scholarly journals Skeletal Muscle Gender Dimorphism from Proteomics

Author(s):  
Kalina Dimova ◽  
Lauren Ann Metskas ◽  
Mohini Kulp ◽  
Stylianos P. Scordilis
PLoS ONE ◽  
2008 ◽  
Vol 3 (10) ◽  
pp. e3466 ◽  
Author(s):  
Borja Guerra ◽  
Teresa Fuentes ◽  
Safira Delgado-Guerra ◽  
Amelia Guadalupe-Grau ◽  
Hugo Olmedillas ◽  
...  

2008 ◽  
Vol 1777 ◽  
pp. S61
Author(s):  
Yolanda Gómez-Pérez ◽  
Emilia Amengual-Cladera ◽  
Antoni Català-Niell ◽  
Elena Thomàs-Moyà ◽  
Magdalena Gianotti ◽  
...  

2011 ◽  
Vol 28 (5) ◽  
pp. 981-996 ◽  
Author(s):  
Tae Seok Oh ◽  
Jung-Won Choi ◽  
Duk Kwon Choi ◽  
Rajib Mukherjee ◽  
Hao Liu ◽  
...  

Author(s):  
Lauren Metskas ◽  
Mohini Kulp ◽  
Stylianos Scordilis

AbstractSkeletal muscle is a plastic tissue with known gender dimorphism, especially at the metabolic level. A proteomic comparison of male and female murine biceps brachii was undertaken, resolving an average of 600 protein spots of MW 15–150 kDa and pI 5–8. Twenty-six unique full-length proteins spanning 11 KOG groups demonstrated statistically significant (p<0.05) abundance differences between genders; the majority of these proteins have metabolic functions. Identified glycolytic enzymes demonstrated decreased abundance in females, while abundance differences in identified oxidative phosphorylation enzymes were specific to the proteins rather than to the functional group as a whole. Certain cytoskeletal and stress proteins showed specific expression differences, and all three phosphorylation states of creatine kinase showed significant decreased abundance in females. Expression differences were significant but many were subtle (≤ 2-fold), and known hormonally-regulated proteins were not identified. We conclude that while gender dimorphism is present in non-exercised murine skeletal muscle, the proteome comparison of male and female biceps brachii in exercise-naive mice indicates subtle differences rather than a large or obviously hormonal dimorphism.


2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Lauren Ann Metskas ◽  
Mohini Kulp ◽  
Stylianos P Scordilis

2008 ◽  
Vol 22 (5-6) ◽  
pp. 539-548 ◽  
Author(s):  
Yolanda Gómez-Pérez ◽  
Emilia Amengual-Cladera ◽  
Antoni Català-Niell ◽  
Elena Thomàs-Moyà ◽  
Magdalena Gianotti ◽  
...  

Author(s):  
D. E. Philpott ◽  
A. Takahashi

Two month, eight month and two year old rats were treated with 10 or 20 mg/kg of E. Coli endotoxin I. P. The eight month old rats proved most resistant to the endotoxin. During fixation the aorta, carotid artery, basil arartery of the brain, coronary vessels of the heart, inner surfaces of the heart chambers, heart and skeletal muscle, lung, liver, kidney, spleen, brain, retina, trachae, intestine, salivary gland, adrenal gland and gingiva were treated with ruthenium red or alcian blue to preserve the mucopolysaccharide (MPS) coating. Five, 8 and 24 hrs of endotoxin treatment produced increasingly marked capillary damage, disappearance of the MPS coating, edema, destruction of endothelial cells and damage to the basement membrane in the liver, kidney and lung.


Author(s):  
Joachim R. Sommer ◽  
Nancy R. Wallace

After Howell (1) had shown that ruthenium red treatment of fixed frog skeletal muscle caused collapse of the intermediate cisternae of the sarcoplasmic reticulum (SR), forming a pentalaminate structure by obi iterating the SR lumen, we demonstrated that the phenomenon involves the entire SR including the nuclear envelope and that it also occurs after treatment with other cations, including calcium (2,3,4).From these observations we have formulated a hypothesis which states that intracellular calcium taken up by the SR at the end of contraction causes the M rete to collapse at a certain threshold concentration as the first step in a subsequent centrifugal zippering of the free SR toward the junctional SR (JSR). This would cause a) bulk transport of SR contents, such as calcium and granular material (4) into the JSR and, b) electrical isolation of the free SR from the JSR.


Author(s):  
A. V. Somlyo ◽  
H. Shuman ◽  
A. P. Somlyo

Electron probe analysis of frozen dried cryosections of frog skeletal muscle, rabbit vascular smooth muscle and of isolated, hyperpermeab1 e rabbit cardiac myocytes has been used to determine the composition of the cytoplasm and organelles in the resting state as well as during contraction. The concentration of elements within the organelles reflects the permeabilities of the organelle membranes to the cytoplasmic ions as well as binding sites. The measurements of [Ca] in the sarcoplasmic reticulum (SR) and mitochondria at rest and during contraction, have direct bearing on their role as release and/or storage sites for Ca in situ.


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