scholarly journals Proper progression of neurogenesis relies on a defined pattern of SUMO-modified proteins

2022 ◽  
Vol 17 (8) ◽  
pp. 0
Author(s):  
Mario García-Domínguez
Keyword(s):  
Modified Proteins

Accumulation of 4-hydroxy-2-nonenal-modified proteins in the white matter damage in chronic cerebral hypo-perfusion rat mode

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S262-S262
Author(s):  
Terubumi Watanabe ◽  
Yoshiko Yanagi ◽  
Takao Urabe ◽  
Yoshikuni Mizuno
Keyword(s):  
White Matter ◽  
White Matter Damage ◽  
Modified Proteins

scholarly journals The Alterations in Methylene Blue/Light-Treated Frozen Plasma Proteins Revealed by Proteomics

2021 ◽  
pp. 1-8
Author(s):  
Tiange Wu ◽  
Xiaoning Wang ◽  
Kai Ren ◽  
Xiaochen Huang ◽  
Jiankai Liu
Keyword(s):  
Mass Spectrometry ◽  
Methylene Blue ◽  
Western Blot ◽  
Blue Light ◽  
Differentially Expressed ◽  
Enzyme Linked Immunosorbent Assay ◽  
Differentially Expressed Protein ◽  
Significant Difference ◽  
Modified Proteins ◽  
Frozen Plasma

Introduction: The aim of this study was to investigate the modified proteins in methylene blue/light-treated frozen plasma (MB-FP) compared with fresh frozen plasma (FFP) in order to gain a better application of MB/light-treated plasma in clinic transfusion. Methods: MB-FP and FFP were collected from Changchun central blood station, and a trichloroacetic acid/acetone precipitation method was used to remove albumin for the enrichment of lower abundance proteins. The plasma protein in MB-FP and FFP were separated using two-dimensional gel electrophoresis (2-DE) and the differentially expressed protein spots were analyzed using mass spectrometry. Finally, the differentially expressed proteins were tested using Western blot and enzyme-linked immunosorbent assay (ELISA). Results: Approximately 14 differentially expressed protein spots were detected in the MB-FP, and FFP was chosen as the control. After 2-DE comparison analysis and mass spectrometry, 8 significantly differentially expressed protein spots were identified, corresponding to 6 different proteins, including complement C1r subcomponent (C1R), inter-alpha-trypsin inhibitor heavy chain H4 (ITI-H4), keratin, type II cytoskeletal 1 (KRT1), hemopexin (HPX), fibrinogen gamma chain (FGG), and transthyretin (TTR). Western blot showed no significant difference in the expression level of KRT1 between MB-FP and FFP (p > 0.05). Both Western blot and ELISA indicated that the level of HPX was significantly higher in FFP than in MB-FP (p < 0.05). Conclusion: This comparative proteomics study revealed that some significantly modified proteins occur in MB-FP, such as C1R, ITI-H4, KRT1, HPX, FGG, and TTR. Our findings provide more theoretical data for using MB-FP in transfusion medicine. However, the relevance of the data for the transfusion of methylene blue/light-treated plasma remains unclear. The exact modification of these proteins and the effects of these modified proteins on their functions and their effects in clinical plasma infusion need to be further studied.

scholarly journals Ion–ion reactions with fixed-charge modified proteins to produce ions in a single, very high charge state

2008 ◽  
Vol 276 (2-3) ◽  
pp. 136-143 ◽  
Author(s):  
Brian L. Frey ◽  
Casey J. Krusemark ◽  
Aaron R. Ledvina ◽  
Joshua J. Coon ◽  
Peter J. Belshaw ◽  
...  
Keyword(s):  
Charge State ◽  
High Charge State ◽  
Fixed Charge ◽  
High Charge ◽  
Modified Proteins ◽  
Very High

scholarly journals Hypertrophy-Reduced Autophagy Causes Cardiac Dysfunction by Directly Impacting Cardiomyocyte Contractility

Cells ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 805
Author(s):  
Christiane Ott ◽  
Tobias Jung ◽  
Sarah Brix ◽  
Cathleen John ◽  
Iris R. Betz ◽  
...  
Keyword(s):  
Cardiomyocyte Hypertrophy ◽  
Aortic Constriction ◽  
Cell Contractility ◽  
Neonatal Cardiomyocytes ◽  
Cardiomyocyte Contractility ◽  
Cardioprotective Effects ◽  
Modified Proteins ◽  
Cardiomyocyte Autophagy

Cardiac remodeling and contractile dysfunction are leading causes in hypertrophy-associated heart failure (HF), increasing with a population’s rising age. A hallmark of aged and diseased hearts is the accumulation of modified proteins caused by an impaired autophagy-lysosomal-pathway. Although, autophagy inducer rapamycin has been described to exert cardioprotective effects, it remains to be shown whether these effects can be attributed to improved cardiomyocyte autophagy and contractility. In vivo hypertrophy was induced by transverse aortic constriction (TAC), with mice receiving daily rapamycin injections beginning six weeks after surgery for four weeks. Echocardiographic analysis demonstrated TAC-induced HF and protein analyses showed abundance of modified proteins in TAC-hearts after 10 weeks, both reduced by rapamycin. In vitro, cardiomyocyte hypertrophy was mimicked by endothelin 1 (ET-1) and autophagy manipulated by silencing Atg5 in neonatal cardiomyocytes. ET-1 and siAtg5 decreased Atg5–Atg12 and LC3-II, increased natriuretic peptides, and decreased amplitude and early phase of contraction in cardiomyocytes, the latter two evaluated using ImageJ macro Myocyter recently developed by us. ET-1 further decreased cell contractility in control but not in siAtg5 cells. In conclusion, ET-1 decreased autophagy and cardiomyocyte contractility, in line with siAtg5-treated cells and the results of TAC-mice demonstrating a crucial role for autophagy in cardiomyocyte contractility and cardiac performance.

Sign in / Sign up

Export Citation Format

Share Document