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...
Saved in:
Published in | American journal of physiology. Regulatory, integrative and comparative physiology Vol. 290; no. 6; pp. R1720 - R1727 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
01.06.2006
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
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 |
Author_xml | – sequence: 1 fullname: Polasek, L. K – sequence: 2 fullname: Dickson, K. A – sequence: 3 fullname: Davis, R. W |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16397095$$D View this record in MEDLINE/PubMed |
BookMark | eNp1kM1O3DAURi1EVYZpX4BF5VVVFple_ySOu0MIaCVQEaJry3GciaknTu2kMG-P6QxqN135yvc7n67OMTocwmAROiGwIqSkn_XDGO16XgFADSsKUB6gRV7QgnAJh2gBrGJFRYg8QscpPeQcZ5y9RUekYlKALBfo5sZOugneGeyG1hk9hZjyiKfe4vTT-rz2eDMn423CocO9jk2IOFntE_502wej8W83zd4N-vQdetPlf_t-_y7Rj8uL-_OvxfX3q2_nZ9eFYZJMhRC0Eky3VdO2FGi-nAEHIhrSGcagtjVIQlpeam5LKupS8JK1ddfVRJpSa7ZEH3e9Ywy_ZpsmtXHJWO_1YMOcVCUkr3mGlojugiaGlKLt1BjdRsetIqBeJKq9RPVHonqRmKEP-_a52dj2L7K3lgNfdoHerftHF60a-21ywYf1Vl3O3t_bp-m1mUpQlbojgoIa2y7Dq__Dr9f8A7FnUSGVQQ |
CitedBy_id | crossref_primary_10_1093_conphys_cov019 crossref_primary_10_1016_j_cbpa_2012_10_010 crossref_primary_10_1038_s41467_022_31863_7 crossref_primary_10_3389_fphys_2014_00217 crossref_primary_10_3389_fmars_2023_1232305 crossref_primary_10_1242_jeb_037929 crossref_primary_10_1002_jmor_20124 crossref_primary_10_1242_jeb_018119 crossref_primary_10_3390_ani11020451 crossref_primary_10_1007_s00360_011_0619_6 crossref_primary_10_1071_ZO11072 crossref_primary_10_1007_s00360_006_0111_x crossref_primary_10_1242_jeb_177758 crossref_primary_10_1007_s00360_015_0922_8 crossref_primary_10_1016_j_tvjl_2015_11_019 |
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 |
ContentType | Journal Article |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 |
DOI | 10.1152/ajpregu.00080.2005 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
DatabaseTitleList | CrossRef MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Anatomy & Physiology |
EISSN | 1522-1490 |
EndPage | R1727 |
ExternalDocumentID | 10_1152_ajpregu_00080_2005 16397095 ajpregu_290_6_R1720 |
Genre | Research Support, Non-U.S. Gov't Journal Article Comparative Study |
GroupedDBID | 02 23M 2WC 39C 4.4 5GY 5VS ACIWK ACPRK ADBBV AFFNX AFRAH ALMA_UNASSIGNED_HOLDINGS BAWUL BKOMP C1A DIK DL EBS EJD F5P H13 KQ8 O0- OK1 P2P PQEST PQQKQ RAP RHF RHI RPL UKR WH7 WOQ 53G 6J9 8M5 AAFWJ BKKCC BTFSW CGR CUY CVF ECM EIF EMOBN ITBOX NPM RPRKH TAE TR2 W8F XSW YSK YYP ~02 AAYXX CITATION 7X8 |
ID | FETCH-LOGICAL-c391t-772673ad6bdd202200304017b1fc3308e80911d45a4e527857453d8ff819c5aa3 |
ISSN | 0363-6119 |
IngestDate | Fri Oct 25 03:27:26 EDT 2024 Fri Aug 23 04:01:30 EDT 2024 Sat Sep 28 07:52:49 EDT 2024 Tue Jan 05 17:52:13 EST 2021 Mon May 06 11:49:45 EDT 2019 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 6 |
Language | English |
LinkModel | OpenURL |
MergedId | FETCHMERGED-LOGICAL-c391t-772673ad6bdd202200304017b1fc3308e80911d45a4e527857453d8ff819c5aa3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
PMID | 16397095 |
PQID | 67948445 |
PQPubID | 23479 |
ParticipantIDs | crossref_primary_10_1152_ajpregu_00080_2005 proquest_miscellaneous_67948445 pubmed_primary_16397095 highwire_physiology_ajpregu_290_6_R1720 |
PublicationCentury | 2000 |
PublicationDate | 20060601 2006-Jun 2006-06-00 |
PublicationDateYYYYMMDD | 2006-06-01 |
PublicationDate_xml | – month: 06 year: 2006 text: 20060601 day: 01 |
PublicationDecade | 2000 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | American journal of physiology. Regulatory, integrative and comparative physiology |
PublicationTitleAlternate | Am J Physiol Regul Integr Comp Physiol |
PublicationYear | 2006 |
References | R21 R20 R23 R22 R25 R24 R27 R26 R29 R28 R1 R2 R3 R4 R6 R7 R8 R9 R30 R10 R32 R31 R12 R34 R11 R33 R14 R36 R13 R35 R16 R15 R37 R18 R17 R19 |
References_xml | – ident: R3 doi: 10.1086/physzool.54.2.30155826 – ident: R12 doi: 10.1152/jappl.1995.79.4.1148 – ident: R30 doi: 10.1152/jappl.1996.81.4.1762 – ident: R22 doi: 10.1111/j.1469-7998.1993.tb02679.x – ident: R35 doi: 10.1242/jeb.00652 – ident: R4 doi: 10.1007/BF00571260 – ident: R6 doi: 10.1242/jeb.202.9.1091 – ident: R24 doi: 10.1242/jeb.204.2.209 – ident: R7 doi: 10.1242/jeb.185.1.179 – ident: R23 – ident: R18 doi: 10.1152/ajpregu.1980.239.5.R437 – ident: R1 doi: 10.1016/S0305-0491(98)00025-X – ident: R11 doi: 10.1111/j.1475-097X.1982.tb00001.x – ident: R27 doi: 10.1242/jeb.194.1.33 – ident: R31 doi: 10.1126/science.90.2334.276 – ident: R34 doi: 10.1093/jn/131.11.2967 – ident: R15 doi: 10.1111/j.1748-1716.1977.tb05956.x – ident: R10 doi: 10.1152/jappl.1972.33.3.312 – ident: R14 – ident: R2 doi: 10.1152/physrev.1997.77.3.837 – ident: R21 doi: 10.1016/0034-5687(81)90079-7 – ident: R37 doi: 10.1146/annurev.ph.51.030189.004233 – ident: R25 doi: 10.1016/0305-0491(78)90187-6 – ident: R29 – ident: R20 doi: 10.1007/BF00309665 – ident: R8 doi: 10.1242/jeb.137.1.157 – ident: R13 doi: 10.1139/z93-294 – ident: R9 doi: 10.1242/jeb.00654 – ident: R16 doi: 10.1152/jappl.1999.86.4.1247 – ident: R28 doi: 10.1152/jappl.1962.17.2.301 – ident: R33 doi: 10.1016/0034-5687(81)90075-X – ident: R32 – ident: R26 doi: 10.1152/jappl.1981.50.5.999 – ident: R36 – ident: R17 – ident: R19 doi: 10.1007/BF00689915 |
SSID | ssj0004343 |
Score | 1.9906442 |
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... |
SourceID | proquest crossref pubmed highwire |
SourceType | Aggregation Database Index Database Enrichment Source Publisher |
StartPage | R1720 |
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) |
URI | http://ajpregu.physiology.org/cgi/content/abstract/290/6/R1720 https://www.ncbi.nlm.nih.gov/pubmed/16397095 https://search.proquest.com/docview/67948445 |
Volume | 290 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFLbKeOEFDcaljIsfEBdVzZI4TtLHiYsmUNGYOmlvlmM7oqCmVZsiwb_iH3KOYycZK9LgJUqjJnX8fT0-5_hcCHmuVZYmOgIEZJGOE1ma8cTkehxzLHaTlorb7g3TT-nJefLhgl8MBr96UUvbugjUz515Jf-DKlwDXDFL9h-QbR8KF-Ac8IUjIAzHa2E8NTVgiGWqcedZSds5xwUubr7BgoKZjovtBiPfrFYo1wD5CGO-rLP19AusZKPv8xrD0aV3CviatH4vp1dcwvpBrCM-AGBsF_tlsw_vy05gIJJLlWurind3tYIYDOqNaVq4B52n9e28Tfj_GHRe1rYSwlnQxAP23RQ-nKpNz2Jgpzr5aJy0BUsYTLSwL45j93F-RbiegbIV7hb7HMvIyq-rNbx6YNVg6y7rfxmgWy0sESLczAyb3p6XK3D_sTK28YruyQLGJlJhx3GD3IyxtiDGAXzuFahnTaCmf1ufp8Xjo6vDw4q1biyX1SJfqvrvZo9Vf2b75LazW-hxQ8I7ZGCqu-TguAICLH7QF_S0xfiATFte0o6XcEqBl9Tzkjpe0mVJG15Sy0v6yrKSela-vkfO37-bvTkZu7YdY8UmUY32WpoxqdNC6xgTuXH3HQR_EZWKsTA3OeiokU64TAyPs5xnCWc6L0tQThWXkt0ne9WyMg8JVRymOIoUOiZAohSTTGpWFFLlYQGGbjYkIz9rYtVUZxHWquWx8JjZ6cZuq3xImJ9Y0TFfoK9nBnj7O3ogi5Uuh-Tlrrt2UGJInnm0BAhp3HmTlVluNyKFVS9PEhjBgwbEbrQO_0fX_pVDcqv7fz0me_V6a56AYlwXTy0VfwPFPrk9 |
link.rule.ids | 315,783,787,27937,27938 |
linkProvider | Colorado Alliance of Research Libraries |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Metabolic+indicators+in+the+skeletal+muscles+of+harbor+seals+%28Phoca+vitulina%29&rft.jtitle=American+journal+of+physiology.+Regulatory%2C+integrative+and+comparative+physiology&rft.au=Polasek%2C+L.+K&rft.au=Dickson%2C+K.+A&rft.au=Davis%2C+R.+W&rft.date=2006-06-01&rft.issn=0363-6119&rft.eissn=1522-1490&rft.volume=290&rft.issue=6&rft.spage=R1720&rft_id=info:doi/10.1152%2Fajpregu.00080.2005&rft_id=info%3Apmid%2F16397095&rft.externalDBID=n%2Fa&rft.externalDocID=ajpregu_290_6_R1720 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0363-6119&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0363-6119&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0363-6119&client=summon |