scholarly journals Redox Modulation of Adipogenesis

2017 ◽  
Author(s):  
Xin Wang
Keyword(s):  
Redox Modulation

NMDA and GABAA receptors, NO and redox modulation

1996 ◽  
Vol 17 (5) ◽  
pp. 187-189 ◽  
Author(s):  
Henri Gozlan ◽  
Yohezkel Ben-Ari
Keyword(s):  
Gabaa Receptors ◽  
Redox Modulation

Redox modulation of curcumin stability: Redox active antioxidants increase chemical stability of curcumin

2015 ◽  
Vol 60 (3) ◽  
pp. 487-494 ◽  
Author(s):  
Yoshiki Nimiya ◽  
Weicang Wang ◽  
Zheyuan Du ◽  
Elvira Sukamtoh ◽  
Julia Zhu ◽  
...  
Keyword(s):  
Chemical Stability ◽  
Redox Modulation ◽  
Redox Active

scholarly journals Molecular and Functional Differences between Heart mKv1.7 Channel Isoforms

2006 ◽  
Vol 128 (1) ◽  
pp. 133-145 ◽  
Author(s):  
Rocio K. Finol-Urdaneta ◽  
Nina Strüver ◽  
Heinrich Terlau
Keyword(s):  
Translation Initiation ◽  
Cell Function ◽  
Functional Divergence ◽  
Initiation Site ◽  
Translation Initiation Site ◽  
Inactivation Kinetics ◽  
Mouse Heart ◽  
Redox Stress ◽  
Redox Modulation ◽  
Stress States

Ion channels are membrane-spanning proteins that allow ions to permeate at high rates. The kinetic characteristics of the channels present in a cell determine the cell signaling profile and therefore cell function in many different physiological processes. We found that Kv1.7 channels from mouse heart muscle have two putative translation initiation start sites that generate two channel isoforms with different functional characteristics, mKv1.7L (489 aa) and a shorter mKv1.7S (457 aa). The electrophysiological analysis of mKv1.7L and mKv1.7S channels revealed that the two channel isoforms have different inactivation kinetics. The channel resulting from the longer protein (L) inactivates faster than the shorter channels (S). Our data supports the hypothesis that mKv1.7L channels inactivate predominantly due to an N-type related mechanism, which is impaired in the mKv1.7S form. Furthermore, only the longer version mKv1.7L is regulated by the cell redox state, whereas the shorter form mKv1.7S is not. Thus, expression starting at each translation initiation site results in significant functional divergence. Our data suggest that the redox modulation of mKv1.7L may occur through a site in the cytoplasmic N-terminal domain that seems to encompass a metal coordination motif resembling those found in many redox-sensitive proteins. The mRNA expression profile and redox modulation of mKv1.7 kinetics identify these channels as molecular entities of potential importance in cellular redox-stress states such as hypoxia.

Redox modulation of glucose-6-P dehydrogenase inAnacystis nidulansand its ‘uncoupling’ by phage infection

FEBS Letters ◽  
1981 ◽  
Vol 126 (1) ◽  
pp. 85-88 ◽  
Author(s):  
Csaba Cséke ◽  
Árpád Balogh ◽  
Gábor L. Farkas
Keyword(s):  
Phage Infection ◽  
Redox Modulation

scholarly journals Selenium-Binding Protein 1 in Human Health and Disease

2018 ◽  
Vol 19 (11) ◽  
pp. 3437 ◽  
Author(s):  
Mostafa Elhodaky ◽  
Alan Diamond
Keyword(s):  
Binding Protein ◽  
Cellular Motility ◽  
Poor Clinical Outcome ◽  
Redox Modulation ◽  
Normal Tissues ◽  
Golgi Transport ◽  
Health And Disease ◽  
Cancer Types ◽  
Low Levels ◽  
Sulfur Containing

Selenium-binding protein 1 (SBP1) is a highly conserved protein that covalently binds selenium. SBP1 may play important roles in several fundamental physiological functions, including protein degradation, intra-Golgi transport, cell differentiation, cellular motility, redox modulation, and the metabolism of sulfur-containing molecules. SBP1 expression is often reduced in many cancer types compared to the corresponding normal tissues and low levels of SBP1 are frequently associated with poor clinical outcome. In this review, the transcriptional regulation of SBP1, the different physiological roles reported for SBP1, as well as the implications of SBP1 function in cancer and other diseases are presented.

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