scholarly journals Changes in the two-dimensional electrophoresis pattern of the Parkinson's disease related protein DJ-1 in human SH-SY5Y neuroblastoma cells after dopamine treatment

IUBMB Life ◽  
2010 ◽  
Vol 62 (9) ◽  
pp. spcone-spcone
Author(s):  
Tiziana Alberio ◽  
Monica Colapinto ◽  
Massimo Natale ◽  
Raffaella Ravizza ◽  
Marzia B. Gariboldi ◽  
...  
2010 ◽  
Vol 26 (7) ◽  
pp. 946-952 ◽  
Author(s):  
Massimo Natale ◽  
Dario Bonino ◽  
Paolo Consoli ◽  
Tiziana Alberio ◽  
Rivka G. Ravid ◽  
...  

1984 ◽  
Vol 30 (12) ◽  
pp. 1933-1937 ◽  
Author(s):  
M G Harrington ◽  
C R Merril

Abstract Cerebrospinal fluid (CSF) proteins, as resolved by two-dimensional electrophoresis and made visible by silver staining, have been examined in patients with various neurological diseases and normal volunteers. The patterns for 15 of 20 patients with Parkinson's disease showed a protein (Mr 25 000) with charge similar to albumin, which was not seen in the patterns for any of 91 normal volunteers. Patterns for 21 of 22 multiple sclerosis patients showed novel immunoglobulin light chain proteins, also not present in the CSF of any normal volunteers. Quantitative analysis by computer-assisted densitometry in Parkinson's disease and multiple sclerosis showed that 20 of 68 and 33 of 85 proteins, respectively, were significantly altered as compared with proteins in the normal population. This ability to characterize both Parkinson's disease and multiple sclerosis molecularly provides a broad baseline for improved clinical diagnosis and may serve as an aid in exploring the underlying pathophysiology. These studies illustrate the potential of applying this methodology in the study of neurological diseases.


1998 ◽  
Vol 19 (8-9) ◽  
pp. 1493-1500 ◽  
Author(s):  
Ingrid Miller ◽  
Paul Haynes ◽  
Manfred Gemeiner ◽  
Ruedi Aebersold ◽  
Cristina Manzoni ◽  
...  

1982 ◽  
Vol 47 (01) ◽  
pp. 019-021 ◽  
Author(s):  
Cemal Kuyas ◽  
André Haeberli ◽  
P Werner Straub

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.


2012 ◽  
Vol 18 (5) ◽  
pp. 819 ◽  
Author(s):  
Yanhua YANG ◽  
Weitong CUI ◽  
Xiaoyong LIU ◽  
Keming ZHU ◽  
Keping CHEN

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