PMID- 9740065
OWN - NLM
STAT- MEDLINE
DCOM- 19990114
LR  - 20061115
IS  - 0173-0835 (Print)
IS  - 0173-0835 (Linking)
VI  - 19
IP  - 11
DP  - 1998 Aug
TI  - Cardiac protein abnormalities in dilated cardiomyopathy detected by 
      two-dimensional polyacrylamide gel electrophoresis.
PG  - 2031-42
AB  - The aim of the investigation was to determine whether there are specific global 
      quantitative and qualitative changes in protein expression in heart tissue from 
      patients with dilated cardiomyopathy (DCM) compared with ischaemic heart disease 
      and undiseased tissue. Two-dimensional (2-D) polyacrylamide gel electrophoresis 
      and computer analysis was used to study protein alteration in DCM biopsy material 
      (n=28) compared with donor heart biopsy samples (n=9) and explanted hearts from 
      individuals suffering from ischaemic heart disease (IHD; n = 21). A total of 88 
      proteins displayed decreased abundance in DCM versus IHD material while five 
      proteins had elevated levels in the DCM group (p<0.01). The most prominent 
      changes occurred in the contractile protein myosin light chain 2 and in a group 
      of proteins identified as desmin. These changes do not appear to be artefactual 
      degradation events occurring during sample processing. These proteins are not 
      apparent in electrophoretic separations of vascular tissue or cultured 
      endothelial cells, mesothelial cells or cardiac fibroblasts, which are clearly 
      distinguishable from the 2-D protein patterns of whole heart and of isolated 
      cardiac myocytes and do not appear to reflect variations in the cellular 
      composition of biopsy samples. The different protein patterns observed in 
      cardiomyopathy showed no obvious relationship with New York Heart Association 
      (NYHA) functional class or haemodynamic parameters. The study has demonstrated 
      significant alterations in quantitative protein expression in the DCM heart which 
      would have serious implications for myocyte function. These changes might be 
      explained by altered protease activity in DCM which could exacerbate contractile 
      dysfunction in the failing heart.
FAU - Corbett, J M
AU  - Corbett JM
AD  - Department of Cardiothoracic Surgery, National Heart and Lung Institute, Imperial 
      College School of Medicine, London, UK.
FAU - Why, H J
AU  - Why HJ
FAU - Wheeler, C H
AU  - Wheeler CH
FAU - Richardson, P J
AU  - Richardson PJ
FAU - Archard, L C
AU  - Archard LC
FAU - Yacoub, M H
AU  - Yacoub MH
FAU - Dunn, M J
AU  - Dunn MJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Electrophoresis
JT  - Electrophoresis
JID - 8204476
RN  - 0 (Proteins)
SB  - IM
MH  - Adult
MH  - Cardiomyopathy, Dilated/*metabolism
MH  - *Electrophoresis, Gel, Two-Dimensional
MH  - Female
MH  - Humans
MH  - Male
MH  - Middle Aged
MH  - Myocardium/*chemistry/pathology
MH  - Proteins/*analysis
MH  - Time Factors
EDAT- 1998/09/18 00:00
MHDA- 1998/09/18 00:01
CRDT- 1998/09/18 00:00
PHST- 1998/09/18 00:00 [pubmed]
PHST- 1998/09/18 00:01 [medline]
PHST- 1998/09/18 00:00 [entrez]
AID - 10.1002/elps.1150191123 [doi]
PST - ppublish
SO  - Electrophoresis. 1998 Aug;19(11):2031-42. doi: 10.1002/elps.1150191123.