scholarly journals Gambaran makroskopik dan mikroskopik otot skelet pada hewan coba postmortem

2016 ◽  
Vol 4 (2) ◽  
Author(s):  
Gabriella B. Nelwan ◽  
Sunny Wangko ◽  
Taufik F. Pasiak
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscles ◽  
Interval Estimation ◽  
Postmortem Interval ◽  
Postmortem Changes ◽  
Muscle Fibres ◽  
Normal Muscle ◽  
Time Intervals ◽  
Death Time ◽  
Microscopic Change

Abstract: To make pathologists and law personnel aware of the importance of postmortem interval, published studies have reported a lot of methods for estimation of postmortem interval estimation of the remains. This study was aimed to obtain macroscopic and microscopic postmortem changes of skeletal muscle of two domestic pigs weighed 20 kg. This was a descriptive observational study. After the pigs were killed, death time, ambient temperature and humadity were noted. Postmortem evaluation were done at several time intervals, as follows: 30 minutes, 1 hour, 2 hours, 3 hours, 4 hours, 5 hours, 6 hours, 9 hours, 12 hours, 15 hours, 18 hours, 21 hours, 24 hours, 30 hours, 36 hours, 42 hours, and 48 hours. The results showed that at 2 hours after death, the skeletal muscle became pale and soft progressively. The earliest microscopic change was identified at 30 minutes postmortem as pyknotic nuclei of skeletal muscles followed by hydrophic degeneration of muscle fibers and congestion of muscle tisue. At 12 hours until 48 hours postmortem, all microscopic changes became more distinct and widely distributed in nearly all muscle fibres. Albeit, the striated pattern and some normal muscle fibres could still be identified until 48 hours postmortem.Conclusion: Macroscopic changes could be identified the earliest at 2 hours postmortem and microscopic changes could be identified at 30 minutes postmortem.Keywords: macroscopic, microscopic, skeletal muscle, postmortem changes Abstrak: Para peneliti telah banyak menggunakan metode-metode tertentu untuk membuat para penegak hukum dan ahli patologis lainnya memahami pentingnya penentuan jarak waktu kematian. Penelitian ini bertujuan untuk mengetahui gambaran perubahan makroskopik dan mikroskopik postmortem pada otot skelet hewan coba babi dengan massa tubuh lebih kurang 20 kg. Jenis penelitian ialah deskriptif observasional. Hewan coba dimatikan dengan cara ditusuk di bagian jantung, selanjutnya waktu kematian, suhu dan kelembaban ruangan dicatat. Otot skelet diamati pada beberapa interval waktu setelah kematian: 30 menit, 1 jam, 2 jam, 3 jam, 4 jam, 5 jam, 6 jam, 9 jam, 12 jam, 15 jam, 18 jam, 21 jam, 24 jam 30 jam, 36 jam, 42 jam dan 48 jam. Hasil penelitian mendapatkan bahwa otot skelet menjadi pucat dan lunak setelah 2 jam postmortem secara progresif. Pada 1 jam postmortem, tampak serat otot mengalami kongesti dan degenerasi hidropik. Perubahan mikroskopik tersebut menjadi lebih nyata dan tersebar luas di sebagian besar serat otot pada 12 jam sampai 48 postmortem. Walaupun demikian, corak seran lintang dan sebagian kecil serat otot masih tampak normal sampai 48 jam postmortem. Simpulan: Perubahan makroskopik telah dapat diidentifikasi pada 2 jam postmortem sedangkan perubahan mikroskopik mulai dapat diidentifikasi pada 30 menit postmortem.Kata kunci: makroskopik, mikroskopik, otot skelet, perubahan setelah kematian

scholarly journals Vesicle budding from endoplasmic reticulum is involved in calsequestrin routing to sarcoplasmic reticulum of skeletal muscles

2004 ◽  
Vol 379 (2) ◽  
pp. 505-512 ◽  
Author(s):  
Alessandra NORI ◽  
Elena BORTOLOSO ◽  
Federica FRASSON ◽  
Giorgia VALLE ◽  
Pompeo VOLPE
Keyword(s):  
Skeletal Muscle ◽  
Endoplasmic Reticulum ◽  
Sarcoplasmic Reticulum ◽  
Golgi Complex ◽  
Skeletal Muscles ◽  
Muscle Fibres ◽  
Vesicle Budding ◽  
Er Exit Sites ◽  
Skeletal Muscle Fibres ◽  
Mutant Forms

CS (calsequestrin) is an acidic glycoprotein of the SR (sarcoplasmic reticulum) lumen and plays a crucial role in the storage of Ca2+ and in excitation–contraction coupling of skeletal muscles. CS is synthesized in the ER (endoplasmic reticulum) and is targeted to the TC (terminal cisternae) of SR via mechanisms still largely unknown, but probably involving vesicle transport through the Golgi complex. In the present study, two mutant forms of Sar1 and ARF1 (ADP-ribosylation factor 1) were used to disrupt cargo exit from ER-exit sites and intra-Golgi trafficking in skeletal-muscle fibres respectively. Co-expression of Sar1-H79G (His79→Gly) and recombinant, epitope-tagged CS, CSHA1 (where HA1 stands for nine-amino-acid epitope of the viral haemagglutinin 1), barred segregation of CSHA1 to TC. On the other hand, expression of ARF1-N126I altered the subcellular localization of GM130, a cis-medial Golgi protein in skeletal-muscle fibres and myotubes, without interfering with CSHA1 targeting to either TC or developing SR. Thus active budding from ER-exit sites appears to be involved in CS targeting and routing, but these processes are insensitive to modification of intracellular vesicle trafficking and Golgi complex disruption caused by the mutant ARF1-N126I. It also appears that CS routing from ER to SR does not involve classical secretory pathways through ER–Golgi intermediate compartments, cis-medial Golgi and trans-Golgi network.

scholarly journals Differential distribution of ryanodine receptor type 3 (RyR3) gene product in mammalian skeletal muscles

1996 ◽  
Vol 316 (1) ◽  
pp. 19-23 ◽  
Author(s):  
Antonio CONTI ◽  
L. GORZA ◽  
Vincenzo SORRENTINO
Keyword(s):  
Skeletal Muscle ◽  
Muscle Contraction ◽  
Gene Product ◽  
Skeletal Muscles ◽  
Mammalian Species ◽  
Diaphragm Muscle ◽  
Muscle Fibres ◽  
Abdominal Muscles ◽  
Mammalian Skeletal Muscle ◽  
Specific Subset

Activation of intracellular Ca2+-release channels/ryanodine receptors (RyRs) is a fundamental step in the regulation of muscle contraction. In mammalian skeletal muscle, Ca2+-release channels containing the type 1 isoform of RyR (RyR1) open to release Ca2+ from the sarcoplasmic reticulum (SR) upon stimulation by the voltage-activated dihydropyridine receptor on the T-tubule/plasma membrane. In addition to RyR1, low levels of the mRNA of the RyR3 isoform have been recently detected in mammalian skeletal muscles. Here we report data on the distribution of the RyR3 gene product in mammalian skeletal muscles. Western-blot analysis of SR of individual muscles indicated that, at variance with the even distribution of the RyR1 isoform, the RyR3 content varies among different muscles, with relatively higher amounts being detected in diaphragm and soleus, and lower levels in abdominal muscles and tibialis anterior. In these muscles RyR3 was localized in the terminal cisternae of the SR. No detectable levels of RyR3 were observed in the extensor digitorum longus. Preferential high content of RyR3 in the diaphragm muscle was observed in several mammalian species. In situ hybridization analysis demonstrated that RyR3 transcripts are not restricted to a specific subset of skeletal-muscle fibres. Differential utilization of the RyR3 isoform in skeletal muscle may be relevant to the modulation of Ca2+ release with respect to specific muscle-contraction properties.

scholarly journals Increase in Subcellular GSK-3 Clusters in Insulin- and Adrenaline-treated Differentiated Rat Skeletal Muscle Fibres

2020 ◽  
Author(s):  
Katja Fink ◽  
Mateja Lobe Prebil ◽  
Nina Vardjan ◽  
Jorgen Jensen ◽  
Robert Zorec ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscles ◽  
Metabolic Regulation ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase 3 ◽  
Muscle Fibres ◽  
Optical Section ◽  
Rat Skeletal Muscle ◽  
Average Size ◽  
Skeletal Muscle Fibres

Glycogen synthase kinase 3 (GSK-3) plays an important role in metabolic regulation in skeletal muscles, and both insulin and adrenaline stimulate   GKS-3 phosphorylation. The aim of the present study was to study the effect of insulin and adrenaline on GSK-3 localisation in skeletal muscles.We characterized subcellular localization of (GSK-3) signal protein in fully differentiated muscle fibre by immunofluorescence and confocal microscopy. We stimulated muscle fibres with insulin and/or adrenaline. Images were analysed by segmentation of single central optical section of the muscle.We found GSK-3 to be localised in clusters. The number of GSK-3 clusters and their average size were increased after stimulation with insulin and/or adrenaline. Average GSK-3 particle size is linearly related to their quantity.We conclude that subcellular GSK-3 in isolated skeletal muscle fibres is localized in clusters and clustering increased after stimulation with insulin and/or adrenaline.

miR-378a influences vascularization in skeletal muscles

2019 ◽  
Vol 116 (7) ◽  
pp. 1386-1397 ◽  
Author(s):  
Bart Krist ◽  
Paulina Podkalicka ◽  
Olga Mucha ◽  
Mateusz Mendel ◽  
Aleksandra Sępioł ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Growth Factor ◽  
Skeletal Muscles ◽  
Viral Vectors ◽  
Muscle Fibres ◽  
Systemic Delivery ◽  
Artery Ligation ◽  
Ischaemic Injury ◽  
Angiogenic Effect

Abstract Aims MicroRNA-378a, highly expressed in skeletal muscles, was demonstrated to affect myoblasts differentiation and to promote tumour angiogenesis. We hypothesized that miR-378a could play a pro-angiogenic role in skeletal muscle and may be involved in regeneration after ischaemic injury in mice. Methods and results Silencing of miR-378a in murine C2C12 myoblasts did not affect differentiation but impaired their secretory angiogenic potential towards endothelial cells. miR-378a knockout (miR-378a−/−) in mice resulted in a decreased number of CD31-positive blood vessels and arterioles in gastrocnemius muscle. In addition, diminished endothelial sprouting from miR-378a−/− aortic rings was shown. Interestingly, although fibroblast growth factor 1 (Fgf1) expression was decreased in miR-378a−/− muscles, this growth factor did not mediate the angiogenic effects exerted by miR-378a. In vivo, miR-378a knockout did not affect the revascularization of the ischaemic muscles in both normo- and hyperglycaemic mice subjected to femoral artery ligation (FAL). No difference in regenerating muscle fibres was detected between miR-378a−/− and miR-378+/+ mice. miR-378a expression temporarily declined in ischaemic skeletal muscles of miR-378+/+ mice already on Day 3 after FAL. At the same time, in the plasma, the level of miR-378a-3p was enhanced. Similar elevation of miR-378a-3p was reported in the plasma of patients with intermittent claudication in comparison to healthy donors. Local adeno-associated viral vectors-based miR-378a overexpression was enough to improve the revascularization of the ischaemic limb of wild-type mice on Day 7 after FAL, what was not reported after systemic delivery of vectors. In addition, the number of infiltrating CD45+ cells and macrophages (CD45+ CD11b+ F4/80+ Ly6G−) was higher in the ischaemic muscles of miR-378a−/− mice, suggesting an anti-inflammatory action of miR-378a. Conclusions Data indicate miR-378a role in the pro-angiogenic effect of myoblasts and vascularization of skeletal muscle. After the ischaemic insult, the anti-angiogenic effect of miR-378a deficiency might be compensated by enhanced inflammation.

Serum carnosinase activities in patients with alcoholic chronic skeletal muscle myopathy

1988 ◽  
Vol 75 (2) ◽  
pp. 185-190 ◽  
Author(s):  
P. Duane ◽  
T. J. Peters
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Enzyme Activities ◽  
Muscle Fibres ◽  
Significant Activity ◽  
Type Ii ◽  
Normal Muscle ◽  
Serum Enzyme ◽  
Chronic Alcoholic ◽  
Muscle Biopsies

1. Serum carnosinase activity was assayed in a group of alcoholic patients with and without histologically proven atrophy of type II skeletal muscle fibres, and in control subjects. No significant activity was detected in muscle biopsy samples or washed erythrocytes. 2. Serum carnosinase activity was significantly lower in chronic alcoholic patients compared with a group of age-matched controls. Alcoholics with abnormal muscle biopsies had significantly lower enzyme activities than either those patients with normal muscle biopsies or the controls. Serum enzyme activities in patients with normal muscle biopsies were not significantly different from controls. 3. Serum carnosinase activity was inversely correlated with the degree of muscle atrophy as measured by the type II fibre atrophy factor. There was a positive correlation between the enzyme activity and skeletal muscle mass as reflected by the creatinine-height index. Furthermore, the enzyme activity significantly increased, with resolution or improvement in the myopathy, in patients who abstained from alcohol. 4. Kinetic studies showed that the reduced carnosinase activity was due mainly to a decrease in the apparent Vmax. The apparent Km was significantly higher in the myopathic compared with non-myopathic alcoholics. Mixing serum from controls and patients with myopathy gave the expected values, indicating the absence of a serum enzyme inhibitory factor. Acute alcohol loading had no effect on the serum carnosinase activity. 5. The decrease in serum carnosinase activity in alcoholics was not related to the severity of their liver disease. Assays of serum carnosinase in chronic alcoholics can thus be used as a marker of their associated myopathy.

scholarly journals Effect of the bendiocarb on the ultrastructure of rabbit skeletal muscle

2017 ◽  
Vol 86 (3) ◽  
pp. 219-222 ◽  
Author(s):  
Katarína Holovská ◽  
Viera Almášiová ◽  
Lucia Tarabová ◽  
Eva Petrovová ◽  
Viera Cigánková
Keyword(s):  
Electron Microscopy ◽  
Skeletal Muscle ◽  
Body Weight ◽  
Sarcoplasmic Reticulum ◽  
Skeletal Muscles ◽  
Ultrastructural Changes ◽  
Muscle Fibres ◽  
Carbamate Insecticides ◽  
Cytoplasmic Vesicles ◽  
Membrane Bound

Bendiocarb belongs to the group of carbamate insecticides that inhibit acetylcholinesterase. In agriculture, it is used to control a variety of insects, therefore it is important to examine every potential aspect of its toxicology. The aim of this study was to observe the effect of bendiocarb on the ultrastructure of the skeletal muscle in rabbits. Rabbits in all experimental groups received capsules of bendiocarb (96% Bendiocarb, Bayer, Germany) per os daily at a dose of 5 mg/kg body weight. Samples of skeletal muscles were collected on days 10 and 20. On day 10 of the experiment, muscle fibres were not affected consistently. The observed changes were moderate and focal. Electron microscopy revealed dilatation of sarcoplasmic reticulum, and myofilament disorganization. On day 20 of the experiment, the ultrastructural changes in muscle fibres were more intense and more frequent. The most important alteration was the disruption of the sarcomeres due to the lysis of both thick and thin myofilaments. However, in the unchanged regions of muscle fibres a prominent mitochondrial swelling was observed. Many mitochondria lacked cristae and thus appeared as large membrane-bound cytoplasmic vesicles. The results presented in this study indicate that bendiocarb affects the ultrastructure of skeletal muscles. The intensity of damage (dissolution of myofilaments and disruption of sarcomeres) was related to the duration of administration of bendiocarb.

scholarly journals MORPHOLOGICAL FEATURES OF THE UTERUS IN WOMEN AT DIFFERENT TIME INTERVALS OF THE POSTMORTEM PERIOD AS DIAGNOSTIC CRITERIA FOR ESTABLISHING THE POSTMORTEM INTERVAL

2021 ◽  
Vol 74 (4) ◽  
pp. 821-827
Author(s):  
Vasil O. Olkhovsky ◽  
Edgar K. Grygorian ◽  
Mykhailo S. Myroshnychenko ◽  
Sergii V. Kozlov ◽  
Kostiantyn M. Suloiev ◽  
...  
Keyword(s):  
Diagnostic Criteria ◽  
Uterine Prolapse ◽  
Postmortem Interval ◽  
Morphological Features ◽  
Postmortem Changes ◽  
Structural Elements ◽  
Autopsy Material ◽  
Time Intervals ◽  
Outer Membranes ◽  
Vascular Walls

The aim is to identify the morphological features of the uterus layers in women at different time intervals of the postmortem period as diagnostic criteria for establishing the postmortem interval. Materials and methods: In the study we used surgical and autopsy material – uterine tissue fragments. All materials were divided into two groups. The 1st group (G 1) included surgical material from women (n=6) who underwent removal of the uterus, or uterus with the appendages due to leiomyoma, uterine prolapse. The 2nd group (G 2) included autopsy material from 42 women with known causes of death and postmortem period (from 24 to 48 hours – 6 cases, from 49 to 72 hours – 7 cases, from 73 to 96 hours – 8 cases, from 97 to 120 hours – 6 cases, from 121 to 144 hours – 8 cases, more than 144 hours – 7 cases). Histological and immunohistochemical study methods were used. Results: A comprehensive morphological study of the women uterus revealed a time-dependent increase of postmortem changes in this organ linked with the increase of postmortem period. In cases of postmortem period duration up to 144 hours, the structural elements of the uterine layers were identified. In cases where the duration of the postmortem period was more than 145 hours, microscopically the uterus was represented by eosinophilic fibrous or dusty masses, the histogenesis of which could not be determined. The processes of autolysis occurred more intensely and faster in the mucous membrane of the uterus, in comparison with the muscular and serous membranes, and in the vessels – in their inner membrane, in comparison with the middle and outer membranes. Autolytic changes in the muscular membrane of the uterus and vascular walls occurred more intensely in muscle fibers compared to connective tissue fibers. Conclusions: The histological and immunohistochemical features of the women uterus at different postmortem periods have a certain forensic medical significance and can be used for establishing the postmortem interval.

Sprouting and degeneration of mammalian motor axons in normal and de-afferentated skeletal muscle

1966 ◽  
Vol 163 (993) ◽  
pp. 538-554 ◽  
Keyword(s):  
Skeletal Muscle ◽  
Life Span ◽  
General Property ◽  
Skeletal Muscles ◽  
Muscle Spindles ◽  
Rabbit Muscle ◽  
Motor Axons ◽  
Normal Muscle ◽  
Retrograde Degeneration ◽  
Limited Life

The occurrence of collateral and ultraterminal sprouting by skeletomotor and fusimotor axons is described in teased, silver preparations of normal and de-afferentated hindlimb skeletal muscles. In twelve cat and ten rabbit muscle spindles the proportions of plate-ending fusimotor axons showing sprouting were 30.4 and 34.0 % , respectively. If small end-plates, previously described in the literature as ‘accessory endings’, are regarded as young plates newly formed by collateral sprouts, the degree of sprouting in the two spindle samples is increased to 33.9 and 38.3 % , respectively. Sprouting by skeletomotor axons was observed in a variety of cat, rabbit, and rat muscles taken from normal muscles. In a sample of 567 terminal branches examined in muscles from the three animals, 8.1% bore sprouts, or 19.4% if the collaterals forming accessory endings are included as sprouts. Some evidence of retrograde degeneration among the terminal branches of skeletomotor axons innervating normal muscle is described. It is suggested that sprouting effects the replacement of old end-plates which degenerate after a limited life-span; and that it is a general property of the vertebrate motoneuron for its peripheral terminals to undergo cyclic renewal in this way. The greater degree of sprouting shown by fusimotor plate-ending axons as compared with skeletomotor ones is attributed to the fact that the innervation supplied to spindles by such axons is both multiple and polyneuronal. In conclusion, some of the implications of the replacement hypothesis, e.g. with regard to neuromuscular pathology, are discussed.

Creatine metabolism in vitamin E deficiency in the rat

1962 ◽  
Vol 202 (3) ◽  
pp. 453-460 ◽  
Author(s):  
G. B. Gerber ◽  
G. Gerber ◽  
T. R. Koszalka ◽  
V. M. Emmel
Keyword(s):  
Skeletal Muscle ◽  
Vitamin E ◽  
Skeletal Muscles ◽  
Normal Values ◽  
Specific Activity ◽  
Turnover Time ◽  
Tocopheryl Acetate ◽  
Time Intervals ◽  
Kidney Liver ◽  
Creatine Metabolism

Creatine-2-C14 was injected intraperitoneally into normal, vitamin E-deficient, and previously deficient rats treated with α-tocopheryl acetate. Creatine was isolated after various time intervals from different skeletal muscles, heart, brain, kidney, liver, blood serum, erythrocytes, retroperitoneal fat, urine, and total residual carcass, and its specific activity and quantity determined. Creatinine was isolated from urine and assayed for radioactivity. An increase in the ratio of specific activities of "free" creatine to muscle creatine was observed in vitamin E-deficient rats. After treatment with α-tocopheryl acetate, this ratio returned to normal values. From plots of specific activity vs. time, turnover times for creatine were computed: total carcass, 56 days; skeletal muscle, 51–53 days. Turnover time of creatine in carcass, brain, and skeletal muscle, with the exception of pectoralis muscle, was identical in normal and vitamin E-deficient rats. Specific activity in pools of free creatine of vitamin E-deficient rats initially was higher but subsequently became lower than that of normal rats. We concluded that uptake of creatine by muscle is diminished in vitamin E-deficient rats and as a consequence the size of the free creatine pool increases and creatinuria results.

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