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Conference Paper: Substrate preference of 5-nucleotidase and the pathways of AMP degradation in rat red skeletal muscle 1031

TitleSubstrate preference of 5-nucleotidase and the pathways of AMP degradation in rat red skeletal muscle 1031
Authors
Issue Date1997
PublisherLippincott Williams & Wilkins. The Journal's web site is located at http://www.acsm-msse.org
Citation
Medicine and Science in Sports and Exercise, 1997, v. 29 suppl. 5, p. 180 How to Cite?
AbstractAdenosine can be formed from cytosolic AMP by 5'-nucleotidase(AMP-ND) or extracellular AMP via the ecto-enzyme. A 5'-nucleotidase(ND) also exists in an IMP-specific form (IMP-ND), and its substrate preference has not been characterized in oxidative skeletal muscle. Also, AMP deaminase (AMPD) competes with AMP-ND by using AMP as a substrate to form IMP by deamination. Again, the pathway dominating AMP metabolism in red skeletal muscle has not been elucidated. Therefore, the purpose of the study was to investigate the substrate specificity of ND and the metabolic pathways of AMP degradation in rat soleus muscle. The membrane and cytosolic fractions of muscle tissues were separated by centrifugation. The influence of AMPD on the pathways of AMP degradation by ND was investigated by inhibiting AMPD with coformycin (CFM), and the properties of AMP-and IMP-ND were studied by comparing the kinetic parameters of the enzymes. The data show that: 1) the preference for AMP over IMP for membrane-bound ND is about 2.4-fold of that for cytosol-bound which exhibits similar selectivity for AMP and IMP, and 2) the presence of CFM increases the maximal activity of AMP-ND by approximately 25% and 236% in membrane and cytosolic fractions, respectively. These results suggest that in oxidative skeletal muscle, the membrane-bound ND has preference for AMP over IMP while the cytosol-bound doesn't and AMPD affects the formation of adenosine more significantly in membrane fractions than that in cytosolic fractions.
DescriptionAnnual Meeting Abstracts
Session: E-23 Poster - Skeletal Muscle: Metabolism
Persistent Identifierhttp://hdl.handle.net/10722/104936
ISSN
2015 Impact Factor: 4.041
2015 SCImago Journal Rankings: 2.007

 

DC FieldValueLanguage
dc.contributor.authorCheng, B-
dc.contributor.authorBallard, HJ-
dc.date.accessioned2010-09-25T22:13:34Z-
dc.date.available2010-09-25T22:13:34Z-
dc.date.issued1997-
dc.identifier.citationMedicine and Science in Sports and Exercise, 1997, v. 29 suppl. 5, p. 180-
dc.identifier.issn0195-9131-
dc.identifier.urihttp://hdl.handle.net/10722/104936-
dc.descriptionAnnual Meeting Abstracts-
dc.descriptionSession: E-23 Poster - Skeletal Muscle: Metabolism-
dc.description.abstractAdenosine can be formed from cytosolic AMP by 5'-nucleotidase(AMP-ND) or extracellular AMP via the ecto-enzyme. A 5'-nucleotidase(ND) also exists in an IMP-specific form (IMP-ND), and its substrate preference has not been characterized in oxidative skeletal muscle. Also, AMP deaminase (AMPD) competes with AMP-ND by using AMP as a substrate to form IMP by deamination. Again, the pathway dominating AMP metabolism in red skeletal muscle has not been elucidated. Therefore, the purpose of the study was to investigate the substrate specificity of ND and the metabolic pathways of AMP degradation in rat soleus muscle. The membrane and cytosolic fractions of muscle tissues were separated by centrifugation. The influence of AMPD on the pathways of AMP degradation by ND was investigated by inhibiting AMPD with coformycin (CFM), and the properties of AMP-and IMP-ND were studied by comparing the kinetic parameters of the enzymes. The data show that: 1) the preference for AMP over IMP for membrane-bound ND is about 2.4-fold of that for cytosol-bound which exhibits similar selectivity for AMP and IMP, and 2) the presence of CFM increases the maximal activity of AMP-ND by approximately 25% and 236% in membrane and cytosolic fractions, respectively. These results suggest that in oxidative skeletal muscle, the membrane-bound ND has preference for AMP over IMP while the cytosol-bound doesn't and AMPD affects the formation of adenosine more significantly in membrane fractions than that in cytosolic fractions.-
dc.languageeng-
dc.publisherLippincott Williams & Wilkins. The Journal's web site is located at http://www.acsm-msse.org-
dc.relation.ispartofMedicine and Science in Sports and Exercise-
dc.rightsThis is a non-final version of an article published in final form in (provide complete journal citation)-
dc.titleSubstrate preference of 5-nucleotidase and the pathways of AMP degradation in rat red skeletal muscle 1031-
dc.typeConference_Paper-
dc.identifier.emailBallard, HJ: ballard@hkucc.hku.hk-
dc.identifier.authorityBallard, HJ=rp00367-
dc.identifier.hkuros37014-
dc.identifier.volume29-
dc.identifier.issuesuppl. 5-
dc.identifier.spage180-
dc.identifier.epage180-
dc.publisher.placeUnited States-

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