Effect of growth promoters on pig muscle structural protein and proteolytic enzyme levels in vivo and in vitro
To elucidate the biochemical mechanism by which the growth hormone porcine somatotrophin (PST) promotes skeletal muscle growth, we have determined the activity of a comprehensive range of protein catabolizing proteolytic enzymes and structural proteins (determined by analytical electrophoresis, SDS-...
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| Veröffentlicht in: | Biochimie 1993, Vol.75 (10), p.839-847 |
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| creator | Blanchard, P. Ellis, M. Maltin, C. Falkous, G. Harris, J.B. Mantle, D. |
| description | To elucidate the biochemical mechanism by which the growth hormone porcine somatotrophin (PST) promotes skeletal muscle growth, we have determined the activity of a comprehensive range of protein catabolizing proteolytic enzymes and structural proteins (determined by analytical electrophoresis, SDS-PAGE) in longissimus dorsi muscle from control and PST treated pigs. There was no significant difference in the levels of muscle structural proteins, or in the activity of muscle proteolytic enzymes at point of slaughter in control or PST treated animals. Similarly, in
post-mortem muscle proteolysis time course experiments at pH 5.5 or pH 7.5, there was no significant difference in the rate of structural protein degradation by endogenous muscle proteases (determined
via SDS-PAGE) using muscle from control or PST treated animals. In addition, investigation of a range of β-agonist related drugs (clenbuterol, salbutamol, pirbuterol, fenoterol) showed no effect (10
−4–10
−8 M)
in vitro on the activity of individual protease types in control muscle, or on the degradation rate of muscle structural proteins by endogenous proteases in time course experiments at pH 5.5 or pH 7.5. We conclude that: i) the anabolic action of growth promoters such as PST in promoting skeletal muscle growth
in vivo does not occur
via simple down-regulation of muscle protease activities, or by alteration in the levels of individual muscle structural proteins; this is supported by the finding that β-agonist drugs do not have any direct effect on the activity of muscle proteases
in vitro; ii) PST treatment
in vivo does not significantly alter subsequent degradation of structural proteins by endogenous proteases
in vitro; similarly the latter process is unaltered in the presence of β-agonist drugs
in vitro, suggesting that the potential effect of growth promoters on subsequent meat quality does not operate
via the mechanism of
post-mortem proteolysis. |
| doi_str_mv | 10.1016/0300-9084(93)90037-S |
| format | Article |
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post-mortem muscle proteolysis time course experiments at pH 5.5 or pH 7.5, there was no significant difference in the rate of structural protein degradation by endogenous muscle proteases (determined
via SDS-PAGE) using muscle from control or PST treated animals. In addition, investigation of a range of β-agonist related drugs (clenbuterol, salbutamol, pirbuterol, fenoterol) showed no effect (10
−4–10
−8 M)
in vitro on the activity of individual protease types in control muscle, or on the degradation rate of muscle structural proteins by endogenous proteases in time course experiments at pH 5.5 or pH 7.5. We conclude that: i) the anabolic action of growth promoters such as PST in promoting skeletal muscle growth
in vivo does not occur
via simple down-regulation of muscle protease activities, or by alteration in the levels of individual muscle structural proteins; this is supported by the finding that β-agonist drugs do not have any direct effect on the activity of muscle proteases
in vitro; ii) PST treatment
in vivo does not significantly alter subsequent degradation of structural proteins by endogenous proteases
in vitro; similarly the latter process is unaltered in the presence of β-agonist drugs
in vitro, suggesting that the potential effect of growth promoters on subsequent meat quality does not operate
via the mechanism of
post-mortem proteolysis.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/0300-9084(93)90037-S</identifier><identifier>PMID: 7906148</identifier><identifier>CODEN: BICMBE</identifier><language>eng</language><publisher>Paris: Elsevier Masson SAS</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Adrenergic beta-Agonists - pharmacology ; Animals ; Biological and medical sciences ; Castration ; CERDO ; Electrophoresis, Polyacrylamide Gel ; Endopeptidases - metabolism ; ENZYMIC ACTIVITY ; Female ; Food industries ; Fundamental and applied biological sciences. Psychology ; growth hormone ; Growth Hormone - pharmacology ; Hydrogen-Ion Concentration ; In Vitro Techniques ; Male ; Meat and meat product industries ; MUSCLE ; Muscle Development ; Muscle Proteins - metabolism ; MUSCLES ; Muscles - drug effects ; MUSCULOS ; plg muscle ; PORCIN ; PROTEASAS ; PROTEASE ; PROTEASES ; PROTEINAS ; PROTEINE ; PROTEINS ; SOMATOTROPIN ; SOMATOTROPINA ; SOMATOTROPINE ; SWINE ; β-agonists</subject><ispartof>Biochimie, 1993, Vol.75 (10), p.839-847</ispartof><rights>1993</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-9b017b7d7be04afd1869f5b018c81bf0903436851fcdd81f424776da17a589413</citedby><cites>FETCH-LOGICAL-c405t-9b017b7d7be04afd1869f5b018c81bf0903436851fcdd81f424776da17a589413</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0300-9084(93)90037-S$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>309,310,314,780,784,789,790,3550,4024,4050,4051,23930,23931,25140,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4125323$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7906148$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Blanchard, P.</creatorcontrib><creatorcontrib>Ellis, M.</creatorcontrib><creatorcontrib>Maltin, C.</creatorcontrib><creatorcontrib>Falkous, G.</creatorcontrib><creatorcontrib>Harris, J.B.</creatorcontrib><creatorcontrib>Mantle, D.</creatorcontrib><title>Effect of growth promoters on pig muscle structural protein and proteolytic enzyme levels in vivo and in vitro</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>To elucidate the biochemical mechanism by which the growth hormone porcine somatotrophin (PST) promotes skeletal muscle growth, we have determined the activity of a comprehensive range of protein catabolizing proteolytic enzymes and structural proteins (determined by analytical electrophoresis, SDS-PAGE) in longissimus dorsi muscle from control and PST treated pigs. There was no significant difference in the levels of muscle structural proteins, or in the activity of muscle proteolytic enzymes at point of slaughter in control or PST treated animals. Similarly, in
post-mortem muscle proteolysis time course experiments at pH 5.5 or pH 7.5, there was no significant difference in the rate of structural protein degradation by endogenous muscle proteases (determined
via SDS-PAGE) using muscle from control or PST treated animals. In addition, investigation of a range of β-agonist related drugs (clenbuterol, salbutamol, pirbuterol, fenoterol) showed no effect (10
−4–10
−8 M)
in vitro on the activity of individual protease types in control muscle, or on the degradation rate of muscle structural proteins by endogenous proteases in time course experiments at pH 5.5 or pH 7.5. We conclude that: i) the anabolic action of growth promoters such as PST in promoting skeletal muscle growth
in vivo does not occur
via simple down-regulation of muscle protease activities, or by alteration in the levels of individual muscle structural proteins; this is supported by the finding that β-agonist drugs do not have any direct effect on the activity of muscle proteases
in vitro; ii) PST treatment
in vivo does not significantly alter subsequent degradation of structural proteins by endogenous proteases
in vitro; similarly the latter process is unaltered in the presence of β-agonist drugs
in vitro, suggesting that the potential effect of growth promoters on subsequent meat quality does not operate
via the mechanism of
post-mortem proteolysis.</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Adrenergic beta-Agonists - pharmacology</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Castration</subject><subject>CERDO</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endopeptidases - metabolism</subject><subject>ENZYMIC ACTIVITY</subject><subject>Female</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>growth hormone</subject><subject>Growth Hormone - pharmacology</subject><subject>Hydrogen-Ion Concentration</subject><subject>In Vitro Techniques</subject><subject>Male</subject><subject>Meat and meat product industries</subject><subject>MUSCLE</subject><subject>Muscle Development</subject><subject>Muscle Proteins - metabolism</subject><subject>MUSCLES</subject><subject>Muscles - drug effects</subject><subject>MUSCULOS</subject><subject>plg muscle</subject><subject>PORCIN</subject><subject>PROTEASAS</subject><subject>PROTEASE</subject><subject>PROTEASES</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>SOMATOTROPIN</subject><subject>SOMATOTROPINA</subject><subject>SOMATOTROPINE</subject><subject>SWINE</subject><subject>β-agonists</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kVGL1DAQx4Mo597pFxCFPMihD9VJk7bJiyDHnQoHgqfPIU2TNZI2a5KurJ_edLvso08Z8v_NMPwGoZcE3hEg7XugAJUAzt4I-lYA0K56eIQ2pKW8agmnj9HmjDxFlyn9AoAGanGBLjoBLWF8g6Zba43OOFi8jeFP_ol3MYwhm5hwmPDObfE4J-0NTjnOOs9R-QXJxk1YTcNaB3_ITmMz_T2MBnuzNz7hAuzdPhypY51jeIaeWOWTeX56r9CPu9vvN5-r-6-fvtx8vK80gyZXogfS9d3Q9QaYsgPhrbBN-eSak96CAMpoyxti9TBwYlnNuq4dFOlUwwUj9Apdr3PLer9nk7IcXdLGezWZMCfZtXVdc84KyFZQx5BSNFbuohtVPEgCctEsF4dycSgFlUfN8qG0vTrNn_vRDOemk9eSvz7lKmnlbVSTdumMMVI3tKYFe7FiVgWptrEgd99EA4yJJfywhkWm2TsTZdLOTNoMLpaTySG4_y_5DxIWoi0</recordid><startdate>1993</startdate><enddate>1993</enddate><creator>Blanchard, P.</creator><creator>Ellis, M.</creator><creator>Maltin, C.</creator><creator>Falkous, G.</creator><creator>Harris, J.B.</creator><creator>Mantle, D.</creator><general>Elsevier Masson SAS</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>1993</creationdate><title>Effect of growth promoters on pig muscle structural protein and proteolytic enzyme levels in vivo and in vitro</title><author>Blanchard, P. ; Ellis, M. ; Maltin, C. ; Falkous, G. ; Harris, J.B. ; Mantle, D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c405t-9b017b7d7be04afd1869f5b018c81bf0903436851fcdd81f424776da17a589413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Adrenergic beta-Agonists - pharmacology</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Castration</topic><topic>CERDO</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endopeptidases - metabolism</topic><topic>ENZYMIC ACTIVITY</topic><topic>Female</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>growth hormone</topic><topic>Growth Hormone - pharmacology</topic><topic>Hydrogen-Ion Concentration</topic><topic>In Vitro Techniques</topic><topic>Male</topic><topic>Meat and meat product industries</topic><topic>MUSCLE</topic><topic>Muscle Development</topic><topic>Muscle Proteins - metabolism</topic><topic>MUSCLES</topic><topic>Muscles - drug effects</topic><topic>MUSCULOS</topic><topic>plg muscle</topic><topic>PORCIN</topic><topic>PROTEASAS</topic><topic>PROTEASE</topic><topic>PROTEASES</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>SOMATOTROPIN</topic><topic>SOMATOTROPINA</topic><topic>SOMATOTROPINE</topic><topic>SWINE</topic><topic>β-agonists</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Blanchard, P.</creatorcontrib><creatorcontrib>Ellis, M.</creatorcontrib><creatorcontrib>Maltin, C.</creatorcontrib><creatorcontrib>Falkous, G.</creatorcontrib><creatorcontrib>Harris, J.B.</creatorcontrib><creatorcontrib>Mantle, D.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Blanchard, P.</au><au>Ellis, M.</au><au>Maltin, C.</au><au>Falkous, G.</au><au>Harris, J.B.</au><au>Mantle, D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of growth promoters on pig muscle structural protein and proteolytic enzyme levels in vivo and in vitro</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>1993</date><risdate>1993</risdate><volume>75</volume><issue>10</issue><spage>839</spage><epage>847</epage><pages>839-847</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><coden>BICMBE</coden><abstract>To elucidate the biochemical mechanism by which the growth hormone porcine somatotrophin (PST) promotes skeletal muscle growth, we have determined the activity of a comprehensive range of protein catabolizing proteolytic enzymes and structural proteins (determined by analytical electrophoresis, SDS-PAGE) in longissimus dorsi muscle from control and PST treated pigs. There was no significant difference in the levels of muscle structural proteins, or in the activity of muscle proteolytic enzymes at point of slaughter in control or PST treated animals. Similarly, in
post-mortem muscle proteolysis time course experiments at pH 5.5 or pH 7.5, there was no significant difference in the rate of structural protein degradation by endogenous muscle proteases (determined
via SDS-PAGE) using muscle from control or PST treated animals. In addition, investigation of a range of β-agonist related drugs (clenbuterol, salbutamol, pirbuterol, fenoterol) showed no effect (10
−4–10
−8 M)
in vitro on the activity of individual protease types in control muscle, or on the degradation rate of muscle structural proteins by endogenous proteases in time course experiments at pH 5.5 or pH 7.5. We conclude that: i) the anabolic action of growth promoters such as PST in promoting skeletal muscle growth
in vivo does not occur
via simple down-regulation of muscle protease activities, or by alteration in the levels of individual muscle structural proteins; this is supported by the finding that β-agonist drugs do not have any direct effect on the activity of muscle proteases
in vitro; ii) PST treatment
in vivo does not significantly alter subsequent degradation of structural proteins by endogenous proteases
in vitro; similarly the latter process is unaltered in the presence of β-agonist drugs
in vitro, suggesting that the potential effect of growth promoters on subsequent meat quality does not operate
via the mechanism of
post-mortem proteolysis.</abstract><cop>Paris</cop><pub>Elsevier Masson SAS</pub><pmid>7906148</pmid><doi>10.1016/0300-9084(93)90037-S</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0300-9084 |
| ispartof | Biochimie, 1993, Vol.75 (10), p.839-847 |
| issn | 0300-9084 1638-6183 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76222884 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Adrenergic beta-Agonists - pharmacology Animals Biological and medical sciences Castration CERDO Electrophoresis, Polyacrylamide Gel Endopeptidases - metabolism ENZYMIC ACTIVITY Female Food industries Fundamental and applied biological sciences. Psychology growth hormone Growth Hormone - pharmacology Hydrogen-Ion Concentration In Vitro Techniques Male Meat and meat product industries MUSCLE Muscle Development Muscle Proteins - metabolism MUSCLES Muscles - drug effects MUSCULOS plg muscle PORCIN PROTEASAS PROTEASE PROTEASES PROTEINAS PROTEINE PROTEINS SOMATOTROPIN SOMATOTROPINA SOMATOTROPINE SWINE β-agonists |
| title | Effect of growth promoters on pig muscle structural protein and proteolytic enzyme levels in vivo and in vitro |
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