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Biophys J. 2000 Nov;79(5):2509-25.
Divergent functional properties of ryanodine receptor types 1 and 3 expressed in a myogenic cell line.

Fessenden JD, Wang Y, Moore RA, Chen SR, Allen PD, Pessah IN.

Department of Molecular Biosciences, School of Veterinary Medicine, University of California Davis, Davis, California 95616, USA.

Of the three known ryanodine receptor (RyR) isoforms expressed in muscle, RyR1 and RyR2 have well-defined roles in contraction. However, studies on mammalian RyR3 have been difficult because of low expression levels relative to RyR1 or RyR2. Using the herpes simplex virus 1 (HSV-1) helper-free amplicon system, we expressed either RyR1 or RyR3 in 1B5 RyR-deficient myotubes. Western blot analysis revealed that RyR1- or RyR3-transduced cells expressed the appropriate RyR isoform of the correct molecular mass. Although RyR1 channels exhibited the expected unitary conductance for Cs(+) in bilayer lipid membranes, 74 of 88 RyR3 channels exhibited pronounced subconductance behavior. Western blot analysis with an FKBP12/12.6-selective antibody reveals that differences in gating behavior exhibited by RyR1 and RyR3 may be, in part, the result of lower affinity of RyR3 for FKBP12. In calcium imaging studies, RyR1 restored skeletal-type excitation-contraction coupling, whereas RyR3 did not. Although RyR3-expressing myotubes were more sensitive to caffeine than those expressing RyR1, they were much less sensitive to 4-chloro-m-cresol (CMC). In RyR1-expressing cells, regenerative calcium oscillations were observed in response to caffeine and CMC but were never seen in RyR3-expressing 1B5 cells. In [(3)H]ryanodine binding studies, only RyR1 exhibited sensitivity to CMC, but both RyR isoforms responded to caffeine. These functional differences between RyR1 and RyR3 expressed in a mammalian muscle context may reflect differences in association with accessory proteins, especially FKBP12, as well as structural differences in modulator binding sites.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11053126&dopt=Abstract

Ultrasound Med Biol. 2000 Sep;26(7):1145-51.
Transcranial Doppler blood velocity measurement--the effect of changes in velocity profile.

Lunt MJ, Jenkinson DF, Kerr D.

Department of Clinical Measurement, Royal Bournemouth Hospital, Castle Lane East, Bournemouth, UK. michael.lunbch-tr.swest.nhs.uk

Transcranial Doppler (TCD) units measure blood velocity in the middle cerebral artery (MCA) and are used to examine the effects of pharmacological agents. The units actually measure the average of the maximum blood velocity envelope (aveV(max)) and it is assumed that changes in aveV(max) follow changes in the true mean velocity (aveV(mean)). This may not be true if there are changes in velocity profile. Results from previous TCD studies using acetazolamide (ACZ) and caffeine were examined for evidence for changes in velocity profile. ACZ increased aveV(max) by 21% (95% CI 13 to 29%) and aveV(mean) by 14% (95% CI 9 to 19%). Caffeine decreased aveV(max) by 8% (95% CI 4 to 12%) and aveV(mean) by 5% (95% CI 4% increase to 13% decrease). In both cases, the true change, measured using aveV(mean) was lower, indicating possible changes in velocity profile. We conclude that the possibility of changes in velocity profile must be considered when using TCD to quantify changes in blood velocity.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11053749&dopt=Abstract

Br J Haematol. 2000 Sep;110(4):819-25.
Activation of an ataxia telangiectasia mutation-dependent intra-S-phase checkpoint by anti-tumour drugs in HL-60 and human lymphoblastoid cells.

Sugimoto K, Tamayose K, Takagi M, Yamada K, Sasaki M, Mizutani S, Oshimi K.

Department of Haematology, Juntendo University School of Medicine, Tokyo, Japan. ksugimoed.juntendo.ac.jp

In yeast cells, the intra-S-phase checkpoint slows down the rate of DNA replication in response to DNA damage. Here we showed that a similar checkpoint mechanism is present and activated by anti-tumour drugs in HL-60 and Epstein-Barr virus (EBV)-transformed human lymphoblastoid cells. Using bromodeoxyuridine (BrdU) pulse labelling combined with two-dimensional flow cytometric analysis, we clearly visualized the cell-cycle progression of the BrdU-positive population (cells originally belonging to the S phase) and detected even subtle changes in S-phase progression induced by mild drug treatment conditions free of apoptosis. The DNA topoisomerase II inhibitors, doxorubicin and etoposide (250 nmol/l and 400 nmol/l, respectively, for 8 h), retained the BrdU-positive HL-60 cells in the latter half of S and G2/M positions, and the pyrimidine analogue anti-metabolite, cytosine beta-D-arabinofuranose (Ara-C; 50 nmol/l), kept them in early-to-late S phase after 8 h of incubation. Because 10 micromol/l of caffeine added 2 h later attenuated the S-phase retardation by these drugs in HL-60 cells, slowing of the S-phase progression should be actively regulated. Furthermore, two ataxia telangiectasia (AT)-derived lymphoblastoid cell lines were impaired in the doxorubicin-induced S-phase retardation, which indicated that the process is at least partially dependent on ataxia telangiectasia mutated (ATM) gene product. The inhibitory mechanism on S-phase progression elicited by anti-tumour drugs in HL-60 and lymphoblastoid cells may therefore correspond to the intra-S-phase checkpoint of the yeast cells.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11054063&dopt=Abstract

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