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J Biol Chem. 2001 Jan 26;276(4):2953-60. Epub 2000 Oct 27.
Selectively suppressed Ca2+-induced Ca2+ release activity of alpha-ryanodine receptor (alpha-RyR) in frog skeletal muscle sarcoplasmic reticulum: potential distinct modes in Ca2+ release between alpha- and beta-RyR.

Murayama T, Ogawa Y.

Department of Pharmacology, Juntendo University School of Medicine, Tokyo 113-8421, Japan.

We reported earlier that the two ryanodine receptor (RyR) isoforms (alpha- and beta-RyR) purified from frog skeletal muscle were equipotent in the Ca(2+)-induced Ca(2+) release (CICR) activity (Murayama, T., Kurebayashi, N., and Ogawa, Y. (2000) Biophys. J. 78, 1810-1824). Whether this is also the case with the native Ca(2+) release channel in the sarcoplasmic reticulum (SR), however, remains to be determined. Taking advantage of the facts that [(3)H]ryanodine binds only to the open form of the channels and that it is practically irreversible at 4 degrees C, we devised a method to separate the total binding to contributions of alpha- and beta-RyR, using immunoprecipitation with an alpha-RyR-specific monoclonal antibody. Surprisingly, the binding of alpha-RyR was strongly suppressed to as low as approximately 4% that of beta-RyR in the SR vesicles. The two isoforms, however, showed no difference in sensitivity to Ca(2+), adenine nucleotides, or caffeine. This reduced binding of alpha-RyR was ascribed to the low affinity for [(3)H]ryanodine, with no change in the maximal binding sites. Solubilization of SR with 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonic acid partly remedied this nonequivalence, whereas 1 m NaCl was ineffective. 12-kDa FK506-binding protein (FKBP12), however, could not be responsible for it, because FK506 treatment did not eliminate the suppression, in contrast to marked removal of 12-kDa FK506-binding protein from alpha-RyR. These results suggest that alpha-RyR in the SR may serve Ca(2+) release in a mode other than CICR, being selectively suppressed in CICR.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11054412&dopt=Abstract

Anal Chem. 2000 Oct 15;72(20):5020-6.
Separation and identification of twelve catechins in tea using liquid chromatography/atmospheric pressure chemical ionization-mass spectrometry.

Zeeb DJ, Nelson BC, Albert K, Dalluge JJ.

Analytical Chemistry Division, National Institute of Standards and Technology, Gaithersburg, Maryland 20899-0001, USA.

A method has been developed for the direct microscale determination of 12 catechins in green and black tea infusions. The method is based on liquid chromatography/atmospheric pressure chemical ionization-mass spectrometry (LC/APCI-MS). Standard catechin mixtures and tea infusions were analyzed by LC/APCI-MS with detection of protonated molecular ions and characteristic fragment ions for each compound. The identities of eight major catechins and caffeine in tea were established based on LC retention times and simultaneously recorded mass spectra. In addition, monitoring of the catechin-specific retro Diels-Alder fragment ion at m/z 139 throughout the chromatogram provided a unique fingerprint for catechin content in the samples that led to the identification of four minor chemically modified catechin derivatives in the infusions. This report is the first to describe the comprehensive determination of all 12 reported catechins in a single analysis. The utility of LC/APCI-MS for providing routine separation and identification of catechins at femtomole to low-picomole levels without extraction or sample pretreatment, and its potential as a standard analytical tool for the determination of polyphenols in natural products and biological fluids, are discussed.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11055724&dopt=Abstract

Circ Res. 2000 Oct 27;87(9):774-80.
Sarcoplasmic reticulum Ca(2+) release causes myocyte depolarization. Underlying mechanism and threshold for triggered action potentials.

Schlotthauer K, Bers DM.

Department of Physiology, Loyola University Medical Center, Maywood, Illinois, USA.

Spontaneous sarcoplasmic reticulum (SR) Ca(2+) release causes delayed afterdepolarizations (DADs) via Ca(2+)-induced transient inward currents (I:(ti)). However, no quantitative data exists regarding (1) Ca(2+) dependence of DADs, (2) Ca(2+) required to depolarize the cell to threshold and trigger an action potential (AP), or (3) relative contributions of Ca(2+)-activated currents to DADs. To address these points, we evoked SR Ca(2+) release by rapid application of caffeine in indo 1-AM-loaded rabbit ventricular myocytes and measured caffeine-induced DADs (cDADs) with whole-cell current clamp. The SR Ca(2+) load of the myocyte was varied by different AP frequencies. The cDAD amplitude doubled for every 88+/-8 nmol/L of Delta[Ca(2+)](i) (simple exponential), and the Delta[Ca(2+)](i) threshold of 424+/-58 nmol/L was sufficient to trigger an AP. Blocking Na(+)-Ca(2+) exchange current (I(Na/Ca)) by removal of [Na](o) and [Ca(2+)](o) (or with 5 mmol/L Ni(2+)) reduced cDADs by >90%, for the same Delta[Ca(2+)](i). In contrast, blockade of Ca(2+)-activated Cl(-) current (I(Cl(Ca))) with 50 micromol/L niflumate did not significantly alter cDADs. We conclude that DADs are almost entirely due to I(Na/Ca), not I(Cl(Ca)) or Ca(2+)-activated nonselective cation current. To trigger an AP requires 30 to 40 micromol/L cytosolic Ca(2+) or a [Ca(2+)](i) transient of 424 nmol/L. Current injection, simulating I(ti)s with different time courses, revealed that faster I:(ti)s require less charge for AP triggering. Given that spontaneous SR Ca(2+) release occurs in waves, which are slower than cDADs or fast I(ti)s, the true Delta[Ca(2+)](i) threshold for AP activation may be approximately 3-fold higher in normal myocytes. This provides a safety margin against arrhythmia in normal ventricular myocytes.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11055981&dopt=Abstract

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