the entire thin filament and the actin pattern also remained unchanged. After Triton X-100 permeabilization and high ionic strength extraction, the giant protein nebulin was found to be still present as a myofibrillar component. Gelsolin treatment after high salt extraction affected neither actin nor nebulin in the thin filaments. We therefore conclude that nebulin confers the gelsolin resistance to the sarcomeric actin filaments.

Actin Cytoskeleton↗
PubMed2005

N-RAP expression during mouse heart development.

N-RAP gene expression and N-RAP localization were studied during mouse heart development using semiquantitative reverse transcriptase-polymerase chain reaction and immunofluorescence. N-RAP mRNA was detected at embryonic day (E) 10.5, significantly increased from E10.5 to E16.5, and remained essentially constant from E16.5 until 21 days after birth. In E9.5-10.5 heart tissue, N-RAP protein was primarily associated with developing premyofibril structures containing alpha-actinin, as well as with the Z-lines and M-lines of more-mature myofibrils. In contrast, N-cadherin was concentrated in patches at the periphery of the cardiomyocytes. N-RAP labeling markedly increased between E10.5 and E16.5; almost all of the up-regulated N-RAP was associated with intercalated disk structures, and the proportion of mature sarcomeres containing N-RAP decreased. In adult hearts, specific N-RAP staining was only observed at the intercalated disks and was not found in the sarcomeres. The results are consistent with N-RAP functioning as a catalytic scaffolding molecule, with low levels of the scaffold being sufficient to repetitively catalyze key steps in myofibril assembly.

Actinin↗
PubMed2007

Rho kinase inhibitor Y27632 affects initial heart myofibrillogenesis in cultured chick blastoderm.

During early vertebrate development, Rho-associated kinases (ROCKs) are involved in various developmental processes. Here, we investigated spatiotemporal expression patterns of ROCK1 protein and examined the role of ROCK during initial heart myofibrillogenesis in cultured chick blastoderm. Immunohistochemistry showed that ROCK1 protein was distributed in migrating mesendoderm cells, visceral mesoderm of the pericardial coelom (from which cardiomyocytes will later develop), and cardiomyocytes of the primitive heart tube. Pharmacological inhibition of ROCK by Y27632 did not alter the myocardial specification process in cultured posterior blastoderm. However, Y27632 disturbed the formation of striated heart myofibrils in cultured posterior blastoderm. Furthermore, Y27632 affected the formation of costamere, a vinculin/integrin-based rib-like cell adhesion site. In such cardiomyocytes, cell-cell adhesion was disrupted and N-cadherin was distributed in the perinuclear region. Pharmacological inactivation of myosin light chain kinase, a downstream of ROCK, by ML-9 perturbed the formation of striated myofibrils as well as costameres, but not cell-cell adhesion. These results suggest that ROCK plays a role in the formation of initial heart myofibrillogenesis by means of actin-myosin assembly, and focal adhesion/costamere and cell-cell adhesion.

Amides↗
PubMed1993

Kettin, a large modular protein in the Z-disc of insect muscles.

Z-discs of insect flight muscle contain a large protein of 500-700 kDa. Monoclonal antibodies label an epitope in the molecule at the Z-disc in Drosophila and Lethocerus (waterbug). A partial cDNA of 1.6 kb from the Drosophila gene has been cloned and sequenced. The corresponding amino acid sequence has a modular structure composed of four conserved repeats of 95 amino acids homologous to immunoglobulin C2 domains (called class II domains in muscle proteins), separated by less conserved linker sequences of 35 amino acids. An expressed class II domain with flanking linker sequences binds to actin and alpha-actinin but not to myosin. Single molecules of the protein would be large enough to span the Z-disc. We suggest that the protein acts as scaffolding in the Z-disc and we call the protein kettin. The Ca2+ activated protease, calpain, disrupts the Z-disc of striated muscle, releasing alpha-actinin intact. Calpain digests kettin to a series of peptides of between 30 and 170 kDa which are released from the myofibril. Digestion of kettin may cause disintegration of the Z-disc and alpha-actinin release which lead to disassembly of the myofibril.

Amino Acid Sequence↗
PubMed2002

Role of N-cadherin- and integrin-based costameres in the development of rat cardiomyocytes.

Costameres, vinculin-containing structures found in skeletal and cardiac muscle, are thought to anchor the Z-discs of the peripheral myofibrils to the sarcolemma. Several lines of evidence indicate that two different sets of costameres, integrin- and N-cadherin-based, are present in cardiac muscles. In this study, immunoblot analysis was used to study the expression of N-cadherin, alpha-catenin, beta-catenin, vinculin, talin, and laminin in rat cardiac muscles at embryonic days 15 and 19, the day of birth (postnatal day 0), postnatal weeks 1, 2, 3, and 4, and in the adult. Double immunofluorescence microscopy was performed to study the spatial and temporal distribution of these two sets of costameres in rat cardiomyocytes. Costameric staining for N-cadherin, codistributed with beta-catenin, was strong from embryonic day 15 up to postnatal week 2, gradually decreased after postnatal week 3, and was undetectable at postnatal week 4 and in the adult. Confocal microscopy showed that N-cadherin colocalized with alpha-actinin at cortical myofibrils. Double-labeling of beta-catenin and talin indicated the coexistence of N-cadherin/catenin- and integrin/talin-based costameres in rat cardiac muscle. Although beta-catenin and vinculin were co-localized at the costamere of cardiomyocytes from embryonic day 15 to postnatal week 3, staining for beta-catenin or talin was mutually exclusive at all stages examined. These results demonstrate the simultaneous, but mutually exclusive, existence of N-cadherin/catenin- and integrin/talin-based costameres in rat cardiomyocytes between late embryonic stages and postnatal week 3, while only integrin/talin-based costameres were found in adult rats. The N-cadherin/catenin-based costameres in rat cardiac muscles may play a role in myofibrillogenesis similar to that of their counterparts in cultured cardiomyocytes.

Animals↗
PubMed1994

Myoepithelium of salivary glands.

In salivary glands and other exocrine organs, there are starfish-shaped cells that lie between the basal lamina and the acinar and ductal cells. These have structural features of both epithelium and smooth muscle cells, and so are called myoepithelial cells. Their functions include contraction when the gland is stimulated to secrete, compressing or reinforcing the underlying parenchymal cells, thus aiding in the expulsion of saliva and preventing damage to the other cells. They also may aid in the propagation of secretory and other stimuli. Their common developmental origin with the basal cells of the larger ducts is displayed in the mature glands by shared structural and immunohistochemical features, but most such basal cells do not have the distinguishing features of myoepithelial cells, such as myofibrils. Although myoepithelial cells can be identified by light microscopy through enzyme histochemistry and special stains and immunohistochemistry for their myofibrils, these techniques can be misleading in salivary gland neoplasms. Thus, the most reliable means of identifying neoplastic myoepithelial cells is with a combination of histochemistry and electron microscopy. The extent to which these cells are derived from undifferentiated stem cells in both normal and neoplastic growth is controversial. The presentation here of transmission electron microscopy (TEM) of well-differentiated myoepithelial cells in mitotic division indicates that stem cells are not necessarily the only source of myoepithelial cells in the later stages of salivary gland development or in neoplasia.

Animals↗
PubMedDate not supplied

Actomyosin ATPase. I. Quantitative measurement of activity in cryostat sections.

A method for the quantitative study of the actomyosin ATPase activity (Ca,MG-ATPase) in thin sections cut in a cryostat is presented. This method is based on the liberation of 32P from [gamma 32P]ATP or 45Ca phosphate precipitation. The advantage of this method lies in the requirement for only a small muscle sample and the availability of serially cut sections for other assays including Ca uptake by sarcoplasmic retciulum and histochemical tests for oxidative and glycolytic enzymes. The actomyosin ATPase activity for various types of muscles determined by this method showed the same sequence found in isolated protein, that is, fast-twitch skeletal greater than slow-twitch skeletal greater than cardiac. The Ca,Mg-ATPase of cryostat sections showed Ca sensitivity. The fact that the sections retained Ca sensitivity at 37 degrees C, in contrast to myofibrils, which have been reported to lose Ca sensitivity at this temperature, indicates that the structural integrity of the contractile and regulatory apparatus is preserved to a higher degree in sections than in isolated myofibrils.

Actomyosin↗
PubMed1993

Developmental toxicity of caffeine in the larvae of Xenopus laevis.

To examine the developmental toxicity of caffeine, Xenopus larvae just after hatching, were continuously exposed to 100-2,000 mg/L caffeine for 48 hours. Caffeine interfered with development of Xenopus larvae at a concentration of 100 mg/L and above in a concentration-dependent manner. Characteristic external abnormalities, such as shortened body with wavy fins, were observed, the severity of which was clearly concentration dependent. These larvae were frequently accompanied by abnormal body flexure and edema in the fin. Light microscopy revealed that exposure to caffeine induced severe damage in the myotome and neural tube, and at higher concentrations, the epidermal tissue was also affected. Myoblasts showed wide intercellular spaces, and their cytoplasm lost uniform staining. Ultrastructural studies of myoblasts revealed distinct myofibril disorganization and degeneration, and mitochondrial alterations. In the neural tube, cells at the dorsal part of tube showed wide intercellular spaces and some of them were segregated to the peripheral region. Furthermore, vacuole-like structures of various sizes appeared in the white matter. The outer layer of epithelial cells in the epidermis were vacuolated and swollen. With regard to the pathogenesis of myofibril damage, caffeine appeared to cause a disturbance of intracellular calcium regulation, by releasing calcium ions from the sarcoplasmic reticulum, and the mitochondrial changes observed in myotomal cells were considered to be reflective of this increased intracellular calcium ion levels. It is speculated that caffeine interferes with cell adhesion in the myotome and neural tube by affecting calcium ion regulation.

Abnormalities, Drug-Induced↗
PubMed1993

Phosphorylation of cardiac myosin light chain 2 by protein kinase C and myosin light chain kinase increases Ca(2+)-stimulated actomyosin MgATPase activity.

Myosin light chain 2 (MLC2) phosphorylation in rat cardiac whole myosin by cardiac myosin light chain kinase (MLCK) or by protein kinase C (PKC) resulted in increased actin-stimulated myosin MgATPase activity. The phosphorylation also increased Ca(2+)-stimulated myofibrillar MgATPase activity upon substitution of the phosphorylated myosin into myofibrils. In addition, phosphorylation of MLC2 in myofibrils by MLCK increased both the Ca(2+)-sensitivity and maximum activity of the myofibrillar Ca(2+)-stimulated MgATPase activity. The latter effect was inhibited by PKC-phosphorylation of troponin I, troponin T and C-protein. A role for both PKC and MLCK in regulating cardiac myofibrillar activity, via phosphorylation of various contractile proteins, is indicated.

Animals↗
PubMed1994

N-cadherin involvement in cardiac myocyte interaction and myofibrillogenesis.

N-cadherin is a cell-surface, Ca(2+)-dependent adhesion molecule found in intercalated disks and extrajunctional sites in the myocardium. In this paper we show that antibodies specific for N-cadherin inhibit the contraction of both interacting and single myocytes isolated from embryonic chicken hearts. Quantitative electron microscopy revealed that anti-N-cadherin significantly decreases cell-cell contact between interacting myocytes, consistent with a role for N-cadherin as a cell-cell adhesion molecule. In addition, quantitative electron microscopy showed that anti-N-cadherin treatment of cardiomyocytes results in a significant reduction in the cytoplasmic area occupied by myofibrils, implying that N-cadherin also plays a role in myofibrillogenesis. We propose that N-cadherin, in addition to mediating cardiac myocyte interaction, promotes myofibril formation necessary for functional activity of the myocardium.

Animals↗
PubMed1993

Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes.

We used immunofluorescence methods to examine the cellular distribution of cofilin in chicken myotubes in primary culture. Cofilin showed mainly diffuse distribution in the cytoplasm except for rather strong staining around the nuclei and faint striated patterns along myofibrils, but did not stain inside the nuclei. Neither stress fiber-like structures nor myofibrils were clearly stained. In the presence of 10% dimethyl sulfoxide (DMSO), intranuclear actin-cofilin rods, which were composed of alpha-actin isoform and cofilin, were formed in all the nuclei of individual myotubes. In the cofilin sequence, a putative nuclear localization signal (NLS) was observed. We examined the NLS activity of this portion by using a synthetic peptide corresponding to the putative NLS. When the NLS peptide conjugated with bovine serum albumin was microinjected into the cytoplasm of myotubes, it was rapidly accumulated into the nuclei. The same result was obtained with in vitro a nuclear protein import assay system with digitonin-permeabilized myotubes. Therefore, we suggest that this portion is responsible for the nuclear transport of cofilin. In myotubes, the majority of cofilin was present in an unphosphorylated form and this form remained unchanged after the DMSO treatment. Thus, we suggest that the phosphorylation of cofilin itself is not directly involved in its nuclear transport at least in myotubes.

Actin Depolymerizing Factors↗
PubMed1999

Nestin is expressed during development and in myotendinous and neuromuscular junctions in wild type and desmin knock-out mice.

Desmin, the main component of intermediate filaments (IFs) in mature skeletal muscle, forms an interlinking scaffold around myofibrils with connections to the sarcolemma and the nuclear membrane. Desmin is enriched in neuromuscular and myotendinous junctions. Mice lacking the desmin gene develop normally and reproduce. However, postnatally they develop a cardiomyopathy and a dystrophy in highly used muscles. We have investigated whether and how neuromuscular and myotendinous junctions are affected and whether nestin compensates for the lack of desmin in the knock-out (K/O) mice. We show that neither neuromuscular nor myotendinous junctions were markedly affected in the desmin K/O mice. In neuromuscular junctions nestin was present between the postjunctional folds and the subneural nuclei and between the nucleus and the myofibrillar cytoskeleton. In myotendinous junctions nestin was present between myofibrils at the Z-disc level and in longitudinal strands close to and at the junction. Nestin expression at these specialized sites, as well as during myogenesis and myofibrillogenesis, is independent of the presence of desmin. In desmin K/O mice nestin was also found in regenerating myofibers. The presence of nestin at neuromuscular and myotendinous junctions might provide enough strength for preservation and organization of the junctional areas, although desmin is lacking.

Aging↗
PubMed1999

Association of mitochondria with plectin and desmin intermediate filaments in striated muscle.

Plectin (M(r) > 500,000) is a versatile and widely expressed cytolinker protein. In striated muscle it is predominantly found at the Z-disc level where it colocalizes with the intermediate filament protein desmin. Both proteins show altered labeling patterns in tissues of muscular dystrophy patients. Moreover, mutations in the plectin gene lead to the autosomal recessive human disorder epidermolysis bullosa simplex with muscular dystrophy, and defects in the desmin gene have been shown to cause familiar cardiac and skeletal myopathy. Since intermediate filaments (IFs) in striated muscle tissue have been found to be intimately associated with mitochondria, we investigated whether plectin is involved in this association. Using postembedding immunogold labeling of Lowicryl sections and immunogold labeling of ultrathin cryosections, we show that plectin is associated with desmin IFs linking myofibrils to mitochondria at the level of the Z-disc and along the entire length of the sarcomere. The localization of plectin label at the mitochondrial membrane itself was consistent with a putative linker function of plectin between desmin IFs and the mitochondrial surface. In mitochondrion-rich muscle fibers, both plectin and desmin were part of an ordered arrangement of mitochondrial side branches, which wound around myofibrils adjacent to the Z-discs and were anchored into a filamentous network transversing from one fibril to the other. The association of mitochondria with plectin and IFs was seen also in tissues without regular distribution patterns of mitochondria, such as heart muscle and neonatal skeletal muscle tissues. These data were supplemented with in vitro binding assays showing direct interaction of plectin with desmin via its carboxy-terminal IF-binding domain. As a cytolinker protein associated with mitochondria and desmin IFs, plectin could play an important role in the positioning and shape formation, in particular branching, of mitochondrial organelles in striated muscle tissues.

Animals↗
PubMed1994

Fetal alcohol effects on the postnatal development of the rat myocardium: an ultrastructural and morphometric analysis.

Heart disease is an entity frequently seen in the fetal alcohol syndrome. This paper describes the effect of in utero ethanol exposure on the postnatal ultrastructural development of rat cardiac muscle. To determine this time-pregnant Sprague-Dawley rats were fed either a nutritionally balanced protein- and vitamin-enriched liquid ethanol diet (with 36% of the calories derived from ethanol) or a liquid diet with maltose-dextrins isocalorically substituted for ethanol. The latter group was designated the pairfed control group. At birth, pups of both the groups were surrogate-fostered by normal dams. Body weights and crown-rump lengths were significantly less in the rat pups exposed to ethanol in utero at 21 days postnatal. Ultrastructural analysis of the cardiac muscle was performed at 7, 14, and 21 days postnatal in ethanol and pairfed groups. Several morphological features of myocyte damage were observed in ethanol-exposed pups, predominantly at 7 days postnatal, with nearly total absence of myocyte damage by 21 days postnatal. The most outstanding changes were observed in the myofibrils, which showed dysplastic changes at 7 days postnatal, a delay in M-band structural development at 14 days postnatal, and a significantly smaller myofibril volume density per tissue volume at 21 days postnatal in the ethanol rat pups compared to the pairfed controls.

Animals↗
PubMed1993

Stunning does not change the relation between calcium and force in skinned rat trabeculae.

To test the hypothesis that stunning is due to a decreased sensitivity of the myofibrils for calcium, we compared the isometric force-Ca2+ relation in skinned trabeculae from stunned and control hearts. Hearts were made ischemic for 40 min followed by 30 min reperfusion. In one group (Group 1) changes in left ventricular systolic and diastolic pressure were monitored. From another group (Group 2), trabeculae were isolated to determine the relation between force and Ca2+ concentration. Trabeculae isolated from hearts (Group 3) perfused aerobically for 90 min served as controls. Left ventricular developed pressure and end diastolic pressure were 5.9 +/- 0.7 kPa and 5.8 +/- 0.7 kPa, respectively in stunned hearts as compared to 9.9 +/- 1.2 kPa and 1.2 +/- 0.1 kPa prior to ischemia. The nucleotide content decreased from 24.9 +/- 3.4 mumol.g-1(dw) in control hearts to 9.3 +/- 0.8 mumol.g-1(dw) after ischemia and reperfusion while the creatine kinase levels were about the same. Force-Ca2+ relations obtained from trabeculae from control and stunned hearts were fitted to the Hill equation. Maximal isometric force, the midpoint and the steepness of the curves estimated for the two groups were not significantly different. We conclude that the maximum isometric force and the sensitivity of the contractile apparatus of skinned myocardium of stunned hearts do not differ from that of control hearts. This suggests that structural changes of the contractile proteins leading to a decreased sensitivity of the myofibrils to calcium are not involved in the mechanism responsible for stunning.

Animals↗
PubMed1994

Cardiac troponin I and tension generation of skinned fibres in the developing rat heart.

During development of the myocardium the troponin I (TNI) isoform expression is switched from a cAMP-insensitive, slow skeletal muscle TNI to a cAMP-sensitive, cardiac TNI isoform (cTNI). To study the functional consequence of alterations in cTNI expression in the rat heart we investigated the cAMP-controlled cTNI phosphorylation in comparison with alterations of functional properties of isolated cardiac myofibrils during the first postnatal month. cTNI was identified by Western blot analysis followed by a semiquantitative assessment. From the third to the 28th postnatal day the relative concentrations of the cardiac isoform of TNI increased 2.9 +/- 0.3-fold. In the same period the amount of phosphate incorporated into cTNI in the presence of exogenous cAMP-dependent protein kinase (PKA) and 32P[gamma]-ATP was increased 5.8 +/- 0.2-fold (24.2 +/- 3.5 v 140.2 +/- 7.6 pmolP/mg protein loaded onto the gel) whereas the phosphorylation of C-protein was only increased 1.6 +/- 0.2-fold. Ca(2+)-activated isometric tension generation of skinned heart fibres measured in the range of pCa from 6 to 4.5 was not affected by PKA at day 3. However, isometric tension generation of fibres prepared from 28-day-old rats was suppressed by incubation with PKA which was accompanied by a rightward shift in the force/pCa relation. Under these conditions half-maximal tension development was found at pCa 5.38 v 5.52 (p < 0.05) in the absence of PKA. The Ca2+ sensitivity of the contractile apparatus was not affected by PKA-induced phosphorylation of C-protein. These data give direct evidence for the physiological relevance of the onset of cAMP-induced phosphorylation of cTNI for the Ca(2+)-activated tension generation in cardiac myofibrils during postnatal development.

Animals↗
PubMed1997

Null mutation in the desmin gene gives rise to a cardiomyopathy.

A null mutation in the desmin gene has been introduced into the germ line of mice. Such mice develop and reproduce normally proving that desmin is not needed either for the formation of the heart or the alignment of functioning myofibrils. However, cardiovascular lesions and a skeletal myopathy were observed in growing and adult mice. In the present study we have carried out a detailed analysis of these cardiac lesions. Homozygous mutant mice, which were confirmed to lack expression of desmin mRNA and desmin protein in the heart, were revealed by electron microscopy to contain degenerating cardiomyocytes as early as 5 days post-partum. At 10 days post-partum and onwards the degeneration of cardiomyocytes gave rise to areas with an accumulation of macrophages, fibrosis and calcification preferentially in the inter-ventricular septum and the free wall of the right ventricle. The localization of the lesions mainly to these sites suggested that it is not the work load and contractions per se which were the pathogenic events leading to the cardiomyopathy. It might be that stress related to lengthening of the myocytes occur more in the right ventricle than in the left. At the ultrastructural level changes in the intercalated discs, disruption of the sarcolemma and supercontraction of myofibrils seemed to be the key events leading to cardiomyocyte death. Thus, the intermediate filaments are required to maintain the basic integrity of cardiomyocytes and especially the link between the intermediate filaments and the sarcolemma appear more important than previously realized.

Animals↗