Metabolic indicators in the skeletal muscles of harbor seals (Phoca vitulina)

1 Department of Marine Biology, Texas A&M University at Galveston, Galveston, Texas; and 2 Department of Biological Science, California State University Fullerton, Fullerton, California Submitted 4 February 2005 ; accepted in final form 4 January 2006 The goal of this study was to determine the...

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Published inAmerican journal of physiology. Regulatory, integrative and comparative physiology Vol. 290; no. 6; pp. R1720 - R1727
Main Authors Polasek, L. K, Dickson, K. A, Davis, R. W
Format Journal Article
LanguageEnglish
Published United States 01.06.2006
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Abstract 1 Department of Marine Biology, Texas A&M University at Galveston, Galveston, Texas; and 2 Department of Biological Science, California State University Fullerton, Fullerton, California Submitted 4 February 2005 ; accepted in final form 4 January 2006 The goal of this study was to determine the distribution of citrate synthase (CS), -hydroxyacyl coenzyme A dehydrogenase (HOAD), and lactate dehydrogenase (LDH) activities and myoglobin (Mb) concentration in the locomotor muscles (epaxial muscles) and heart of harbor seals. The entire epaxial musculature, which produces most of the power for submerged swimming, was removed and weighed, and three transverse sections (cranial, middle, and caudal) were taken along the muscle bundle. Multiple samples were taken along points on a circular grid using a 6-mm biopsy. A single sample was taken from the left ventricle of the heart. Muscle groups of similar function were taken from three dogs as a control. Mean values were calculated for four roughly equal quadrants in each transverse section of the epaxial muscles. There were no significant differences among the quadrants within any of the transverse sections for the three enzymes or Mb. However, there were significant differences in the mean enzyme activities and Mb concentrations along the length of the muscle. The middle and caudal sections had significantly higher mean levels of CS, LDH, and Mb than the cranial section, which may be correlated with power production during swimming. The enzyme ratios CS/HOAD and LDH/CS exhibited no variation within transverse sections or along the length of the epaxial muscles. Relative to the dog, the epaxial muscles and heart of the harbor seal had higher HOAD levels and lower CS/HOAD, which, taken together, indicate an increased capacity for aerobic lipid metabolism during diving. biochemistry; citrate synthase; lactate dehydrogenase; myoglobin; -hydroxyacyl coenzyme A dehydrogenase Address for reprint requests and other correspondence: L. Polasek, Alaska SeaLife Center, P.O. Box 1329, Seward, AK 99664 (e-mail: lori_polasek{at}alaskasealife.org )
AbstractList The goal of this study was to determine the distribution of citrate synthase (CS), β-hydroxyacyl coenzyme A dehydrogenase (HOAD), and lactate dehydrogenase (LDH) activities and myoglobin (Mb) concentration in the locomotor muscles (epaxial muscles) and heart of harbor seals. The entire epaxial musculature, which produces most of the power for submerged swimming, was removed and weighed, and three transverse sections (cranial, middle, and caudal) were taken along the muscle bundle. Multiple samples were taken along points on a circular grid using a 6-mm biopsy. A single sample was taken from the left ventricle of the heart. Muscle groups of similar function were taken from three dogs as a control. Mean values were calculated for four roughly equal quadrants in each transverse section of the epaxial muscles. There were no significant differences among the quadrants within any of the transverse sections for the three enzymes or Mb. However, there were significant differences in the mean enzyme activities and Mb concentrations along the length of the muscle. The middle and caudal sections had significantly higher mean levels of CS, LDH, and Mb than the cranial section, which may be correlated with power production during swimming. The enzyme ratios CS/HOAD and LDH/CS exhibited no variation within transverse sections or along the length of the epaxial muscles. Relative to the dog, the epaxial muscles and heart of the harbor seal had higher HOAD levels and lower CS/HOAD, which, taken together, indicate an increased capacity for aerobic lipid metabolism during diving.
1 Department of Marine Biology, Texas A&M University at Galveston, Galveston, Texas; and 2 Department of Biological Science, California State University Fullerton, Fullerton, California Submitted 4 February 2005 ; accepted in final form 4 January 2006 The goal of this study was to determine the distribution of citrate synthase (CS), -hydroxyacyl coenzyme A dehydrogenase (HOAD), and lactate dehydrogenase (LDH) activities and myoglobin (Mb) concentration in the locomotor muscles (epaxial muscles) and heart of harbor seals. The entire epaxial musculature, which produces most of the power for submerged swimming, was removed and weighed, and three transverse sections (cranial, middle, and caudal) were taken along the muscle bundle. Multiple samples were taken along points on a circular grid using a 6-mm biopsy. A single sample was taken from the left ventricle of the heart. Muscle groups of similar function were taken from three dogs as a control. Mean values were calculated for four roughly equal quadrants in each transverse section of the epaxial muscles. There were no significant differences among the quadrants within any of the transverse sections for the three enzymes or Mb. However, there were significant differences in the mean enzyme activities and Mb concentrations along the length of the muscle. The middle and caudal sections had significantly higher mean levels of CS, LDH, and Mb than the cranial section, which may be correlated with power production during swimming. The enzyme ratios CS/HOAD and LDH/CS exhibited no variation within transverse sections or along the length of the epaxial muscles. Relative to the dog, the epaxial muscles and heart of the harbor seal had higher HOAD levels and lower CS/HOAD, which, taken together, indicate an increased capacity for aerobic lipid metabolism during diving. biochemistry; citrate synthase; lactate dehydrogenase; myoglobin; -hydroxyacyl coenzyme A dehydrogenase Address for reprint requests and other correspondence: L. Polasek, Alaska SeaLife Center, P.O. Box 1329, Seward, AK 99664 (e-mail: lori_polasek{at}alaskasealife.org )
The goal of this study was to determine the distribution of citrate synthase (CS), beta-hydroxyacyl coenzyme A dehydrogenase (HOAD), and lactate dehydrogenase (LDH) activities and myoglobin (Mb) concentration in the locomotor muscles (epaxial muscles) and heart of harbor seals. The entire epaxial musculature, which produces most of the power for submerged swimming, was removed and weighed, and three transverse sections (cranial, middle, and caudal) were taken along the muscle bundle. Multiple samples were taken along points on a circular grid using a 6-mm biopsy. A single sample was taken from the left ventricle of the heart. Muscle groups of similar function were taken from three dogs as a control. Mean values were calculated for four roughly equal quadrants in each transverse section of the epaxial muscles. There were no significant differences among the quadrants within any of the transverse sections for the three enzymes or Mb. However, there were significant differences in the mean enzyme activities and Mb concentrations along the length of the muscle. The middle and caudal sections had significantly higher mean levels of CS, LDH, and Mb than the cranial section, which may be correlated with power production during swimming. The enzyme ratios CS/HOAD and LDH/CS exhibited no variation within transverse sections or along the length of the epaxial muscles. Relative to the dog, the epaxial muscles and heart of the harbor seal had higher HOAD levels and lower CS/HOAD, which, taken together, indicate an increased capacity for aerobic lipid metabolism during diving.
Author Polasek, L. K
Davis, R. W
Dickson, K. A
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Cites_doi 10.1086/physzool.54.2.30155826
10.1152/jappl.1995.79.4.1148
10.1152/jappl.1996.81.4.1762
10.1111/j.1469-7998.1993.tb02679.x
10.1242/jeb.00652
10.1007/BF00571260
10.1242/jeb.202.9.1091
10.1242/jeb.204.2.209
10.1242/jeb.185.1.179
10.1152/ajpregu.1980.239.5.R437
10.1016/S0305-0491(98)00025-X
10.1111/j.1475-097X.1982.tb00001.x
10.1242/jeb.194.1.33
10.1126/science.90.2334.276
10.1093/jn/131.11.2967
10.1111/j.1748-1716.1977.tb05956.x
10.1152/jappl.1972.33.3.312
10.1152/physrev.1997.77.3.837
10.1016/0034-5687(81)90079-7
10.1146/annurev.ph.51.030189.004233
10.1016/0305-0491(78)90187-6
10.1007/BF00309665
10.1242/jeb.137.1.157
10.1139/z93-294
10.1242/jeb.00654
10.1152/jappl.1999.86.4.1247
10.1152/jappl.1962.17.2.301
10.1016/0034-5687(81)90075-X
10.1152/jappl.1981.50.5.999
10.1007/BF00689915
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Snippet 1 Department of Marine Biology, Texas A&M University at Galveston, Galveston, Texas; and 2 Department of Biological Science, California State University...
The goal of this study was to determine the distribution of citrate synthase (CS), beta-hydroxyacyl coenzyme A dehydrogenase (HOAD), and lactate dehydrogenase...
The goal of this study was to determine the distribution of citrate synthase (CS), β-hydroxyacyl coenzyme A dehydrogenase (HOAD), and lactate dehydrogenase...
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SubjectTerms 3-Hydroxyacyl CoA Dehydrogenases - metabolism
Animals
Biomarkers - metabolism
Citrate (si)-Synthase - metabolism
Dogs
Energy Metabolism - physiology
Female
Heart Ventricles - chemistry
Heart Ventricles - enzymology
Heart Ventricles - metabolism
Lactate Dehydrogenases - metabolism
Male
Muscle, Skeletal - chemistry
Muscle, Skeletal - enzymology
Muscle, Skeletal - metabolism
Myoglobin - analysis
Phoca - metabolism
Rats
Title Metabolic indicators in the skeletal muscles of harbor seals (Phoca vitulina)
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