scholarly journals The effects of hibernation on the contractile and biochemical properties of skeletal muscles in the thirteen-lined ground squirrel, Ictidomys tridecemlineatus

2013 ◽  
Vol 216 (14) ◽  
pp. 2587-2594 ◽  
Author(s):  
R. S. James ◽  
J. F. Staples ◽  
J. C. L. Brown ◽  
S. N. Tessier ◽  
K. B. Storey
Keyword(s):  
Ground Squirrel ◽  
Skeletal Muscles ◽  
Biochemical Properties ◽  
Ictidomys Tridecemlineatus

Characterisation of a novel UV filter in the lens of the thirteen-lined ground squirrel (Ictidomys tridecemlineatus)

2014 ◽  
Vol 121 ◽  
pp. 114-120 ◽  
Author(s):  
Brian Lyons ◽  
Peter Karuso ◽  
Joanne F. Jamie ◽  
Mukoma F. Simpanya ◽  
Frank Giblin ◽  
...  
Keyword(s):  
Ground Squirrel ◽  
Uv Filter ◽  
Ictidomys Tridecemlineatus

The harp seal, Pagophilus groenlandicus (Erxleben, 1777). VII. A histophysiological study of certain skeletal muscles

1971 ◽  
Vol 49 (1) ◽  
pp. 25-30 ◽  
Author(s):  
J. C. George ◽  
N. V. Vallyathan ◽  
K. Ronald
Keyword(s):  
Skeletal Muscles ◽  
Biochemical Properties ◽  
Histochemical Demonstration ◽  
Harp Seal ◽  
Activity Levels ◽  
Sodium Pentobarbital ◽  
Pagophilus Groenlandicus

A quantitative and histochemical study of Ms. pectoralis, gluteus, psoas, diaphragma (dorsal, lateral, and ventral parts separately) of the harp seal was carried out. Myoglobin and iron contents of all the muscles were high, highest being of M. psoas. Fat and glycogen were low in all muscles. The low glycogen value was possibly due to rapid glycolysis during struggle in capture and while the animal was under an overdose of sodium pentobarbital that was administered for killing it. Phosphorylase and succinate dehydrogenase (SDH) activity levels were also low. Lipase (tributyrinase) activity was high, that of M. diaphragma being higher than the other muscles studied. The histochemical investigation revealed some of the morphological and biochemical properties of the component fibers. Two types of fiber, the red (type 1) and white (type 2), comparable to those of other skeletal muscles were distinguished in all muscles except in the case of M. pectoralis where an intermediate type was also seen in sections treated for the histochemical demonstration of SDH activity.The low levels of fat and SDH in the muscles indicate that fat is not a favored metabolite for muscular energy. The significance of the high lipase (tributyrinase) activity is doubtful. It is suggested that the role of this enzyme is to clear the fat so as to prevent the accumulation of fat in the muscles which are, by and large, geared for a glycolytic metabolism as an adaptation for the animal's diving habit. The high myoglobin content of the muscles, however, should provide the oxygen necessary for the oxidation of glucose during the initial part of the dive.

scholarly journals Ca-ATPase Activity and Protein Composition of Sarcoplasmic Reticulum Membranes Isolated from Skeletal Muscles of Typical Hibernator, the Ground Squirrel Spermophilus undulatus

2001 ◽  
Vol 21 (6) ◽  
pp. 831-838 ◽  
Author(s):  
Anna N. Malysheva ◽  
Kenneth B. Storey ◽  
Olga D. Lopina ◽  
Alexander M. Rubstov
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Electrophoretic Mobility ◽  
Ground Squirrel ◽  
Skeletal Muscles ◽  
Binding Proteins ◽  
Protein Composition ◽  
Ground Squirrels ◽  
Ground Squirrel Spermophilus Undulatus ◽  
Spermophilus Undulatus

Ca-ATPase activity in sarcoplasmic reticulum (SR) membranes isolated from skeletal muscles of the typical hibernator, the ground squirrel Spermophilus undulatus, is about 2-fold lower than that in SR membranes of rats and rabbits and is further decreased 2-fold during hibernation. The use of carbocyanine anionic dye Stains-All has revealed that Ca-binding proteins of SR membranes, histidine-rich Ca-binding protein and sarcalumenin, in ground squirrel, rat, and rabbit SR have different electrophoretic mobility corresponding to apparent molecular masses 165, 155, and 170 kDa and 130, 145, and 160 kDa, respectively; the electrophoretic mobility of calsequestrin (63 kDa) is the same in all preparations. The content of these Ca-binding proteins in SR membranes of the ground squirrels is decreased 3–4 fold and the content of 55, 30, and 22 kDa proteins is significantly increased during hibernation.

The conversion of some biochemical properties of mammalian skeletal muscles following cross-reinnervation

1977 ◽  
Vol 55 (3) ◽  
pp. 637-653 ◽  
Author(s):  
W.F.H.M. Mommaerts ◽  
K. Seraydarian ◽  
Miwon Suh ◽  
C.J.C. Kean ◽  
A.J. Buller
Keyword(s):  
Skeletal Muscles ◽  
Biochemical Properties

scholarly journals Comparison of different skeletal muscles from growing domestic pigs and wild boars

2013 ◽  
Vol 56 (1) ◽  
pp. 766-777 ◽  
Author(s):  
D. Lösel ◽  
A. Franke ◽  
C. Kalbe
Keyword(s):  
Skeletal Muscles ◽  
Muscle Growth ◽  
Biochemical Properties ◽  
Cross Sectional Area ◽  
Sectional Area ◽  
Cross Sectional ◽  
Wild Boars ◽  
Domestic Pigs ◽  
Psoas Major ◽  
Fast Twitch

Abstract. The domestication process of pigs was associated with substantial morphological and physiological changes. The aim of this study was to comparatively investigate muscle microstructure and biochemical properties of four different skeletal muscles (M. longissimus, M. semitendinosus, M. psoas major, M. rhomboideus) in growing domestic pigs (n=5) and wild boars (n=4). The superiority of domestic pigs in body and muscle growth at three months of age was reflected by a 4-fold body weight and higher absolute weights of heart, liver and muscles. Relative muscle weights of M. psoas major and M. rhomboideus were reduced, whereas a 1.6-fold heavier M. semitendinosus was observed in domestic pigs compared with wild boars. In addition, the muscle cross-sectional area was greater in all muscles of domestic pigs resulting from about 3-fold fibre cross-sectional area, whereas total fibre number remained unchanged. As a consequence of intensified fibre hypertrophy, the fibre area per capillary is higher in all muscles of domestic pigs. Thus, the impaired supply with oxygen and nutrients may be one reason for the shift to the glycolytic muscle metabolism as indicated by a greater proportion of fast-twitch glycolytic fibres at the expense of fast-twitch oxidative fibres. This is also reflected by a higher ratio of lactate dehydrogenase to isocitrate dehydrogenase activity. Our data suggest that the intensified muscle growth was realized by myofibre hypertrophy at unchanged myofibre number in growing domestic pigs. It seems that domestication-induced changes were most pronounced in M. semitendinosus as the exterior ham muscle which may be related to muscle specific selection for lean growth.

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