TY - JOUR
T1 - Sarcoplasmic reticulum calcium ATPase interactions with decaniobate, decavanadate,vanadate, tungstate and molybdate
AU - Fraqueza, Gil
AU - Ohlin, Christian Andre
AU - Casey, William
AU - Aureliano, Manuel
PY - 2012
Y1 - 2012
N2 - Over the last few decades there has been increasing interest in oxometalate and polyoxometalate applications to medicine and pharmacology. This interest arose, at least in part, due to the properties of these classes of compounds as anti-cancer, anti-diabetic agents, and also for treatment of neurodegenerative diseases, among others. However, our understanding of the mechanism of action would be improved if biological models could be used to clarify potential toxicological effects in main cellular processes. Sarcoplasmic reticulum (SR) vesicles, containing a large amount of Ca2+-ATPase, an enzyme that accumulates calcium by active transport using ATP, have been suggested as a useful model to study the effects of oxometalates on calcium homeostasis. In the present article, it is shown that decavanadate, decaniobate, vanadate,
tungstate and molybdate, all inhibited SR Ca2+-ATPase, with the following IC50 values: 15, 35, 50, 400 I?M and 45 mM, respectively.
AB - Over the last few decades there has been increasing interest in oxometalate and polyoxometalate applications to medicine and pharmacology. This interest arose, at least in part, due to the properties of these classes of compounds as anti-cancer, anti-diabetic agents, and also for treatment of neurodegenerative diseases, among others. However, our understanding of the mechanism of action would be improved if biological models could be used to clarify potential toxicological effects in main cellular processes. Sarcoplasmic reticulum (SR) vesicles, containing a large amount of Ca2+-ATPase, an enzyme that accumulates calcium by active transport using ATP, have been suggested as a useful model to study the effects of oxometalates on calcium homeostasis. In the present article, it is shown that decavanadate, decaniobate, vanadate,
tungstate and molybdate, all inhibited SR Ca2+-ATPase, with the following IC50 values: 15, 35, 50, 400 I?M and 45 mM, respectively.
UR - http://www.sciencedirect.com/science/article/pii/S016201341100314X
U2 - 10.1016/j.jinorgbio.2011.10.010
DO - 10.1016/j.jinorgbio.2011.10.010
M3 - Article
VL - 107
SP - 82
EP - 89
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
SN - 0162-0134
ER -
