scholarly journals Correlation between isometric force and intramuscular pressure in rabbit tibialis anterior muscle with an intact anterior compartment

2009 ◽  
Vol 40 (1) ◽  
pp. 79-85 ◽  
Author(s):  
Taylor M. Winters ◽  
Genaro S. Sepulveda ◽  
Patrick S. Cottler ◽  
Kenton R. Kaufman ◽  
Richard L. Lieber ◽  
...  
Keyword(s):  
Tibialis Anterior ◽  
Isometric Force ◽  
Tibialis Anterior Muscle ◽  
Intramuscular Pressure ◽  
Anterior Compartment

Intramuscular pressure varies with depth: The tibialis anterior muscle studied in 12 volunteers

1993 ◽  
Vol 64 (3) ◽  
pp. 377-381 ◽  
Author(s):  
Manoutch Nakhostine ◽  
Jorma R Styf ◽  
Sandra van Leuven ◽  
Alan R Hargens ◽  
David H Gershuni
Keyword(s):  
Tibialis Anterior ◽  
Tibialis Anterior Muscle ◽  
Intramuscular Pressure

scholarly journals Intramuscular Pressure of Human Tibialis Anterior Muscle Reflects in vivo Muscular Activity

2019 ◽  
Vol 10 ◽  
Author(s):  
Filiz Ateş ◽  
Brenda L. Davies ◽  
Swati Chopra ◽  
Krista Coleman-Wood ◽  
William Litchy ◽  
...  
Keyword(s):  
Tibialis Anterior ◽  
Tibialis Anterior Muscle ◽  
Muscular Activity ◽  
Intramuscular Pressure ◽  
Human Tibialis Anterior Muscle

Intramuscular Pressure in the Leg and Thigh Related to Tensile Strap Force During Knee Brace Wear

1998 ◽  
Vol 26 (4) ◽  
pp. 567-570 ◽  
Author(s):  
Olof Lundin ◽  
Jorma R. Styf
Keyword(s):  
Tibialis Anterior ◽  
Muscle Relaxation ◽  
Tensile Force ◽  
Tibialis Anterior Muscle ◽  
Blood Perfusion ◽  
Rectus Femoris ◽  
Intramuscular Pressure ◽  
Knee Brace ◽  
External Compression ◽  
Mean Values

The effects of a functional knee brace on intramuscular pressure in the leg and thigh were measured in eight subjects with a mean age of 32 years. Pressures in the tibialis anterior and rectus femoris muscles were recorded without a knee brace and with a brace applied with strap tensile force of 25 N, 50 N, and a force preferred by the subject. External compression caused by the brace significantly increased intramuscular pressures at rest and muscle relaxation pressure during exercise in the leg and thigh muscles. Pressure in the tibialis anterior muscle increased 3 to 10 times, to mean values between 17.5 and 41 mm Hg, depending on the tensile force of the straps used at brace application. Corresponding mean pressure values in the rectus femoris muscle were between 17.5 and 32.5 mm Hg. Mean pressures in the standing subject varied between 37 and 62 mm Hg. Our study showed that intramuscular pressure at rest and muscle relaxation pressure during exercise in the tibialis anterior and the rectus femoris muscles increased significantly in the braced limb. Local blood perfusion pressure in the supine subject decreased significantly, by 16% to 42%, in the compressed muscles.

Motor-unit categorization based on contractile and histochemical properties: a glycogen depletion analysis of normal and reinnervated rat tibialis anterior muscle

1992 ◽  
Vol 67 (5) ◽  
pp. 1404-1415 ◽  
Author(s):  
J. E. Totosy de Zepetnek ◽  
H. V. Zung ◽  
S. Erdebil ◽  
T. Gordon
Keyword(s):  
Tibialis Anterior ◽  
Isometric Force ◽  
Tibialis Anterior Muscle ◽  
Continuous Distribution ◽  
Motor Units ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Glycogen Depletion ◽  
Time To Peak ◽  
Fast Twitch

1. Isolated and glycogen-depleted motor units (MUs) have been studied in normal and reinnervated tibialis anterior (TA) muscles of the rat to examine 1) the correspondence between physiological and histochemical classifications, 2) the extent to which unit properties cluster according to type, 3) the relation between unit force and fatigability, and 4) the extent to which reinnervated MUs recover their former properties. 2. MUs were isolated by ventral root dissection and stimulation in reinnervated and normal TA muscles, 3.5-8 mo after common peroneal (CP) nerve section and resuture and in age-matched control rats, respectively. The units were characterized physiologically for classification into four types: slow twitch (S), fast twitch, fatigue resistant (FR), fast twitch fatigue intermediate (FI), and fast twitch fatigue sensitive (FF). Four muscle fiber types were identified histochemically with the use of a modification of the techniques of Brooke and Kaiser, and Guth and Samaha to delineate fiber subtypes on the basis of the pH sensitivity of myofibrillar adenosine triphosphatase (ATPase). 3. Neither the time-to-peak twitch force development nor the profile of unfused tetanus ("sag test") was unambiguous in separating fast from slow MUs. However, all units with a time to peak greater than 22 ms were fatigue resistant, and this time was chosen to delineate fast from slow. The fast unit population was further subdivided on the basis of their fatigability. There is normally a small proportion of S units (6% S) that increased to 20% after reinnervation. Although the fast population was subdivided, there was a continuous distribution of fatigue indexes in normal and reinnervated muscles with the highest number of fast units falling into the FI category. The proportions of fast units were 28% FR, 45% FI, and 21% FF in normal muscles and 29% FR, 38% FI, and 13% FF in reinnervated muscles. 4. In normal muscles, delineation of fast and slow fibers and subdivision of fast fiber types on the basis of acid and alkali stability of myofibrillar ATPase provided a histochemical classification that showed 78% correspondence with physiological classification of the same identified units. In reinnervated muscles the correspondence between physiological and histochemical classifications was reduced to 72%. 5. The normal correlation between MU fatigability and isometric force in TA muscles was not seen in reinnervated muscles that contained more FR MUs. Mean fatigue index from normal units was significantly less at 0.55 +/- 0.03 (mean +/- SE) compared with 0.68 +/- 0.03 from reinnervated units.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals A High Protein Diet Does Not Improve Protein Synthesis in the Nonweight-Bearing Rat Tibialis Anterior Muscle

1996 ◽  
Vol 126 (1) ◽  
pp. 266-272 ◽  
Author(s):  
Daniel Taillandier ◽  
Charles-Yannick Guezennec ◽  
Philippe Patureau-Mirand ◽  
Xavier Bigard ◽  
Maurice Arnal ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Tibialis Anterior ◽  
Tibialis Anterior Muscle ◽  
High Protein Diet ◽  
High Protein ◽  
Protein Diet

Structure of the cortical cytoskeleton in fibers of postural muscles and cardiomyocytes of mice after 30-day 2-g centrifugation

2015 ◽  
Vol 118 (5) ◽  
pp. 613-623 ◽  
Author(s):  
Irina V. Ogneva ◽  
V. Gnyubkin ◽  
N. Laroche ◽  
M. V. Maximova ◽  
I. M. Larina ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Tibialis Anterior ◽  
Mechanical Load ◽  
Tibialis Anterior Muscle ◽  
Muscle Fibers ◽  
Control Group ◽  
Negative Effects ◽  
Transverse Stiffness ◽  
G 12 ◽  
Cortical Cytoskeleton

Altered external mechanical loading during spaceflights causes negative effects on muscular and cardiovascular systems. The aim of the study was estimation of the cortical cytoskeleton statement of the skeletal muscle cells and cardiomyocytes. The state of the cortical cytoskeleton in C57BL6J mice soleus, tibialis anterior muscle fibers, and left ventricle cardiomyocytes was investigated after 30-day 2- g centrifugation (“2- g” group) and within 12 h after its completion (“2- g + 12-h” group). We used atomic force microscopy for estimating cell's transverse stiffness, Western blotting for measuring protein content, and RT-PCR for estimating their expression level. The transverse stiffness significantly decreased in cardiomyocytes (by 16%) and increased in skeletal muscles fibers (by 35% for soleus and by 29% for tibialis anterior muscle fibers) in animals of the 2-g group (compared with the control group). For cardiomyocytes, we found that, in the 2- g + 12-h group, α-actinin-1 content decreased in the membranous fraction (by 27%) and increased in cytoplasmic fraction (by 28%) of proteins (compared with the levels in the 2- g group). But for skeletal muscle fibers, similar changes were noted for α-actinin-4, but not for α-actinin-1. In conclusion, we showed that the different isoforms of α-actinins dissociate from cortical cytoskeleton under increased/decreased of mechanical load.

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