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PubMed1989

Effects of extracellular matrix on cytoskeletal and myofibrillar organization in vitro.

The distribution and three-dimensional relationship of myofibrillar and cytoskeletal components during myofibrillogenesis were examined in preparations of neonatal rat cardiac myocytes processed in parallel for scanning electron microscopy (SEM), intermediate voltage transmission electron microscopy (IVEM) and immunofluorescence (IF). Of the various methods used for processing, optimal results were achieved by pre-extraction with Triton X-100 in an actin-stabilizing buffer. This procedure effectively removed the surface membrane, as viewed by SEM images, while preserving myofibrillar and cytoskeletal structure, as evidenced by IF for actin, alpha-actinin and vinculin. Cytoskeletons in SEM images consisted of a cortex of anastomosing filaments through which ran parallel filament bundles oriented in the long axis of the cell and attached along their length to the substrate by numerous fine filaments. In IVEM images, myofibrils were laterally connected at the level of the Z bands. Myocytes grown on different extracellular matrices showed different patterns and distributions of both striated myofibrils and focal adhesions, as determined by IF for alpha-actinin and vinculin, respectively. Cells on collagen I and III contained striated myofibrils which extended to the cell perimeters where focal adhesions were predominately located. Cells on laminin and fibronectin matrices exhibited myofibrils and focal adhesions more centrally located. In addition, cells on laminin contained circumferential arcs of filaments near the cell periphery.

Animals↗
PubMed1988

Effects of milrinone on Ca++-sensitivity of myofibrillar Mg-adenosine triphosphatase isolated from normal human and canine hearts.

Sensitization or desensitization of cardiac actomyosin to calcium has been demonstrated with several pharmacological agents. The effect of milrinone on the sensitivity of cardiac Mg-adenosine triphosphatase (ATPase) activity to calcium was studied in purified myofibrils isolated from normal human hearts (after accidental death or trauma that caused no cardiac damage as established by the attending physician) and from normal canine hearts (established by echocardiography), over a range of calcium concentrations (pCa, 8 to 5). Caffeine, a cardiac stimulant that has been shown to increase the sensitivity of myofibrillar Mg-ATPase activity to calcium in rat ventricle, was used in this study to establish its effect on canine and human myofibrils in comparison with that of milrinone. Caffeine, at concentrations of 40 mM, caused statistically significant sensitization of canine and human myofibrils to calcium. In canine myofibrils, the calcium-dependent Mg-ATPase activity increased from 11.0 +/- 1.2 to 18.8 +/- 2.6 nmol of Pi per mg of protein per min at pCa 6.73 (N = 9, P less than .05) and from 32.9 +/- 2.1 to 37.3 +/- 2.2 nmol of Pi per mg of protein per min at pCa 6.16 (N = 9, P less than .05), whereas total Mg-ATPase activity increased from 23.4 +/- 1.5 to 33.6 +/- 2.6 nmol of Pi per mg of protein per min at pCa 6.73 (N = 9, P less than .05) and from 45.2 +/- 2.2 to 52.2 +/- 2.5 nmol of Pi per mg of protein per min at pCa 6.16 (N = 9, P less than .05).(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1987

[Contractile properties and creatine kinase activity of myofilaments after ischemia and reperfusion of the rat heart].

The state of myofibril creatinkinase and contractile properties of chemically skinned myocardial fibers of rat after 70-90 min ischemia and 15-30 min reperfusion was studied. In spite of sharp fall in the total creatinkinase activity in the tissue, the enzyme activity in myofibrils does not change greatly. Ischemia does not change the functional abilities of myofibril creatinkinase as well as characteristics of Ca-activated contraction of skinned fibers. The results show that irreversible loss of myocardial contractile activity after prolonged ischemia and reperfusion is not connected with violation of myofilament characteristics or deterioration of functional association between myofibril creatinkinase and ATPase.

Actin Cytoskeleton↗
PubMed1982

Preparation of normal and ischemic myocardial tissue for scanning electron microscopy.

Normal and ischemic myocardium was prepared by slicing and cryofracture techniques for examination with the SEM. The tissues were dehydrated in ethanol and Freon 113 (slicing method) or were cryofractured in Freon 113 cooled with liquid nitrogen, followed by critical point drying and coating with gold and palladium. Some osmicated tissue pieces were treated with thiocarbohydrazide for examination without metal coating. Some hearts were infiltrated with silver particles and were examined with backscattered electron imaging technique (BSI). The cryofractured tissue provided the most useful and consistent surface features of the cell organelles with a minimum of mechanical disorder compared to other methods. Although the myocardium prepared by slicing method revealed the interior of the cells, it contained several frayed edges and loose myofibrils making interpretation of the ischemic myocardium difficult. The normal cells exhibited myofibrils covered by transverse tubules at the level of Z bands as confirmed by BSI using silver particles as an extracellular tracer and numerous oval to elongated mitochondria located between the myofibrils. An extensive network of tubules (sarcoplasmic reticulum) over the sarcomeres and nuclei were observed. The changes observed by SEM in the ischemic hearts were consistent with those seen in TEM. With prolonged coronary ligation the changes became obvious. The T-tubules were often broken and nuclei were distorted. The myofibrils were disorganized and formed homogeneous bands. These SEM studies suggest that myocardium prepared by cryofracture technique yields information on normal and ischemic cell structure consistent with data obtained by TEM.

Animals↗
PubMed1995

Human and canine cardiac troponin T and creatine kinase-MB distribution in normal and diseased myocardium. Infarct sizing using serum profiles.

OBJECTIVE: Cardiac troponin T (cTnT) has been suggested as a new, more specific marker of myocardial cellular damage. The objectives of this study were to examine the distribution of cTnT and creatine kinase (CK)-MB in normal and diseased heart tissue of dogs and humans, and to assess the use of serum cTnT for the estimation of infarct size in dogs. DESIGN: Serial serum specimens over 7 days were obtained from normal dogs (controls, n = 3) and dogs that underwent surgical coronary artery occlusion (n = 6). Heart muscle samples were obtained from the controls and after 3 weeks of occlusion in experimental dogs. Diseased human heart muscle samples were obtained at autopsy from patients who had died of acute myocardial infarction (n = 3). Normal heart muscle samples (n = 3) were obtained at autopsy from patients who died of non-cardiac-related illnesses. Tissues were sectioned and homogenized to harvest both cytosolic and myofibril-bound proteins. Serum samples and tissue homogenates were assayed for cTnT, CK-MB, and myoglobin (humans only). Total protein was assayed on homogenate samples and results were reported as milligrams per gram of total protein. RESULTS: The distributions of cTnT, CK-MB, and myoglobin were equivalent across 14 sites within normal human heart. Creatine kinase-MB and myoglobin were more than 99% cytosolic. Cardiac troponin T was 92% myofibril bound and 8% cytosolic. In the control dog hearts, cTnT was higher and CK-MB was lower in the right ventricle than in the left ventricle. While CK-MB and myoglobin were more than 99% cytosolic, cTnT was 98% myofibril bound and 2% cytosolic. Infarct sizing in dog hearts initially did not correlate well with serum cTnT or CK-MB concentrations. However, when the data were separated by infarct location (right coronary artery; left circumflex coronary artery), the correlations improved dramatically. Differences in tissue concentrations of cTnT and CK-MB between the left and right ventricle might explain the change in correlations. Coronary artery occlusion in dogs and humans resulted in decreased cytosolic and myofibril cTnT and increased CK-MB and myoglobin in diseased myocardial tissue. CONCLUSIONS: Our observed biochemical alterations suggest that the energy-producing proteins CK-MB and myoglobin are upregulated following cellular damage, while the structural and regulatory protein cTnT does not have a mechanism for replacement of lost protein following cell injury and necrosis.

Animals↗
PubMed1964

INTRACELLULAR DISTRIBUTION OF CALCIUM IN DEVELOPING BREAST MUSCLE OF NORMAL AND DYSTROPHIC CHICKENS.

To follow the intracellular distribution of calcium in the breast muscles of developing chickens, Ca(45) was injected into the albumen of predeveloped eggs. Since the embryos were grown in a radioactive medium, a complete exchange of the isotope for its non-radioactive counterpart in muscles was accomplished. Subcellular particulates of the muscle cells were separated by the method of differential centrifugation. Analysis of the separated fractions showed that in the muscles of the 13-day embryo, when the nuclear-myofibrillar ratio is high, 65 per cent of the muscle calcium is in the nuclei. With the increased synthesis of myofibrils, the nuclear-myofibrillar ratio decreases with a concomitant fall in radioactivity. Thus, calcium was not associated with the developing myofibrils. At the time of hatching, when myofibrils perform physiological work, the highest level of calcium is in the mitochondria. This suggests that the mitochondria play a key role in the physiological activities of calcium in the cell. The microsomal fraction reaches a maximal level of calcium when the adult composition of muscle is attained. Results of investigations on dystrophic muscles show changes in the calcium distribution of the fractions as early as the 3rd week of embryonic development, which are interpreted to indicate an alteration in the protein metabolism of the cell, or an early destruction of muscle tissue. Further, alterations in the calcium content of fractions which seem to regulate the movements of this ion in the cell are discussed. A new technique for homogenizing tissues from embryos of different ages is presented.

Animals↗
PubMed1997

Ultrastructural changes of the myocardium in the embryonic rat heart.

BACKGROUND: Ultrastructural changes of the embryonic heart have been described, and quantitative studies have reported the changes of cellular organelles in late fetal and postnatal development. However, no specific data are available on the quantitative morphology of the individual segments and intersegmental junctions of the early embryonic heart, although these components must have different functions. METHODS: We measured the absolute volumes of glycogen, Golgi complex, myofibrils, mitochondria, and the surface areas of the rough endoplasmic reticulum and mitochondrial cristae in the different regions of the embryonic rat heart by using stereological tools. RESULTS: During embryonic development, the cardiac segments and intersegmental junctions increase their glycogen volume. The sinoatrial junction and primary fold show a more rapid increase than all the other cardiac regions, whereas the atrioventricular canal shows a high level of glycogen content throughout the period studied. The Golgi complex and rough endoplasmic reticulum show a conspicuous decrease from day 15 onward. The cellular content of myofibrils and mitochondria and the surface area of the mitochondrial cristae show a gradual increase from day 11 to day 17 of development, but full maturation apparently takes place in late fetal and early postnatal stages. At day 15 of development, the cellular volumes of myofibrils and mitochondria show a temporary decrease. CONCLUSIONS: The glycogen content cannot be explained on the basis of metabolism alone. The storage of glycogen is hypothesized to serve mechanical cell stability and may also be related to a target mechanism for ingrowing nerves. Myofibrillar and mitochondrial contents of the myocytes indicate a relatively late differentiation of the venous pole of the heart. Uninterrupted maturation is only started at the time of septation.

Animals↗
PubMed1998

Role of M-line proteins in sarcomeric titin assembly during cardiac myofibrillogenesis.

A rat polyclonal anti-M-line protein antiserum and three mouse monoclonal anti-titin antibodies (E2, F3, and A12) were used to study the spatiotemporal relationship between M-line proteins and titin during myofibril assembly in cultured chicken cardiomyocytes by immunofluorescence microscopy. In day 2 cultures, M-line proteins and titin were detected as punctate staining in most cardiomyocytes, which possessed many nonstriated fibrils. At a late stage (day 3 cultures), M-line proteins were incorporated into dot-like structures along nonstriated fibrils, while titin staining was continuous on these structures. As development progressed, M-line proteins were registered in periodic pattern in the mid-A band. In cardiomyocytes from day 5 cultures, the titin bands were separated by an unstained region, and achieved their adult doublet pattern. Thus, the organization of titin in the sarcomere appears to occur later than that of M-line proteins in the M-line. Our morphological data indicate that the early registration of M-line proteins in primitive myofibrils may guide titin filament alignment via interaction between M-line proteins and titin. In order to investigate the role of M-line proteins in the assembly of titin filaments, anti-M-line protein or anti-titin antibodies were introduced into cultured cardiomyocytes by electroporation to functionally bind the respective proteins, and the profile of myofibril assembly was examined. Cardiomyocytes from day 2-3 cultures with incorporated anti-M-line protein antibodies became shrunk, and exhibited defective myofibrillar assembly, as shown by the failure of titin to assemble into a typical sarcomeric pattern. Incorporation of anti-titin antibody E2, which recognizes the M-line end domain of titin, resulted in the failure of M-line proteins organized into the M-line structure, as shown by random, sporadic staining with anti-M-line protein antibody. These studies confirm the essential role of M-line proteins in the organization of titin filaments in the sarcomere and that the interaction between titin and M-line proteins is crucial to the formation of the M-line structure.

Animals↗
PubMed2000

Role of desmin filaments in chicken cardiac myofibrillogenesis.

Desmin filaments are muscle-specific intermediate filaments located at the periphery of the Z-discs, and they have been postulated to play a critical role in the lateral registration of myofibrils. Previous studies suggest that intermediate filaments may be involved in titin assembly during the early stages of myofibrillogenesis. In order to investigate the putative function of desmin filaments in myofibrillogenesis, rabbit anti-desmin antibodies were introduced into cultured cardiomyocytes by electroporation to perturb the normal function of desmin filaments. Changes in the assembly of several sarcomeric proteins were examined by immunofluorescence. In cardiomyocytes incorporated with normal rabbit serum, staining for alpha-actinin and muscle actin displayed the typical Z-line and I-band patterns, respectively, while staining for titin with monoclonal anti-titin A12 antibody, which labels a titin epitope at the A-I junction, showed the periodic doublet staining pattern. Staining for C-protein gave an amorphous pattern in early cultures and identified A-band doublets in older cultures. In contrast, in cardiomyocytes incorporated with anti-desmin antibodies, alpha-actinin was found in disoriented Z-discs and the myofibrils became fragmented, forming mini-sarcomeres. In addition, titin was not organized into the typical A-band doublet, but appeared to be aggregated. Muscle actin staining was especially weak and appeared in tiny clusters. Moreover, in all ages of cardiomyocytes tested, C-protein remained in the disassembled form. The present data suggest the essential role of desmin in myofibril assembly.

Actinin↗
PubMed1980

New fine structural features of cardiac rhabdomyoma: report of a case.

Electron microscopy of a cardiac rhabdomyoma revealed two varieties of cells: (1) typical "spider cells' characterized by few myofibrils and large aggregates of glycogen particles free in the cytoplasm; and (2) cells with more myofibrils, less glycogen, and glycogen within membrane-limited vacuoles. These differences in myofibril development and glycogen content represent two succeeding stages in the early maturation of normal cardiocytes. The vacuoles containing glycogen were interpreted as autophagic and, consequently, active in the glycogen decrease typical of normal maturing cardiocytes. Rhabdomyoma cells did not show the structures, e.g., T system, characteristic of the late normal heart development. This study supports the theory that arrested cardiocyte maturation is a factor in the pathogenesis of cardiac rhabdomyoma.

Female↗
PubMed2000

Myofibrillogenesis and formation of cell contacts mediate the localization of N-RAP in cultured chick cardiomyocytes.

The expression of N-RAP was investigated in immuofluorescently stained embryonic chick cardiomyocyte cultures. After 1 day in culture, the cardiomyocytes were spherical and N-RAP, titin, alpha-actinin, and vinculin were all diffusely distributed. As the cardiomyocytes spread and formed myofibrils and cell contacts, N-RAP became localized to distinct areas in the cells. During myofibrillogenesis, N-RAP was found concentrated in premyofibrils. As the premyofibrils transformed into bundles of mature myofibrils, N-RAP became concentrated at the longitundal ends of the cells, and was not found in the mature sarcomeres. At sites of cell-cell contacts, N-RAP was localized to the cell junction even in cells without any significant myofibril formation. As the cell-cell contacts became more extensive and formed structures resembling the intercalated disks found in hearts, N-RAP became even more specifically concentrated at these junctions. The results show that myofibrillogenesis and cell contact formation can each independently target N-RAP to the longitudinal ends of cardiomyocytes.

Actinin↗
PubMed1979

Differentiation of myoepithelial cells in the developing rat sublingual gland.

Sublingual glands of rats were prepared for light and electron microscopy and for the histochemical demonstration of myofibrils and alkaline phosphatase (AkPase) activity. Through 17 days in utero, the epithelial cells of the glandular rudiment are relatively undifferentiated. At 18 days, the inner cells of the terminal buds begin to assemble around a lumen and accumulate secretory granules, while the outer cells flatten and form long processes. At 19 days, many of the outer cells have dilated cisternae of rough endoplasmic reticulum engorged with finely granular material. At 20 days, some of the outer cells have thin bands of microfilaments in their processes, suggesting that they are differentiating into myoepithelial cells (MEC). Though the secretory cells are almost mature at birth, only a few of the MEC have myofibrils detected with an actomyosin reaction, and AkPase activity is very weak. Progressive increases in AkPase activity and in myofibril size and number continue until the acini and intercalated ducts are fully invested with mature MEC at about 14 days after birth. Thus, the MEC and secretory cells begin to differentiate at the same time, but the MEC subsequently differentiate asynchronously with the secretory cells and with each other. Although the sublingual MEC are only partly differentiated in the newborn rat, their overall development occurs somewhat more rapidly than in the adjacent submandibular gland.

Actomyosin↗
PubMed1980

Differentiation of myoepithelial cells in the developing rat parotid gland.

Parotid glands of rats were prepared for light and electron microscopy and for the histochemical demonstration of myofibrils and alkaline phosphatase (AkPase) activity. Through 18 days in utero, the epithelial cells of the developing gland remain relatively undifferentiated. At 20 days in utero, a few cells in the outer layer of the terminal buds and adjacent segments of ducts acquire a cilium, the initial indication that they are differentiating into myoepithelial cells (MEC). Up until the time of birth, the only additional characteristics of MEC that the outer cells develop are to flatten against the underlying cells, begin to send out processes, and produce a few dilated cisternae of rough endoplasmic reticulum. Myofibrils and AkPase activity are first detected at the light microscopic level at five days after birth, around both the developing acini and intercalated ducts. Progressive increases in AkPase activity and in the size and number of myofibrils continue until the acini and intercalated ducts are invested with well-differentiated MEC at 15 days. Subsequently, as the acini undergo maturation during the weaning period (18-25 days), the MEC cease to surround the acini and assume the adult pattern of investing only the intercalated ducts. The pattern of MEC differentiation in the parotid gland differs from those in the sublingual and submandibular glands of the rat in several important respects. They begin to differentiate last, yet mature almost as early as do the MEC of the sublingual gland; they begin to differentiate prior to, rather than simultaneously with, the secretory cells; and their distribution changes as the acinar cells become mature.

Animals↗
PubMed1988

Immunolocalization of muscle and nonmuscle isoforms of actin in myogenic cells and adult skeletal muscle.

In vertebrate skeletal muscle, the proliferating myoblasts synthesize nonmuscle isoforms of actin, and the cells begin to express muscle-specific actin isoforms during their myogenic differentiation. To study the distributions of the actin isoforms in myogenic cells and fully differentiated skeletal muscle, we prepared a peptide antibody specific for the skeletal alpha isoform of actin and used this antibody along with an antibody specifically reactive with nonmuscle gamma actin to stain cultured myotubes and adult skeletal myofibrils by double-indirect immunofluorescence. At this level of resolution, no differences in isoform localization were seen: Both muscle and nonmuscle actins were detected in the myotubes and in the striations of mature myofibrils. Myotubes were also double-stained using immunogold electron microscopy, and the isoform distributions were determined quantitatively by counting the two sizes of gold particles that corresponded to labeling with each antibody. A quantitative analysis of immunoreactivity revealed that, although both forms were present in all actin-containing structures, nonmuscle actin was relatively more prevalent along the edges (cortical microfilaments) of the myotubes, whereas the muscle isoform predominated in the interior regions (containing forming myofibrils). Thus, we have found evidence of a heterogeneous distribution of muscle and nonmuscle actin isoforms in differentiating myogenic cells, and we have demonstrated that a nonmuscle actin isoform is a component of the muscle contractile apparatus.

Actins↗
PubMed1995

Deletion of amino acids from the carboxy-terminal end of actin.

A series of deletions was made from the C-terminal end of actin by inserting termination codons into a full length cDNA of human alpha-skeletal muscle actin. These included deletions of 2, 3, 10, 20, 30, and 40 amino acids. The cDNA clones were transcribed and the resulting mRNAs were translated in vitro using 35S-labeled methionine. The 35S-labeled actin and actin mutants were then tested for the ability to coassemble with carrier actin, bind DNAse I, bind myosin S-1, bind a 27 kDa proteolytic fragment of alpha-actinin, and incorporate into myofibrils in vitro. Removal of the C-terminal two or three amino acids did not grossly alter the properties of actin tested. Deletion of an additional 7 amino acids (10 amino acids total) significantly decreased coassembly, binding to DNAse I, and incorporation into myofibrils, but did not dramatically reduce binding to myosin S-1 or the 27 kDa fragment of alpha-actinin. Deletion of 20 or more amino acids virtually abolished all normal actin function tested. By examining the structure of actin, we propose that the effect of removing residues 356-365 is due to the important role Trp356 plays in maintaining hydrophobic bonds between three non-contiguous segments of actin. We also suggest that removal of residues 366-372 adversely affected the structure or orientation of the DNAse I binding loop and that this change can account for defects in actin binding to DNAse I, coassembly with wild type actin, and incorporation into myofibrils.

Actinin↗
PubMed1995

Nebulette: a 107 kD nebulin-like protein in cardiac muscle.

A 107-kD protein has been identified in primary cultures of chicken embryonic cardiomyocytes by immunoprecipitations with certain anti-nebulin monoclonal antibodies (mAbs). These mAbs, prepared against a fragment of human skeletal muscle nebulin located near the carboxyl terminus, detect a 107-kD protein in extracts of adult chicken heart, adult mouse heart, and adult rabbit heart by immunoblot analysis. A partial cDNA corresponding to this protein has been isolated by immunological screening of a chicken heart cDNA expression vector library. The partial cDNA encodes a 380-amino acid open reading frame composed entirely of nebulin-like 35-residue modules marked by the highly conserved sequence motifs: SXXXYK and TPD. The open reading frame exhibits 60-85% homology with skeletal muscle nebulins from a variety of species. This cDNA recognizes an approximately 8-kb transcript in cardiac RNA and does not hybridize to skeletal muscle RNAs by northern analysis. Immunofluorescence localization of this nebulin-like protein in primary cultures of chicken cardiomyocytes and embryonic chicken cardiac myofibrils indicates that the protein is localized to the I-Z-I complex of the myofibrils, extending approximately 25% of the thin filament length. Comparisons of the distribution of this protein relative to actin, myosin, and titin in spreading cardiomyocytes suggest that the cardiac nebulin-like protein becomes aligned with the nascent myofibrils early during myofibrillogenesis. To distinguish this petite nebulin-like protein from the 600-900 kD skeletal muscle nebulin, we have named it nebulette.

Animals↗
PubMed1975

Nature of muscular change in osteomalacia: light- and electron-microscope observations.

Thirteen muscle biopsy specimens (mainly the gluteus maximus) from 12 patients with laboratory confirmation of osteomalacia and proximal muscle weakness in 10 were examined by light and electron microscopy. Light microscopy revealed mild diffuse non-specific atrophy of the muscle fibres in 10 cases, severe generalised atrophy in one and patchy group atrophy in one. There was no myopathic change in specimens from cases with either a nutritional aetiology, or a mixed aetiology. The former, mostly women gave a history of severe chronic malnutrition often accompanied by repeated pregnancies and prolonged lactation; those with a mixed aetiology gave, in addition, evidence of a metabolic or endocrine disorder such as hyperparathyroidism, hyperthyroidism, uraemia, or treatment with anti-epileptic drugs or were of uncertain origin. Electron-microscope examination of muscle from the nutritional group showed atrophic changes in the fibres, such as loss of myofibrils, prominence of mitochondria and glycogen, loosening and folding of the basement-membrane but good preservation of the remaining myofibrils. In contrast muscle from cases of mixed aetiology showed, in addition to the atrophic features, clear degenerative changes in the myofibrils and the mitochondria, accumulation of amorphous material at the site of myofibrillar loss and of lipofuscin in muscle fibres, vascular endothelium and satellite cells. The earliest degenerative change was in the "I" band, involving actin filaments and "Z" line. The triads were generally preserved but the sarcoplasmic reticulum appeared affected in a patient with tetany and severe mitochondrial degeneration. In a patient with thyrotoxicosis, proliferation of central nuclei, "Z" line streaming and formation of "T" tubular aggregates were seen. In one patient with hyperparathyroidism and hypercalcaemia, severe myofibrillar degeneration and mitochondria showing osmiophilic deposits, possibly of calcium phosphate, were encountered. It is concluded: (1) that all osteomalacic muscle weakness is not myopathic but a non-specific atrophy occurring probably on the basis of disuse and malnutrition, and (2) patients with an added metabolic or endocrinological disorder show in addition to the atrophy, degenerative changes in the muscle fibre and its sub-cellular components consistent with myopathy, and these patients should be clearly distinguished from those with a background of malnutrition only.

Adolescent↗
PubMed2000

Purification of a novel serine proteinase inhibitor from the skeletal muscle of white croaker (Argyrosomus argentatus).

A novel serine proteinase inhibitor has been purified to homogeneity from the skeletal muscle of white croaker (Argyrosomus argentatus). The purification was carried out by ammonium sulfate fractionation, DEAE-Sephacel, heating treatment followed by column chromatographies on SP-Sepharose, Sephadex G-150 and gel-filtration high performance liquid chromatography. The molecular mass of the inhibitor was 55 kDa as estimated by SDS-PAGE and gel filtration. It specifically inhibited a myofibril-bound serine proteinase (MBSP) isolated from the skeletal muscle of lizard fish (Saurida wanieso). No inhibition, however, was detected toward other serine proteinases such as bovine trypsin, bovine chymotrypsin and a myofibril-bound serine proteinase from carp (Cyprinus carpio) muscle. Interestingly, the sequences of tryptic digested peptide fragments of MBSPI revealed high identity to that of porcine phosphoglucose isomerase (PGI) (76%) and other PGIs. Furthermore, purified MBSPI exhibits PGI activity, suggesting the inhibitor is a protein closely related to PGI. When rabbit muscle PGI was investigated, it also specifically suppressed the activity of MBSP. It thus strongly suggests that MBSPI is actually PGI and conversely, PGI is a specific inhibitor toward myofibril-bound serine proteinase(s).

Amino Acid Sequence↗