Relationship between the level of polarization of skeletal muscle fibers and their total protein content in young mature and immature rats

1972 ◽  
Vol 74 (4) ◽  
pp. 1231-1233
Author(s):  
N. V. Darinskii ◽  
L. A. Siryk
Keyword(s):  
Skeletal Muscle ◽  
Protein Content ◽  
Total Protein ◽  
Muscle Fibers ◽  
Total Protein Content ◽  
Skeletal Muscle Fibers ◽  
Immature Rats

Basal, but not overload-induced, myonuclear addition is attenuated by NG-nitro-l-arginine methyl ester (l-NAME) administration

2007 ◽  
Vol 85 (6) ◽  
pp. 646-651 ◽  
Author(s):  
Scott E. Gordon ◽  
Christopher M. Westerkamp ◽  
Kathleen J. Savage ◽  
Robert C. Hickner ◽  
Sarah C. George ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Methyl Ester ◽  
Protein Content ◽  
Body Mass ◽  
Total Protein ◽  
Total Protein Content ◽  
Sham Operation ◽  
Sprague Dawley ◽  
Surgical Ablation ◽  
Cross Sectional

The purpose of this study was to examine the effect of blocking nitric oxide synthase (NOS) activity via NG-nitro-l-arginine methyl ester (l-NAME) on myonuclear addition in skeletal muscle under basal and overloaded conditions. Female Sprague–Dawley rats (approx. 220 g) were placed into 1 of the following 4 groups (n = 7–9/group): 7-day skeletal muscle overload (O), sham operation (S), skeletal muscle overload with l-NAME treatment (OLN), and sham operation with l-NAME treatment (SLN). Plantaris muscles were overloaded via bilateral surgical ablation of the gastrocnemius muscles and l-NAME (0.75 mg/mL) was administered in the animals’ daily drinking water starting 2 days prior to surgery and continued until sacrifice. Myonuclear addition was assessed as subsarcolemmal incorporation of nuclei labeled with 5-bromo-2′-deoxyuridine (approx. 25 mg·(kg body mass)–1·day–1) delivered via osmotic pump during the overload period. As expected, muscle wet mass, total protein content, fiber cross-sectional area, and myonuclear addition were significantly higher (p ≤ 0.05) in O vs. S; however, only the increase in wet mass and total protein content (per body mass) were attenuated by l-NAME administration. Interestingly, l-NAME significantly reduced myonuclear addition by 75% in nonoverloaded muscles (SLN vs. S). Muscle hepatocyte growth factor protein content increased with overload, but was unaffected by l-NAME in either loading state. These data indicate that NOS inhibition in rat plantaris muscle attenuates myonuclear addition under basal, but not overloaded, conditions.

COPD Results in a Reduction in UCP3 Long mRNA and UCP3 Protein Content in Types I and IIa Skeletal Muscle Fibers

2004 ◽  
Vol 24 (5) ◽  
pp. 332-339 ◽  
Author(s):  
Aaron P. Russell ◽  
Emmanuel Somm ◽  
Richard Debigaré ◽  
Oliver Hartley ◽  
Denis Richard ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Content ◽  
Muscle Fibers ◽  
Skeletal Muscle Fibers

The “KIMWIPE” Effect in Ultra-Thin Cryosections

1985 ◽  
Vol 43 ◽  
pp. 458-459
Author(s):  
I. Taylor ◽  
P. Ingram ◽  
J.R. Sommer
Keyword(s):  
Skeletal Muscle ◽  
Electrical Stimulation ◽  
Muscle Fibers ◽  
Ice Crystals ◽  
Crystal Formation ◽  
Ice Crystal ◽  
Thin Sections ◽  
Skeletal Muscle Fibers ◽  
Freeze Dried ◽  
Ice Crystal Formation

In studying quick-frozen single intact skeletal muscle fibers for structural and microchemical alterations that occur milliseconds, and fractions thereof, after electrical stimulation, we have developed a method to compare, directly, ice crystal formation in freeze-substituted thin sections adjacent to all, and beneath the last, freeze-dried cryosections. We have observed images in the cryosections that to our knowledge have not been published heretofore (Figs.1-4). The main features are that isolated, sometimes large regions of the sections appear hazy and have much less contrast than adjacent regions. Sometimes within the hazy regions there are smaller areas that appear crinkled and have much more contrast. We have also observed that while the hazy areas remain still, the regions of higher contrast visibly contract in the beam, often causing tears in the sections that are clearly not caused by ice crystals (Fig.3, arrows).

Effect of External Calcium and other Divalent Cations on K+ Contractures in Denervated Slow Skeletal Muscle Fibers of the Frog

2019 ◽  
Author(s):  
Leonardo Hernández
Keyword(s):  
Skeletal Muscle ◽  
Binding Capacity ◽  
Divalent Cations ◽  
Muscle Fibers ◽  
Free Calcium ◽  
Slow Skeletal Muscle ◽  
Skeletal Muscle Fibers ◽  
Free Calcium Concentration ◽  
Chronic Denervation ◽  
Denervated Muscles

The influence of Ca2+ and other divalent cations on contractile responses of slow skeletal muscle fibers of the frog (Rana pipiens) under conditions of chronic denervation was investigated.Isometric tension was recorded from slow bundles of normal and denervated cruralis muscle in normal solution and in solutions with free calcium concentration solution or in solutions where other divalent cations (Sr2+, Ni2+, Co2+ or Mn2+) substituted for calcium. In the second week after nerve section, in Ca2+-free solutions, we observed that contractures (evoked from 40 to 80 mM-K+) of non-denervated muscles showed significantly higher tensions (p<0.05), than those from denervated bundles. Likewise, in solutions where calcium was substituted by all divalent cations tested, with exception of Mn2+, the denervated bundles displayed lower tension than non-denervated, also in the second week of denervation. In this case, the Ca2+ substitution by Sr2+ caused the higher decrease in tension, followed by Co2+ and Ni2+, which were different to non-denervated bundles, as the lowest tension was developed by Mn2+, followed by Co2+, and then Ni2+ and Sr2+. After the third week, we observed a recovery in tension. These results suggest that denervation altering the binding capacity to divalent cations of the voltage sensor.

scholarly journals NOS I IN PIGEON SKELETAL MUSCLE FIBERS*

1997 ◽  
Vol 75 ◽  
pp. 36
Author(s):  
R Gossrau ◽  
Z Grozdanovic
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Skeletal Muscle Fibers

scholarly journals Development of a human neuromuscular tissue-on-a-chip model on a 24-well-plate-format compartmentalized microfluidic device

Lab on a Chip ◽  
2021 ◽  
Author(s):  
Kazuki Yamamoto ◽  
Nao Yamaoka ◽  
Yu Imaizumi ◽  
Takunori Nagashima ◽  
Taiki Furutani ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Microfluidic Device ◽  
Motor Neurons ◽  
Muscle Fibers ◽  
Three Dimensional ◽  
Tissue Model ◽  
Skeletal Muscle Fibers

A three-dimensional human neuromuscular tissue model that mimics the physically separated structures of motor neurons and skeletal muscle fibers is presented.

scholarly journals Glycogenin is Dispensable for Glycogen Synthesis in Human Muscle, and Glycogenin Deficiency Causes Polyglucosan Storage

2019 ◽  
Vol 105 (2) ◽  
pp. 557-566 ◽  
Author(s):  
Kittichate Visuttijai ◽  
Carola Hedberg-Oldfors ◽  
Christer Thomsen ◽  
Emma Glamuzina ◽  
Cornelia Kornblum ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Skeletal Muscle ◽  
Western Blot ◽  
Cardiac Muscle ◽  
Glycogen Synthesis ◽  
Muscle Fibers ◽  
Human Muscle ◽  
Missense Mutations ◽  
Skeletal Muscle Fibers ◽  
Glycogen Biosynthesis

Abstract Context Glycogenin is considered to be an essential primer for glycogen biosynthesis. Nevertheless, patients with glycogenin-1 deficiency due to biallelic GYG1 (NM_004130.3) mutations can store glycogen in muscle. Glycogenin-2 has been suggested as an alternative primer for glycogen synthesis in patients with glycogenin-1 deficiency. Objective The objective of this article is to investigate the importance of glycogenin-1 and glycogenin-2 for glycogen synthesis in skeletal and cardiac muscle. Design, Setting, and Patients Glycogenin-1 and glycogenin-2 expression was analyzed by Western blot, mass spectrometry, and immunohistochemistry in liver, heart, and skeletal muscle from controls and in skeletal and cardiac muscle from patients with glycogenin-1 deficiency. Results Glycogenin-1 and glycogenin-2 both were found to be expressed in the liver, but only glycogenin-1 was identified in heart and skeletal muscle from controls. In patients with truncating GYG1 mutations, neither glycogenin-1 nor glycogenin-2 was expressed in skeletal muscle. However, nonfunctional glycogenin-1 but not glycogenin-2 was identified in cardiac muscle from patients with cardiomyopathy due to GYG1 missense mutations. By immunohistochemistry, the mutated glycogenin-1 colocalized with the storage of glycogen and polyglucosan in cardiomyocytes. Conclusions Glycogen can be synthesized in the absence of glycogenin, and glycogenin-1 deficiency is not compensated for by upregulation of functional glycogenin-2. Absence of glycogenin-1 leads to the focal accumulation of glycogen and polyglucosan in skeletal muscle fibers. Expression of mutated glycogenin-1 in the heart is deleterious, and it leads to storage of abnormal glycogen and cardiomyopathy.

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