- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Annual Issues ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
BioMed Research International
Volume 2014 (2014), Article ID 151726, 9 pages
Comparison of the Ventricle Muscle Proteome between Patients with Rheumatic Heart Disease and Controls with Mitral Valve Prolapse: HSP 60 May Be a Specific Protein in RHD
1Department of Cardiothoracic Surgery, The Affiliated Hospital, Ningbo Medical Centre Lihuili Hospital, Ningbo University, Ningbo, Zhejiang 315041, China
2Department of Cardiothoracic Surgery, The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang 310006, China
Received 2 December 2013; Revised 31 January 2014; Accepted 3 February 2014; Published 12 March 2014
Academic Editor: Anthony Gramolin
Copyright © 2014 Dawei Zheng et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- B. Shah, M. Sharma, R. Kumar, K. N. Brahmadathan, V. J. Abraham, and R. Tandon, “Rheumatic heart disease: progress and challenges in India,” The Indian Journal of Pediatrics, vol. 80, 1, supplement, pp. S77–S86, 2013.
- D. Toor and H. Vohra, “Immune responsiveness during disease progression from acute rheumatic fever to chronic rheumatic heart disease,” Microbes Infect, vol. 14, no. 12, pp. 1111–1117, 2012.
- V. Kuma, A. K. Abbas, N. Fausto, and R. Mitchell, Robbins Basic Pathology, 2007.
- R. Bhardwaj, A. Kandoria, R. Marwah et al., “Prevalence of rheumatic fever and rheumatic heart disease in rural population of Himachal—a population based study,” Journal of the Association of Physicians of India, vol. 60, pp. 13–14, 2012.
- P. Nordet, R. Lopez, A. Dueñas, and L. Sarmiento, “Prevention and control of rheumatic fever and rheumatic heart disease: the Cuban experience (1986–1996–2002),” Cardiovascular Journal of Africa, vol. 19, no. 3, pp. 135–140, 2008.
- J. L. Boehmer, J. A. DeGrasse, M. A. McFarland et al., “The proteomic advantage: label-free quantification of proteins expressed in bovine milk during experimentally induced coliform mastitis,” Veterinary Immunology and Immunopathology, vol. 138, no. 4, pp. 252–266, 2010.
- H. Hondermarck, A. S. Vercoutter-Edouart, F. Révillion et al., “Proteomics of breast cancer for marker discovery and signal pathway profiling,” Proteomics, vol. 1, no. 10, pp. 1216–1232, 2001.
- K. C. Faé, D. Diefenbach da Silva, A. M. B. Bilate et al., “PDIA3, HSPA5 and vimentin, proteins identified by 2-DE in the valvular tissue, are the target antigens of peripheral and heart infiltrating T cells from chronic rheumatic heart disease patients,” Journal of Autoimmunity, vol. 31, no. 2, pp. 136–141, 2008.
- S. Gupta and A. A. Knowlton, “HSP60, Bax, apoptosis and the heart,” Journal of Cellular and Molecular Medicine, vol. 9, no. 1, pp. 51–58, 2005.
- S. C. Kim, J. P. Stice, L. Chen et al., “Extracellular heat shock protein 60, cardiac myocytes, and apoptosis,” Circulation Research, vol. 105, no. 12, pp. 1186–1195, 2009.
- Z. A. Malik, K. S. Kott, A. J. Poe et al., “Cardiac myocyte exosomes: stability, HSP60, and proteomics,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 304, no. 7, pp. H954–H965, 2013.
- W. Chen, U. Syldath, K. Bellmann, V. Burkart, and H. Kolb, “Human 60-kDa heat-shock protein: a danger signal to the innate immune system,” Journal of Immunology, vol. 162, no. 6, pp. 3212–3219, 1999.
- A. Kol, A. H. Lichtman, R. W. Finberg, P. Libby, and E. A. Kurt-Jones, “Cutting edge: heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells,” Journal of Immunology, vol. 164, no. 1, pp. 13–17, 2000.
- J. Tian, X. Guo, X. M. Liu et al., “Extracellular HSP60 induces inflammation through activating and up-regulating TLRs in cardiomyocytes,” Cardiovascular Research, vol. 98, pp. 391–401, 2013.
- L. Lin, S. C. Kim, Y. Wang et al., “HSP60 in heart failure: abnormal distribution and role in cardiac myocyte apoptosis,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 293, no. 4, pp. H2238–H2247, 2007.
- A. A. Knowlton, S. Kapadia, G. Torre-Amione et al., “Differential expression of heat shock proteins in normal and failing human hearts,” Journal of Molecular and Cellular Cardiology, vol. 30, no. 4, pp. 811–818, 1998.
- J. Sakai, H. Ishikawa, H. Satoh, S. Yamamoto, S. Kojima, and M. Kanaoka, “wo-dimensional differential gel electrophoresis of rat heart proteins in ischemia and ischemia-reperfusion,” Methods in Molecular Biology, vol. 357, pp. 33–43, 2007.
- D. Tontsch, S. Pankuweit, and B. Maisch, “Autoantibodies in the sera of patient with rheumatic heart disease: characterization of myocardial antigens by two-dimensional immunoblotting and N-terminal sequence analysis,” Clinical and Experimental Immunology, vol. 121, no. 2, pp. 270–274, 2000.
- Y. Wang, L. Chen, N. Hagiwara, and A. A. Knowlton, “Regulation of heat shock protein 60 and 72 expression in the failing heart,” Journal of Molecular and Cellular Cardiology, vol. 48, no. 2, pp. 360–366, 2010.
- S. Kobba, S. C. Kim, L. Chen et al., “The heat shock paradox and cardiac myocytes: role of heat shock factor,” Shock, vol. 35, no. 5, pp. 478–484, 2011.
- J. Pye, F. Ardeshirpour, A. McCain et al., “Proteasome inhibition ablates activation of NF-κB in myocardial reperfusion and reduces reperfusion injury,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 284, no. 3, pp. H919–H926, 2003.
- A. Anbanandam, D. C. Albarado, D. C. Tirziu, M. Simons, and S. Veeraraghavan, “Molecular basis for proline- and arginine-rich peptide inhibition of proteasome,” Journal of Molecular Biology, vol. 384, no. 1, pp. 219–227, 2008.
- P. Vicart, J. M. Dupret, J. Hazan et al., “Human desmin gene: cDNA sequence, regional localization and exclusion of the locus in a familial desmin-related myopathy,” Human Genetics, vol. 98, no. 4, pp. 422–429, 1996.
- P. M. McLendon and J. Robbins, “Desmin-related cardiomyopathy: an unfolding story,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 301, no. 4, pp. H1220–H1228, 2011.
- S. Di Somma, M. P. Di Benedetto, G. Salvatore et al., “Desmin-free cardiomyocytes and myocardial dysfunction in end stage heart failure,” European Journal of Heart Failure, vol. 6, no. 4, pp. 389–398, 2004.
- A. Pawlak, R. J. Gil, T. Kulawik et al., “Type of desmin expression in cardiomyocytes—a good marker of heart failure development in idiopathic dilated cardiomyopathy,” Journal of Internal Medicine, vol. 272, pp. 287–297, 2012.
- G. Monreal, L. M. Nicholson, B. Han et al., “Cytoskeletal remodeling of desmin is a more accurate measure of cardiac dysfunction than fibrosis or myocyte hypertrophy,” Life Sciences, vol. 83, no. 23-24, pp. 786–794, 2008.
- J. L. Kadrmas and M. C. Beckerle, “The LIM domain: from the cytoskeleton to the nucleus,” Nature Reviews Molecular Cell Biology, vol. 5, no. 11, pp. 920–931, 2004.
- K. Jani and F. Schöck, “Zasp is required for the assembly of functional integrin adhesion sites,” Journal of Cell Biology, vol. 179, no. 7, pp. 1583–1597, 2007.
- G. Schaffar, J. Taniguchi, T. Brodbeck et al., “LIM-only protein 4 interacts directly with the repulsive guidance molecule a receptor Neogenin,” Journal of Neurochemistry, vol. 107, no. 2, pp. 418–431, 2008.
- M. Zheng, H. Cheng, I. Banerjee, and J. Chen, “ALP/Enigma PDZ-LIM domain proteins in the heart,” Journal of Molecular Cell Biology, vol. 2, no. 2, pp. 96–102, 2010.
- H. Xia, S. T. Winokur, W. L. Kuo, M. R. Altherr, and D. S. Bredt, “Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs,” Journal of Cell Biology, vol. 139, no. 2, pp. 507–515, 1997.
- M. Pashmforoush, P. Pomiès, K. L. Peterson et al., “Adult mice deficient in actinin-associated LIM-domain protein reveal a developmental pathway for right ventricular cardiomyopathy,” Nature Medicine, vol. 7, no. 5, pp. 591–597, 2001.
- I. Lorenzen-Schmidt, A. D. McCulloch, and J. H. Omens, “Deficiency of actinin-associated LIM protein alters regional right ventricular function and hypertrophic remodeling,” Annals of Biomedical Engineering, vol. 33, no. 7, pp. 888–896, 2005.
- K. Jo, B. Rutten, R. C. Bunn, and D. S. Bredt, “Actinin-associated LIM protein-deficient mice maintain normal development and structure of skeletal muscle,” Molecular and Cellular Biology, vol. 21, no. 5, pp. 1682–1687, 2001.
- P. Gunning, R. Weinberger, and P. Jeffrey, “Actin and tropomyosin isoforms in morphogenesis,” Anatomy and Embryology, vol. 195, no. 4, pp. 311–315, 1997.
- S. V. Perry, “Vertebrate tropomyosin: distribution, properties and function,” Journal of Muscle Research and Cell Motility, vol. 22, no. 1, pp. 5–49, 2001.
- C. L. Albert Wang and L. M. Coluccio, “New insights into the regulation of the actin cytoskeleton by tropomyosin,” International Review of Cell and Molecular Biology, vol. 281, pp. 91–128, 2010.
- G. Jagatheesan, S. Rajan, and D. F. Wieczorek, “Investigations into tropomyosin function using mouse models,” Journal of Molecular and Cellular Cardiology, vol. 48, no. 5, pp. 893–898, 2010.
- P. Minarik, N. Tomaskova, M. Kollarova, and M. Antalik, “Malate dehydrogenases—structure and function,” General Physiology and Biophysics, vol. 21, pp. 257–265, 2002.
- S. M. Lee, S. H. Dho, S. K. Ju, J. S. Maeng, J. Y. Kim, and K. S. Kwon, “Cytosolic malate dehydrogenase regulates senescence in human fibroblasts,” Biogerontology, vol. 13, no. 5, pp. 525–536, 2012.
- R. Y. L. Zee, A. J. Castonguay, N. S. Barton, S. Germer, and M. Martin, “Mean leukocyte telomere length shortening and type 2 diabetes mellitus: a case-control study,” Translational Research, vol. 155, no. 4, pp. 166–169, 2010.
- M. Knecht, V. Regitz-Zagrosek, K. P. Pleissner et al., “Characterization of myocardial protein composition in dilated cardiomyopathy by two-dimensional gel electrophoresis,” European Heart Journal, vol. 15, pp. 37–44, 1994.
- J. Mollet, A. Delahodde, V. Serre et al., “CABC1 gene mutations cause ubiquinone deficiency with cerebellar ataxia and seizures,” American Journal of Human Genetics, vol. 82, no. 3, pp. 623–630, 2008.
- R. Horvath, B. Czermin, S. Gulati et al., “Adult-onset cerebellar ataxia due to mutations in CABC1/ADCK3,” Journal of Neurology, Neurosurgery and Psychiatry, vol. 83, no. 2, pp. 174–178, 2012.
- M. Iiizumi, H. Arakawa, T. Mori, A. Ando, and Y. Nakamura, “Isolation of a novel gene, CABC1, encoding a mitochondrial protein that is highly homologous to yeast activity of bc1 complex,” Cancer Research, vol. 62, no. 5, pp. 1246–1250, 2002.
- R. A. Musrati, M. Kollárová, N. Mernik, and D. Mikulášová, “Malate dehydrogenase: distribution, function and properties,” General Physiology and Biophysics, vol. 17, no. 3, pp. 193–210, 1998.