Effects of renovascular hypertension on myocardial protein patterns: Analysis by computer-assisted two-dimensional gel electrophoresis

1998 ◽  
Vol 19 (11) ◽  
pp. 2043-2050 ◽  
Author(s):  
Klaus-Peter Pleißner ◽  
Vera Regitz-Zagrosek ◽  
Bernd Krüdewagen ◽  
Jörg Trenkner ◽  
Berthold Hocher ◽  
...  
Keyword(s):  
Renovascular Hypertension ◽  
Gel Electrophoresis ◽  
Computer Assisted ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Two Dimensional Gel Electrophoresis

Protein variability among Portuguese and other populations of Globodera rostochiensis revealed by two-dimensional gel electrophoresis with computed image analysis

Nematology ◽  
2000 ◽  
Vol 2 (4) ◽  
pp. 461-471 ◽  
Author(s):  
Maria Susana Newton De Almeida Santos ◽  
Didier Mugniéry ◽  
Maria José Moreno Da Cunha ◽  
Isabel Maria De Oliveira Abrantes ◽  
Michel Bossis
Keyword(s):  
Image Analysis ◽  
Gel Electrophoresis ◽  
Gaussian Model ◽  
Globodera Rostochiensis ◽  
Computer Assisted ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Two Dimensional Gel Electrophoresis ◽  
Bootstrap Analysis ◽  
Biological Studies

AbstractSilver-stained two dimensional gel electrophoresis (2-DGE) was used to characterize 46 populations of G. rostochiensis and, as an outgroup, one population of G. pallida. Protein patterns of white females were compared with the aid of computer assisted image analysis using Kepler software. A synthetic master pattern of G. rostochiensis, built with spots present in all populations and detected in at least two of three gels of each population, revealed the presence of 379 protein spots. The populations were compared taking into account the main spots present in each isolate (spots present in two of three gels, amplitude greater than 7, volume greater than 500 and with values fitting the Gaussian model). Comparison allowed the identification of 200 polymorphic spots. Similarity indices (F) and genetic distances (D = 1 ­ F) between populations were calculated on the basis of homologous polymorphic spots, and a dendrogram was constructed according to the UPGMA method. Bootstrap analysis was used to assess the significance of the results from the phenetic study. The presence or absence of specific spots in some G. rostochiensis populations is discussed. Further biochemical and biological studies are necessary to determine if specific proteins are linked to virulence. Variabilité protéique de populations portugaises et d'origines diverses de Globodera rostochiensis détectée par électrophorèse bidimensionnelle et analysée par informatique - L'électrophorèse bidimensionnelle (E2D) est utilisée pour caractériser 46 populations européennes de G. rostochiensis et une population de G. pallida, prise comme groupe extérieur. Les protéinogrammes obtenus à partir de femelles blanches sont comparés par analyse informatisée d'images à l'aide du logiciel Kepler. Une image de référence est constituée au vu des taches protéiques détectées dans l'ensemble des populations étudiées par transfert vers cette image synthétique de chaque protéine détectée au moins deux fois sur trois dans une population. Celle-ci permet de répertorier et de localiser 379 protéines. Les populations ont été comparées avec les taches pröteiques les plus importantes (taches présentes dans au moins deux gels sur trois, amplitude plus grande que 7, volume plus grand que 500 et valeurs dans le model Gaussien). La comparaison des populations a permis de détecter 200 protéines. Les indices de similarité (F) et les distances génétiques (D = 1 ­ F) ont été étudiés à partir des taches polymorphes homologues présentes dans chaque population. Le dendrogramme a été construit selon la méthode UPGMA. Une analyse des valeurs de bootstraps a été utilisée pour estimer la signification des résultats phénétiques. La présence ou l'absence de protéines spécifiques de certaines populations de G. rostochiensis est discutée. D'autres études biochimiques et biologiques sont en cours pour déterminer si les protéines spécifiques sont ou non liées à la virulence.

Proteins in normal, irradiated, and postmortem human brain quantitatively compared by using two-dimensional gel electrophoresis.

1984 ◽  
Vol 30 (12) ◽  
pp. 1989-1995 ◽  
Author(s):  
R K Narayan ◽  
W E Heydorn ◽  
G J Creed ◽  
P L Kornblith ◽  
D M Jacobowitz
Keyword(s):  
Cerebral Cortex ◽  
Gel Electrophoresis ◽  
Protein Pattern ◽  
Relative Molecular Mass ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Human Cerebral Cortex ◽  
Postmortem Human Brain ◽  
Two Dimensional Gel Electrophoresis ◽  
Fresh Frozen

Abstract Using a combination of two-dimensional gel electrophoresis (2DE), silver staining, and computerized densitometry, we studied protein patterns in human cerebral cortex: normal fresh-frozen, fresh-frozen but previously irradiated, and post-mortem. The relative molecular mass of the resolved proteins ranged from 14 400 to 100 000, the isoelectric points from 4.75 to 7.0. The pattern of proteins (six of them identified) was essentially the same for all three groups. However, computerized densitometry demonstrated significant alterations in the density of several spots in the irradiated and postmortem groups as compared with the normal controls. Irradiated cortex showed statistically significant changes in only six spots (three increased and three decreased in density); postmortem material showed 20 altered spots (16 diminished and four increased). Evidently normal human cerebral cortex has a consistent protein pattern on 2DE, which is quantitatively (but not qualitatively) altered in irradiated and postmortem material. These findings provide a point of reference against which proteins from abnormal brain material can be compared, both qualitatively and quantitatively.

Induction of Heat-Shock Protein (hsp) by Moxibustion

1995 ◽  
Vol 23 (03n04) ◽  
pp. 327-330 ◽  
Author(s):  
Kazuko Kobayashi
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Hsp 70 ◽  
Protein Patterns ◽  
Two Dimensional Gel Electrophoresis ◽  
Hip Muscle ◽  
And Control ◽  
Muscular Tissues

Rats were treated by moxibustion at the point of hip muscle, and intramuscular temperature was kept at 40°C for 15 minutes. The rats were sacrificed under deep anesthesia and the muscular tissues were excised immediately, three hours and 24 hours after stimulation. Proteins were extracted from the homogenized and centrifuged tissues of the stimulated rats and control rats. Two-dimensional gel electrophoresis of the proteins was carried out. Heat-shock protein (hsp) with molecular weight of 70,000 (hsp 70), 85,000 (hsp 85) and 100,000 (hsp 100) was detected in rats sacrificed three hours after the stimulation by moxibustion. Protein patterns were analyzed and the ratios of the hsps were obtained.

scholarly journals Analysis of proteins associated with storage root formation in cassava using two-dimensional gel electrophoresis

2001 ◽  
Vol 13 (1) ◽  
pp. 41-48 ◽  
Author(s):  
GLAUCIA B. CABRAL ◽  
LUIZ J.C.B. CARVALHO
Keyword(s):  
Gel Electrophoresis ◽  
Adventitious Root ◽  
Protein Pattern ◽  
Protein Profile ◽  
Secondary Growth ◽  
Starch Accumulation ◽  
Computer Assisted ◽  
Two Dimensional ◽  
Storage Root ◽  
Two Dimensional Gel Electrophoresis

Two-dimensional gel electrophoresis analysis was performed on adventitious and storage root in cassava (Manihot esculenta Crantz). Adventitious root lacking swelling formation and swelled storage root were obtained from the accession WU104 grown in the green house of the Department of Biology in Washington University in St. Louis (MO-USA). Saline buffer-soluble proteins were extracted, separated in a high-resolution 2-D electrophoresis system, visualized with silver staining gel procedure, and digital image generate for further analysis. Quantitative and qualitative protein spots analysis was performed with a computer assisted image software system. Results revealed large variation in the complexity of the gel protein profile between the two root systems. About 90% of the protein spots appeared in the pI range value of 4.0 to 6.5 and between 14 to 80 Kda of molecular mass. Detailed computer assisted analysis of this gel allowed us to establish 5 distinct classes of protein based on spot quantification that could be associated with swelling and non-swelling roots. Variation in the complexity of protein pattern was related with different type of root. Whereas the adventitious root showed a more simple profile related to primary growth, the storage root showed to be a more complex profile related to secondary growth and starch accumulation.

Two-dimensional protein patterns of tomato (Lycopersicon esculentum Mill.) seeds; effects of isolation procedure and imbibition

1994 ◽  
Vol 4 (3) ◽  
pp. 275-283 ◽  
Author(s):  
J. H. W. Bergervoet ◽  
H. L. Kraak ◽  
C. H. R. De Vos ◽  
R. J. Bino
Keyword(s):  
Lycopersicon Esculentum ◽  
Gel Electrophoresis ◽  
Protein Pattern ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Two Dimensional Gel Electrophoresis ◽  
General Picture ◽  
Isolation Methods ◽  
Lysis Buffer

AbstractA computer-aided comparison of tomato (Lycopersicon esculentum Mill.) seed protein patterns, obtained after two-dimensional gel electrophoresis, was made for three different extraction procedures: TCA acetone/lysis buffer, lysis buffer only and modified Laemmli/lysis buffer. Comparison of the isolation methods showed that about half of the amount of proteins detected was common in each method. Also, proteins specific to some isolation methods were detected. Protein synthesis during imbibition was monitored using 35S-methionine. After labelling the proteins were extracted using TCA acetone/lysis buffer. Following two-dimensional gel electrophoresis the gels were first silver stained, to give a general picture of all proteins present in the seed, then the gels were exposed to a film for autoradiography. Comparison of the in vivo-synthesized protein patterns and the silver-stained proteins revealed that from day 0 to day 1 the protein pattern was changed but the total number of different spots was similar. After 1 day of imbibition, the number of protein spots increased greatly and the protein pattern changed again.

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