Role of different proteolytic pathways in degradation of muscle protein from streptozotocin-diabetic rats

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorPepato, Maria Teresa
dc.creatorMigliorini, Renato H.
dc.creatorGoldberg, Alfred L.
dc.creatorKettelhut, Isis C.
dc.date2014-05-27T11:18:06Z
dc.date2016-10-25T18:13:55Z
dc.date2014-05-27T11:18:06Z
dc.date2016-10-25T18:13:55Z
dc.date1996-08-01
dc.date.accessioned2017-04-06T00:47:33Z
dc.date.available2017-04-06T00:47:33Z
dc.identifierAmerican Journal of Physiology - Endocrinology and Metabolism, v. 271, n. 2 34-2, 1996.
dc.identifier0193-1849
dc.identifierhttp://hdl.handle.net/11449/64817
dc.identifierhttp://acervodigital.unesp.br/handle/11449/64817
dc.identifier2-s2.0-0029741353
dc.identifierhttp://ajpendo.physiology.org/content/271/2/E340
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/886603
dc.descriptionIn vitro rates of overall proteolysis and the activities of four different proteolytic pathways (lysosomal, Ca2+ dependent, ATP dependent, and ATP independent), as well as rates of protein synthesis, were measured in soleus and extensor digitorum longus (EDL) muscles from streptozotocin- diabetic rats. In the acute phase (1-3 days) of diabetes, there was an increase in overall proteolysis that coincided with an increased activity of the Ca2+-dependent pathway in both soleus and EDL and of the ATP-dependent pathway in EDL. After longer periods (5-10 days) of diabetes, the overall rate of protein degradation decreased and reached values similar to or even lower than those of controls as a result of a reduction in the activities of Ca2+-dependent and ATP-dependent pathways. No change was detected at any time interval in the activity of the intralysosomal proteolytic system in muscles from diabetic animals. Rates of protein synthesis were already reduced 24 h after diabetes induction and decreased further thereafter. Insulin treatment restored to normal the activities of the proteolytic pathways and rates of protein synthesis.
dc.languageeng
dc.relationAmerican Journal of Physiology: Endocrinology and Metabolism
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectadenosine triphosphate-dependent proteolysis
dc.subjectcalcium-dependent proteolysis
dc.subjectlysosomal proteolysis
dc.subjectprotein synthesis
dc.subjectadenosine triphosphate
dc.subjectcalcium ion
dc.subjectcalpain
dc.subjectcycloheximide
dc.subjectfatty acid
dc.subjectinsulin
dc.subjectlysosome enzyme
dc.subjectmuscle protein
dc.subjectphenylalanine
dc.subjectanimal model
dc.subjectanimal tissue
dc.subjectbody weight
dc.subjectcontrolled study
dc.subjectenzyme activity
dc.subjectextensor digitorum longus muscle
dc.subjectfatty acid blood level
dc.subjectglucose blood level
dc.subjectinsulin treatment
dc.subjectmale
dc.subjectmuscle mass
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectprotein degradation
dc.subjectrat
dc.subjectsoleus muscle
dc.subjectstreptozocin diabetes
dc.subjectAdenosine Triphosphate
dc.subjectAnimals
dc.subjectBlood Glucose
dc.subjectBody Weight
dc.subjectCalcium
dc.subjectDiabetes Mellitus, Experimental
dc.subjectFatty Acids, Nonesterified
dc.subjectInsulin
dc.subjectLysosomes
dc.subjectMale
dc.subjectMuscle Proteins
dc.subjectMuscles
dc.subjectOrgan Size
dc.subjectPeptide Hydrolases
dc.subjectRats
dc.subjectRats, Wistar
dc.titleRole of different proteolytic pathways in degradation of muscle protein from streptozotocin-diabetic rats
dc.typeOtro


Este ítem pertenece a la siguiente institución