Re-Expression of Fetal Troponin Isoforms in the Postinfarction Failing Heart of the Rat.

Kim, Sang-Hyun; Kim, Hyo–Soo; Lee, Hae Young

doi:10.1253/circj.66.959

Cited by 18 publications

(22 citation statements)

References 31 publications

(39 reference statements)

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“…All protein identifications were confirmed by comparing our data with an existing 2-D gel database for the rat heart (http://www.mpiib-berlin.mpg.de/ 2D-PAGE/RAT-HEART/2d/2d.html) and our previous 2-D gel analysis of canine hearts (38). 16 1. Two-dimensional (2-D) gel analysis of neonatal and adult rat myofilament proteins.…”

Section: Methodssupporting

confidence: 59%

“…17). Moreover, reexpression of fetal and neonatal proteins in disorders of the adult heart (16) makes it important to fully understand the developmental transitions in the structure and function of regulatory proteins of the sarcomere. Developmental modifications in sarcomere proteins are also relevant to the therapeutic use of stem cells.…”

mentioning

confidence: 99%

“…These approaches include relative protein quantification with two-dimensional (2-D) difference gel electrophoresis (2D-DIGE) (24,32) and relative peptide quantification with 16 O/ 18 O labeling (28). We used titanium dioxide (TiO 2 ) (18,25) to enrich phosphopeptides from in gel digestion.…”

mentioning

confidence: 99%

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Quantitative comparison of sarcomeric phosphoproteomes of neonatal and adult rat hearts

Yuan¹,

Sheng²,

Tang³

et al. 2008

American Journal of Physiology-Heart and Circulatory Physiology

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Neonatal hearts respond to stress and function in an environment quite different from adult hearts. There is evidence that these functional differences not only reflect modifications in the abundance and isoforms of sarcomeric proteins but also in the modulation of sarcomeric protein phosphorylation. Yet our understanding of changes in sarcomeric protein phosphorylation in development is incomplete. In the experiments reported here, we first quantified the intact sarcomeric protein phosphorylation status between neonatal and adult rat hearts by employing comparative two-dimensional (2-D) gel electrophoresis in conjunction with phosphoprotein-specific staining. Subsequently, we measured phosphorylation changes at the peptide level by employing high-resolution linear ion trap-Fourier transform (LTQ-FT) mass spectrometry analysis of titanium dioxide-enriched phosphopeptides differentially labeled with (16)O/(18)O during in-gel digestion. We also employed Western blot analysis using phosphorylation site-specific antibodies to measure phosphorylation changes. Our data demonstrated the novel finding that phosphorylation levels of myosin-binding protein C (MyBP-C) at Ser(295) and Ser(315) as well as tropomyosin at Ser(283) increased, whereas phosphorylation levels of MyBP-C at Ser(320) and myosin light chain 2 at Ser(15) decreased in neonatal hearts compared with the same sites in adult hearts. Although our data highlight the significant challenges in understanding relations between protein phosphorylation and cardiac function, they do support the hypothesis that developmental changes in the modulation of protein are functionally significant and correlate with the prevailing physiological state.

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Section: Methodssupporting

confidence: 59%

mentioning

confidence: 99%

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Quantitative comparison of sarcomeric phosphoproteomes of neonatal and adult rat hearts

Yuan¹,

Sheng²,

Tang³

et al. 2008

American Journal of Physiology-Heart and Circulatory Physiology

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“…AmpliWcation of the resulting cDNA was performed with speciWc primers (MWG Biotech). Primers for TnT isoforms are described by Kim et al (2002), while primes for MHC isoforms are described by Danzi et al (2005). Four microliters of the reverse transcriptase product was incubated in 50 l volume with 1£ reaction buVer, 0.2 nM dNTP´s, 2 pmol speciWc forward and reverse primers for the speciWc isoform amd 50 U of Taq DNA polymerase.…”

Section: Immunoblottingmentioning

confidence: 99%

Altered tension cost in (TG(mREN-2)27) rats overexpressing the mouse renin gene

et al. 2006

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The present study aimed to characterize cardiac hypertrophy induced by activation of the renin-angiotensin system in terms of functional alterations on the level of the contractile proteins, employing transgenic rats harboring the mouse renin gene (TGR(mREN2)27). Ca2+-dependent tension and myosin ATPase activity were measured in skinned fiber preparations obtained from TGR(mREN2)27 and from age-matched Sprague-Dawley rats (SPDR). Western blots for troponin I (TnI) and troponin T (TnT) were performed and the phosphorylation status of TnI were evaluated in myocardial preparations. TnT and myosin heavy chain (MHC) isoforms were analyzed by RT-PCR. The pCa/tension relationship was shifted to the right in TGR(mREN2)27 compared to SPDR as indicated by increased Ca2+-concentrations required for half maximal activation of tension (SPDR 5.80, 95% confidence limits 5.77-5.82 vs. TGR(mREN2)27 5.69, 95% confidence limits 5.67-5.72, pCa units), while maximal developed tension was unaltered. Even more pronounced was the shift in the relationship between pCa and myosin-ATPase (SPDR 6.01, 95% confidence limits 5.99-6.03 vs. TGR(mREN2)27 5.77, 95% confidence limits 5.73-5.79, pCa units). The maximal myosin-ATPase activity was reduced in TGR(mREN2)27 compared to SPDR, respectively (211.0 +/- 28.77 micromol ADP/s vs. 271.6 +/- 43.66 micromol ADP/s, P < 0.05). Tension cost (ATPase activity/tension) was significantly reduced in TGR(mREN2)27. The beta-MHC expression was significantly increased in TGR(mREN2)27. There was no isoform shift for TnT (protein and mRNA), as well as TnI, and no alteration of the phosphorylation of TnI in TGR(mREN2)27 compared to SPRD. The present study demonstrates that cardiac hypertrophy, induced by an activation of the renin-angiotensin system, leads to adapting alterations on the level of the contractile filaments, which reduce tension cost.

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“…This shorter transcript is also detected in undifferentiated mouse embryonic stem cells but is rapidly down-regulated after differentiation (Slager et al, 1993), and is generally regarded as an embryonic isoform. It is, thus, one of several examples of so-called "embryonic genes" that are up-regulated post-MI (Kim et al, 2002;Razeghi et al, 2001). The combined studies described here on the expression of CTGF in development, adulthood, and post-MI indicates that CTGF also falls into this category.…”

Section: Up-regulation Of Ctgf and Tgf␤ But Not Bmp Signaling In Scamentioning

confidence: 99%

Connective tissue growth factor expression and Smad signaling during mouse heart development and myocardial infarction

Lopes

Feijen

Korving

et al. 2004

Developmental Dynamics

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Connective tissue growth factor (CTGF) is reported to be a target gene of transforming growth factor ␤ (TGF␤) and bone morphogenetic protein (BMP) in vitro. Its physiological role in angiogenesis and skeletogenesis during mouse development has been described recently. Here, we have mapped expression of CTGF mRNA during mouse heart development, postnatal adult life, and after experimental myocardial infarction. Furthermore, we investigated the relationship between CTGF and the BMP/TGF␤ signaling pathway in particular during heart development in mutant mice. Postnatally, CTGF expression in the heart became restricted to the atrium. Strikingly, 1 week after myocardial infarction, when myocytes have disappeared from the infarct zone, CTGF and TGF␤ expression as well as activated forms of TGF␤ but not BMP, Smad effector proteins are colocalized exclusively in the fibroblasts of the scar tissue, suggesting possible cooperation between CTGF and TGF␤ during the pathological fibrotic response. Developmental Dynamics 231:542-550, 2004.

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Re-Expression of Fetal Troponin Isoforms in the Postinfarction Failing Heart of the Rat.

Cited by 18 publications

References 31 publications

Quantitative comparison of sarcomeric phosphoproteomes of neonatal and adult rat hearts

Quantitative comparison of sarcomeric phosphoproteomes of neonatal and adult rat hearts

Altered tension cost in (TG(mREN-2)27) rats overexpressing the mouse renin gene

Connective tissue growth factor expression and Smad signaling during mouse heart development and myocardial infarction

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