title: Postnatal changes in contractile time parameters, calcium regulatory proteins, and phosphatases.
abstract: Compared with isolated electrically driven neonatal ventricular preparations, the total time of contraction, the time to peak tension, and the time of relaxation were decreased to approximately 50% in adult ventricular preparations. The expression of sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) was increased to 133% at the protein level and to 154% at the mRNA level in adult vs. neonatal ventricular preparations, whereas phospholamban was unchanged at both the protein and mRNA levels. Moreover, Ca2+ uptake was increased to 180% in adult vs. neonatal ventricular preparations. Phospholamban phosphorylation was enhanced in adult vs. neonatal ventricular preparations. In adult ventricular preparations, phosphatase activity was reduced to 53% of neonatal preparations, the protein levels of the immunologically detectable catalytic subunits of protein phosphatase types 1 and 2A were reduced to 28 and 61% of neonatal preparations, respectively, and the mRNA levels of type 1alpha, 1beta, 1gamma, 2Aalpha, and 2Abeta phosphatase isoforms were decreased to 69, 68, 54, 67, and 63%, respectively. We conclude that in the adult rat heart, the shortened time parameters of contraction can be explained by an elevated expression of SERCA. In addition, an increased phosphorylation state of phospholamban due to reduced phosphatase activity may be involved.
authors.affiliation: Institut fur Pharmakologie und Toxikologie, Westfalische Wilhelms-Universitat, D-48149 Munster, Germany.
authors.forename: I
authors.initials: I
authors.lastname: Gombosova
authors.forename: P
authors.initials: P
authors.lastname: Boknik
authors.forename: U
authors.initials: U
authors.lastname: Kirchhefer
authors.forename: J
authors.initials: J
authors.lastname: Knapp
authors.forename: H
authors.initials: H
authors.lastname: Luss
authors.forename: F U
authors.initials: FU
authors.lastname: Muller
authors.forename: T
authors.initials: T
authors.lastname: Muller
authors.forename: U
authors.initials: U
authors.lastname: Vahlensieck
authors.forename: W
authors.initials: W
authors.lastname: Schmitz
authors.forename: G S
authors.initials: GS
authors.lastname: Bodor
authors.forename: J
authors.initials: J
authors.lastname: Neumann
mesh_terms: D000199:Actins / Q000378:metabolism; D000367:Age Factors; D000818:Animals; D000831:Animals, Newborn; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002155:Calsequestrin / Q000378:metabolism; D003971:Diastole; D009200:Myocardial Contraction / Q000502:physiology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010766:Phosphorylation; D012333:RNA, Messenger / Q000302:isolation & purification; D051381:Rats; D017207:Rats, Sprague-Dawley; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*; D013599:Systole; D014336:Troponin / Q000378:metabolism; D016276:Ventricular Function; D000099211:Phospholamban
chemical_list: D000199:Actins; D002118:Calcium; D002135:Calcium-Binding Proteins; D000252:Calcium-Transporting ATPases; D002155:Calsequestrin; D010744:Phosphoric Monoester Hydrolases; D012333:RNA, Messenger; D014336:Troponin; D000099211:Phospholamban