지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2021.1
- 수록면
- 500 - 516 (17page)
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초록· 키워드
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Cardiac hypertrophic signaling cascades resulting in heart failure diseases are mediated by protein phosphorylation. Recent developments in mass spectrometry-based phosphoproteomics have led to the identification of thousands of differentially phosphorylated proteins and their phosphorylation sites. However, functional studies of these differentially phosphorylated proteins have not been conducted in a large-scale or high-throughput manner due to a lack of methods capable of revealing the functional relevance of each phosphorylation site. In this study, an integrated approach combining quantitative phosphoproteomics and cell-based functional screening using phosphorylation competition peptides was developed. A pathological cardiac hypertrophy model, junctate-1 transgenic mice and control mice, were analyzed using label-free quantitative phosphoproteomics to identify differentially phosphorylated proteins and sites. A cell-based functional assay system measuring hypertrophic cell growth of neonatal rat ventricle cardiomyocytes (NRVMs) following phenylephrine treatment was applied, and changes in phosphorylation of individual differentially phosphorylated sites were induced by incorporation of phosphorylation competition peptides conjugated with cell-penetrating peptides. Cell-based functional screening against 18 selected phosphorylation sites identified three phosphorylation sites (Ser-98, Ser-179 of Ldb3, and Ser-1146 of palladin) displaying near-complete inhibition of cardiac hypertrophic growth of NRVMs. Changes in phosphorylation levels of Ser-98 and Ser-179 in Ldb3 were further confirmed in NRVMs and other pathological/physiological hypertrophy models, including transverse aortic constriction and swimming models, using site-specific phospho-antibodies. Our integrated approach can be used to identify functionally important phosphorylation sites among differentially phosphorylated sites, and unlike conventional approaches, it is easily applicable for large-scale and/or high-throughput analyses.
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참고문헌 (66)
참고문헌 신청
Brandenburg, S. / 2016 / The molecular and functional identities of atrial cardiomyocytes in health and disease / Biochim. Biophys. Acta 1863(7 Pt B):1882~1893
Lundby, A. / 2013 / In vivo phosphoproteomics analysis reveals the cardiac targets of β-adrenergic receptor signaling / Sci. Signal 6:rs11
Luther, P. K. / 2011 / Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle / Proc. Natl. Acad. Sci. U. S. A 108:11423~11428
MacLennan, D. H. / 2003 / Phospholamban: a crucial regulator of cardiac contractility / Nat. Rev. Mol. Cell Biol 4:566~577
Mamidi, R. / 2017 / Cardiac myosin binding protein-C Ser 302 phosphorylation regulates cardiac β-adrenergic reserve / Sci. Adv 3:e1602445
Lundby, A. / 2013 / In vivo phosphoproteomics analysis reveals the cardiac targets of β-adrenergic receptor signaling / Sci. Signal 6:rs11
Luther, P. K. / 2011 / Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle / Proc. Natl. Acad. Sci. U. S. A 108:11423~11428
MacLennan, D. H. / 2003 / Phospholamban: a crucial regulator of cardiac contractility / Nat. Rev. Mol. Cell Biol 4:566~577
Mamidi, R. / 2017 / Cardiac myosin binding protein-C Ser 302 phosphorylation regulates cardiac β-adrenergic reserve / Sci. Adv 3:e1602445
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