TY - JOUR
T1 - Normal human mitral valve proteome
T2 - A preliminary investigation by gel-based and gel-free proteomic approaches
AU - Brioschi, Maura
AU - Baetta, Roberta
AU - Ghilardi, Stefania
AU - Gianazza, Erica
AU - Guarino, Anna
AU - Parolari, Alessandro
AU - Polvani, Gianluca
AU - Tremoli, Elena
AU - Banfi, Cristina
PY - 2016/10/1
Y1 - 2016/10/1
N2 - The mitral valve is a highly complex structure which regulates blood flow from the left atrium to the left ventricle (LV) avoiding a significant forward gradient during diastole or regurgitation during systole. The integrity of the mitral valve is also essential for the maintenance of normal LV size, geometry, and function. Significant advances in the comprehension of the biological, functional, and mechanical behavior of the mitral valve have recently been made. However, current knowledge of protein components in the normal human mitral valve is still limited and complicated by the low cellularity of this tissue and the presence of high abundant proteins from the extracellular matrix. We employed here an integrated proteomic approach to analyse the protein composition of the normal human mitral valve and reported confident identification of 422 proteins, some of which have not been previously described in this tissue. In particular, we described the ability of pre-MS separation technique based on liquid-phase IEF and SDS-PAGE to identify the largest number of proteins. We also demonstrated that some of these proteins, e.g. αB-Crystallin, septin-11, four-and-a-half LIM domains protein 1, and dermatopontin, are synthesised by interstitial cells isolated from human mitral valves. These initial results provide a valuable basis for future studies aimed at analysing in depth the mitral valve protein composition and at investigating potential pathogenetic molecular mechanisms. Data are available via ProteomeXchange with identifier PXD004397.
AB - The mitral valve is a highly complex structure which regulates blood flow from the left atrium to the left ventricle (LV) avoiding a significant forward gradient during diastole or regurgitation during systole. The integrity of the mitral valve is also essential for the maintenance of normal LV size, geometry, and function. Significant advances in the comprehension of the biological, functional, and mechanical behavior of the mitral valve have recently been made. However, current knowledge of protein components in the normal human mitral valve is still limited and complicated by the low cellularity of this tissue and the presence of high abundant proteins from the extracellular matrix. We employed here an integrated proteomic approach to analyse the protein composition of the normal human mitral valve and reported confident identification of 422 proteins, some of which have not been previously described in this tissue. In particular, we described the ability of pre-MS separation technique based on liquid-phase IEF and SDS-PAGE to identify the largest number of proteins. We also demonstrated that some of these proteins, e.g. αB-Crystallin, septin-11, four-and-a-half LIM domains protein 1, and dermatopontin, are synthesised by interstitial cells isolated from human mitral valves. These initial results provide a valuable basis for future studies aimed at analysing in depth the mitral valve protein composition and at investigating potential pathogenetic molecular mechanisms. Data are available via ProteomeXchange with identifier PXD004397.
KW - 2-dimensional electrophoresis (2-DE)
KW - Human normal mitral valve
KW - LC/MS
KW - Liquid-phase IEF
KW - Valvular interstitial cells
UR - http://www.scopus.com/inward/record.url?scp=84990241934&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84990241934&partnerID=8YFLogxK
U2 - 10.1002/elps.201600081
DO - 10.1002/elps.201600081
M3 - Article
VL - 37
SP - 2633
EP - 2643
JO - Electrophoresis
JF - Electrophoresis
SN - 0173-0835
IS - 20
ER -