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Fluorescence Measurements of Steady State Peroxynitrite Production Upon SIN-1 Decomposition: NADH Versus Dihydrodichlorofluorescein and Dihydrorhodamine 123
- F. Martin-Romero, Yolanda Gutiérrez-Martín, F. Henao, C. Gutiérrez-Merino
- BiologyJournal of Fluorescence
NADH was found to be less sensitive than dihydrorhodamine 123 and 2′,7′-dichlorodihydrofluorescein diacetate to oxidation by H2O2, which is produced during SIN-1 decomposition in common buffers.
Quantification and removal of glycogen phosphorylase and other enzymes associated with sarcoplasmic reticulum membrane preparations.
Modulation of sarcoplasmic reticulum Ca(2+)-ATPase by chronic and acute exposure to peroxynitrite.
- Yolanda Gutiérrez-Martín, F. Martin-Romero, F. Inesta-Vaquera, C. Gutiérrez-Merino, F. Henao
- BiologyEuropean journal of biochemistry
- 1 July 2004
The results showed that the target of peroxynitrite is the cytosolic globular domain of the SERCA and that major skeletal muscle intracellular reductants protected against inhibition of this ATPase by peroxlynitrite.
Store-operated calcium entry in differentiated C2C12 skeletal muscle cells.
Dissociation of Ca2+ from sarcoplasmic reticulum Ca2+-ATPase and changes in fluorescence of optically selected Trp residues. Effects of KCl and NaCl and implications for substeps in Ca2+ dissociation.
It is concluded that in the presence of KCl or NaCl and with an excitation wavelength of 290 nm, the rapid drop in tryptophan fluorescence mainly monitors the dissociation of the first of the two Ca2+ ions to be released from Ca2-ATPase, while excitation at 296 nm optically selects a subpopulation of Trp residues whose fluorescence level is lower in the ATPase species with one Ca2+.
Cancellation of the cooperativity of Ca2+ binding to sarcoplasmic reticulum Ca(2+)-ATPase by the non-ionic detergent dodecylmaltoside.
DM is found to be a useful tool in the analysis of the sequence of events occurring during Ca2+ binding, as compared to other detergents, the maltoside head group of DM might favor a stronger interaction with membranous ATPase, resulting in its high perturbing effect on Ca2- binding.
2,3,7,8-Tetrachlorodibenzo-p-dioxin induces apoptosis by disruption of intracellular calcium homeostasis in human neuronal cell line SHSY5Y
- Antonio Morales-Hernández, F. J. Sánchez-Martín, M. P. Hortigon-Vinagre, F. Henao, J. Merino
- 18 September 2012
The hypothesis that TCDD toxicity in SHSY5Y neuroblastoma cells provokes the disruption of calcium homeostasis, probably affecting membrane structural integrity, leading to an apoptotic process is supported.
A Remarkably Stable Phosphorylated Form of Ca2+-ATPase Prepared from Ca2+-loaded and Fluorescein Isothiocyanate-labeled Sarcoplasmic Reticulum Vesicles*
- P. Champeil, F. Henao, J. Lacapere, D. McIntosh
- Biology, ChemistryThe Journal of Biological Chemistry
- 23 February 2001
It is shown that, as long as the free calcium concentration on the cytosolic side is kept in the nanomolar range, this low fluorescence species is remarkably stable, even when the calcium gradient is subsequently dissipated by ionophore, and might open a path toward structural characterization of a stable phosphorylated form of Ca2+-ATPase for the first time.
The content of glycogen phosphorylase and glycogen in preparations of sarcoplasmic reticulum–glycogenolytic complex is enhanced in diabetic rat skeletal muscle
- E. Garduño, M. Nogues, J. M. Merino, C. Gutiérrez-Merino, F. Henao
- Biology, ChemistryDiabetologia
- 1 October 2001
Results suggest that under diabetic conditions, both glycogen phosphorylase and a small percentage of muscle glycogen are relocalized in the sarcoplasmic reticulum–glycogenolytic complex.
Phosphorylated Ca2+-ATPase Stable Enough for Structural Studies*
- F. Henao, F. Delavoie, J. Lacapere, D. McIntosh, P. Champeil
- Chemistry, BiologyThe Journal of Biological Chemistry
- 29 June 2001
It is shown that this phosphorylated fluorescein isothiocyanate-ATPase can form two-dimensional arrays in membranes, similar to those that were used previously to reconstruct from cryoelectron microscopy images the three-dimensional structure of Ca2+-free unphosphorylated ATPase.