Influence of substrate structure on turnover of the organic cation/H + exchanger of the renal luminal membrane

1998 ◽  
Vol 436 (3) ◽  
pp. 469-477 ◽  
Author(s):  
Stephen H. Wright ◽  
Theresa M. Wunz
Keyword(s):  
Organic Cation ◽  
Substrate Structure ◽  
Luminal Membrane ◽  
Influence Of Substrate

Influence of substrate structure on the development of stress anisotropy in CrN coatings

2008 ◽  
Vol 2 (5) ◽  
pp. 337 ◽  
Author(s):  
F. Gauzzi ◽  
G. Gusmano ◽  
F.R. Lamastra ◽  
R. Montanari ◽  
T. Valente
Keyword(s):  
Stress Anisotropy ◽  
Substrate Structure ◽  
Influence Of Substrate ◽  
Crn Coatings

scholarly journals Interaction of H+ with the extracellular and intracellular aspects of hMATE1

2011 ◽  
Vol 301 (3) ◽  
pp. F520-F528 ◽  
Author(s):  
Yodying Dangprapai ◽  
Stephen H. Wright
Keyword(s):  
Time Course ◽  
Organic Cation ◽  
Physiological Function ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Ovary Cells ◽  
Molecular Identity ◽  
Luminal Membrane ◽  
Ph Conditions ◽  
Kinetics Of

Human multidrug and toxin extrusion 1 (hMATE1, SLC47A1) is a major candidate for being the molecular identity of organic cation/proton (OC/H+) exchange activity in the luminal membrane of renal proximal tubules. Although physiological function of hMATE1 supports luminal OC efflux, the kinetics of hMATE1-mediated OC transport have typically been characterized through measurement of uptake, i.e., the interaction between outward-facing hMATE1 and OCs. To examine kinetics of hMATE1-mediated transport in a more physiologically relevant direction, i.e., an interaction between inward-facing hMATE1 and cytoplasmic substrates, we measured the time course of hMATE1-mediated efflux of the prototypic MATE1 substrate, [3H]1-methyl-4-phenylpyridinium, under a variety of intra- and extracellular pH conditions, from Chinese hamster ovary cells that stably expressed the transporter. In this study, we showed that an IC50/ Ki for interaction between extracellular H+ and outward-facing hMATE1 determined from conventional uptake experiments [12.9 ± 1.23 nM (pH 7.89); n = 9] and from the efflux protocol [14.7 ± 3.45 nM (pH 7.83); n = 3] was not significantly different ( P = 0.6). Furthermore, kinetics of interaction between intracellular H+ and inward-facing hMATE1 determined using the efflux protocol revealed an IC50 for H+ of 11.5 nM (pH 7.91), consistent with symmetrical interactions of H+ with the inward-facing and outward-facing aspects of hMATE1.

scholarly journals The Influence of Substrate Structure on Membrane Adhesion

Langmuir ◽  
1999 ◽  
Vol 15 (26) ◽  
pp. 8902-8914 ◽  
Author(s):  
Peter S. Swain ◽  
David Andelman
Keyword(s):  
Substrate Structure ◽  
Membrane Adhesion ◽  
Influence Of Substrate

scholarly journals Influence of substrate structure on in vitro ribozyme activity of a group II intron

RNA ◽  
1998 ◽  
Vol 4 (6) ◽  
pp. 694-708 ◽  
Author(s):  
ALEXIS NOLTE ◽  
GUILLAUME CHANFREAU ◽  
ALAIN JACQUIER
Keyword(s):  
Group Ii Intron ◽  
Substrate Structure ◽  
Group Ii ◽  
Influence Of Substrate
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