Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 17

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych:  myosin heavy chain
help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
The aim of the present study was to define the effect of TGF-β1 on C2C12 myoblasts myogenesis. TGF-β1 together with its receptor is a negative auto-paracrine regulator of myogenesis, which influences the proliferation, differentiation, and functions of muscle cells. TGF-β1 exerts highly significant inhibitory effect on differentiation of C2C12 mouse myoblasts manifested by the impairment of cell fusion and very low expression of myosin heavy chain. The study of differentiating C2C12 mouse myoblasts treated with TGF-β1 revealed 502 genes (436 down-regulated and 66 up-regulated) with statistically different expression. TGF-β1-regulated genes were identified to be involved in 29 biological processes, 29 molecular functions groups and 59 pathways. The strongest inhibiting effect of TGF-β1 was observed in the cadherin and Wnt pathways. The key-genes that could play the role of TGF-β1 targets during myoblasts differentiation was identified such as: Max, Creb1, Ccna2, Bax, MdfI, Tef, Tubg1, Cxcl5, Rho, Calca and Lgals4.
We have examined the effect of 5 week cycling endurance training program on the sarco(endo)plasmic reticulum Ca2+ ATPase isoforms (SERCA1 and 2) and myosin heavy chain (MyHC) in the vastus lateralis muscle as well as on the oxygen uptake to power output ratio (VO2/PO) during incremental cycling. Fifteen untrained men performed an incremental cycling exercise until exhaustion before and after moderate intensity training. Muscle biopsies were taken from vastus lateralis before and after training program. Training resulted in higher (P = 0.048) maximal oxygen uptake (VO2max) as well as in higher power output reached at VO2max (P = 0.0001). Moreover, lower (P = 0.02) VO2/PO ratio determined during incremental moderate intensity cycling (i.e. 30-120 W) as well as lower (P = 0.003) VO2/PO ratio reached at VO2max were observed after the training. A significant down regulation of SERCA2 protein (P = 0.03) and tendency (P = 0.055) to lower SERCA1 content accompanied by lower (P<10-4) plasma thyroid hormone concentration, with no changes (P = 0.67) in MyHC composition in vastus lateralis muscle were found after training. We have concluded that the increase in mechanical efficiency of cycling occurring during first weeks of endurance training is not related to changes in MyHC composition but it may be due to down-regulation of SERCA pumps.
In this study we have examined the relationship between the content of different isoforms of MyHC in the vastus lateralis m. quadricipitis femoris and the VO2 / power output relationship during incremental cycling exercise. Twenty-one male subjects: aged 24.0 ± 2.5 years, body mass 73.0 ± 7.2 kg, height 179 ± 5 cm, BMI 22.78 ± 1.84 kg . m-2 , VO2 max 3697 ± 390 ml . min-1 , 50.9 ± 5.2 ml . kg-1 . min-1 , participated in this experiment. The subjects performed an incremental exercise test until exhaustion. The exercise test started at power output of 30 W, followed by an increase amounting to 30 W every 3 minutes. The pedalling rate was maintained at 60 rev . min-1 . Gas exchange variables were measured continuously using breath-by- breath system Oxycon Jaeger. At the end of each step blood samples were taken for lactate concentration. Muscle biopsy samples taken from the vastus lateralis m. quadricipitis femoris, using the Bergstrom needle, were analysed for the content of different MyHC (I, IIa, IIx) using SDS-PAGE and Western blotting. The pre-exercise VO2, as a mean value of six-minute measurements, expressed both in ml . min-1 , and in ml . kg -1 . min-1 , was positively correlated with the content of MyHC II in the vastus lateralis (p < 0.01). We have also found that the pre-exercise values of VO2 in the group of subjects with a high proportion of MyHC II (59.9 ± 11.2 %) were significantly higher (p < 0.02, when VO2 was expressed in ml . min-1 , and p < 0.01 when VO2 was expressed in ml . kg-1 . min-1 ) than in the group with low content of MyHC II (27.5 ± 6.0 %) in the vastus lateralis. Moreover, we have found a significant negative correlation (r = -0.562, p < 0.01) between the slope in the VO2/PO relationship below the lactate threshold (LT) and the content of MyHC IIa in the vastus lateralis. The most interesting finding of our study was that the magnitude of the non-linear increase in the VO2 / power output relationship present above the LT was positively correlated ( r = 0.510, p < 0.02) with the content of MyHC II in the vastus lateralis. Our results show, that there is no simple relationship between the content of different types of MyHC in the vastus lateralis and the oxygen cost of work during incremental exercise test. Individuals with a high content of MyHC II in the vastus lateralis m. quadricipitis femoris consume more oxygen in the pre-exercise conditions than subjects with a low content of MyHC II in their muscles. Subjects with a high content of MyHC II require a smaller increase in VO2 for maintaining a linear increase in power output up to the lactate threshold (lower slope in this relationship), but after exceeding the LT, they consume more oxygen above that expected from the linear relationship below the LT, than the subjects with a low content of MyHC II in their muscles. Therefore, non-linear increase in the VO2 / power output relationship, present above the LT, is more pronounced in subjects with a higher content of MyHC II in the vastus lateralis m. quadricipitis femoris.
The myosin heavy chain (MHC) was studied by biochemical methods in the slow-twitch (soleus) and two fast-twitch leg muscles of the triiodothyronine treated (hyperthyroid), thyreoidectomized (hypothyroid) and euthyroid (control) rats. The changes in the contents of individual MHC isoforms (MHC-1, MHC-2A, MHC-2B and MHC-2X) were evaluated in relation to the muscle mass and the total MHC content. The MHC-1 content decreased in hyperthyreosis, while it increased in hypothyreosis in the soleus and in the fast muscles. The MHC-2A content increased in hyperthyreosis and it decreased in hypothyreosis in the soleus muscle. In the fast muscles hyperthyreosis did not affect the MHC-2A content, whereas hypothyreosis caused an increase in this MHC isoform content. The MHC-2X, present only in traces or undetected in the control soleus muscle, was synthesised in considerable amount in hyperthyreosis; in hypothyreosis the MHC-2X was not detected in the soleus. In the fast muscles the content of MHC-2X was not affected by any changes in the thyroid hormone level. The MHC-2B seemed to be not influenced by hyperthyreosis in the fast muscles, whereas the hypothyreosis caused a decrease of its content. In the soleus muscle the MHC-2B was not detected in any groups of rats. The results suggest that the amount of each of the four MHC isoforms expressed in the mature rat leg muscles is influenced by the thyroid hormone in a different way. The MHC-2A and the MHC-2X are differently regulated in the soleus and in the fast muscles; thyroid hormone seems to be necessary for expression of those isoforms in the soleus muscle.
 The sarcoplasmic reticulum Ca2+-ATPase (SERCA) isoforms are normally expressed in coordination with the corresponding myosin heavy chain (MyHC) isoforms in the fibers of skeletal muscle but this coordination is often disrupted in pathological conditions. In the streptozotocin-induced diabetes of rats (stz-rats), the soleus muscle showed peripheral neuropathy and the SERCA2a level decreased in type I (slow-oxidative) fibers compared to the control muscles, whereas the expression of the corresponding slow MyHC1 did not change. No difference was found at the mRNA and protein levels of SERCA and MyHC isoforms in the whole soleus, except that the level of the SERCA2a protein specifically declined in stz-rats compared to the controls. This shows that the coordinated expression of SERCA2a and MyHC1 is disrupted at the SERCA2a protein level in the diabetic soleus. The results are in line with previous observations that regulators of the Ca-homeostasis may adapt faster to type I diabetes than the contractile elements.
The aim of this studyto determine the amount of myosin heavy chain (MyHC) proteins and MyHC mRNA in muscles of patients with different positions of the mandible. Ten adult patients for orthognathic surgery were divided into two groups: distal and mesial malocclusion. The mRNA expression of two MyHC isoforms of the anterior and posterior part of the right and left side of the human masseter muscle was analysed with a competitive RT-PCR assay. An exogenous template that includes oligonucleotide sequences specific for sarcomeric MyHC isoforms (1 and 2x) was constructed and utilized as competitor. Different isoforms of the MyHC protein were identified by Western blot analysis. In the total mRNA pool of the masseter muscle, the MyHC 1 mRNA level was 25.5 ± 7.6% and the MyHC 2x mRNA was 2.5 ± 1.2%. The anterior part of the masseter muscle from patients with distal occlusion contained more type 1 and 2x MyHC mRNA, as compared to patients with mesial occlusion (P < 0.05). No difference in the protein distribution was observed. The differences in mRNA expression may be caused by the enforced stress of the masticatory muscle in distal occlusion because of the disadvantageous pivot.
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.