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C K Wang

Publications and source records attributed to C K Wang.

103 records · Page 6Linked to original sources
PubMed1986

Proximity relationship in the binary complex formed between troponin I and troponin C.

We have determined six molecular distances among four sites in the binary complex formed between troponin C (TnC) and troponin I (TnI) by fluorescence resonance energy transfer between donor and acceptor probes that were either an intrinsic fluorophore (Trp158 of TnI) or extrinsic probes attached to the sites. The three extrinsic probes were dansylaziridine (DNZ), N'-(iodoacetyl)-N'-(8-sulfo-1-naphthyl)ethylenediamine (IAEDANS) and 5-(iodoacetamido)eosin (IAE). The four fluorophores provided four donor-acceptor pairs: DNZ----IAE, Trp----IAEDANS, IAEDANS----IAE, and Trp----DNZ. They allowed determinations of separations between specific sites from measurements of energy transfer from (1) Met25 (DNZ) to Cys98 (IAE) in TnC, (2) Trp158 to Cys133 (IAEDANS) in TnI, (3) Cys98 (IAEDANS) of TnC to Cys133(IAE) of TnI, (4) Trp158 of TnI to Cys98(IAEDANS) of TnC, and (6) Met25(DNZ) of TnC to Cys133(IAE) of TnI. Distance (1) in TnC was little affected when the isolated protein was complexed with TnI, whereas distance (2) in TnI increased by 6A (29%) when TnI was incorporated into the binary complex. In the presence of EGTA, the six donor-acceptor separations (R) in the complex were in the range 28 to 57 A based on kappa 2 = 2/3. Mg2+ had only small effects on R, but Ca2+ induced substantial increases or decreases of R in five of the six distances. These changes were not accompanied by significant changes in the axial depolarization of the fluorophores. The results indicate global structural perturbations of regions of the two proteins in the complex by Ca2+ binding to the TnC, and suggest that large-scale movements of domains of troponin subunits may be the initial molecular events that occur in the transmission of the Ca2+ signal in the regulation of contraction by calcium.

Adenosine Triphosphatases↗
PubMed1985

Energetics of the binding of calcium and troponin I to troponin C from rabbit skeletal muscle.

We determined the free energy of interaction between rabbit skeletal troponin I (TNI) and troponin C (TNC) at 10 degrees and 20 degrees C with fluorescently labeled proteins. The sulfhydryl probe 5-iodoacetamidoeosin (IAE) was attached to cysteine (Cys)-98 of TNC and to Cys-133 of TNI, and each of the labeled proteins was titrated with the other unlabeled protein. The association constant for formation of the complex between labeled TNC (TNC*) and TNI was 6.67 X 10(5) M-1 in 0.3 M KCl, and pH 7.5 at 20 degrees C. In the presence of bound Mg2+, the binding constant increased to 4.58 X 10(7) M-1 and in the presence of excess of Ca2+, the association constant was 5.58 X 10(9) M-1. Very similar association constants were obtained when labeled TNI was titrated with unlabeled TNC. The energetics of Ca2+ binding to TNC* and the complex TNI X TNC* were also determined at 20 degrees C. The two sets of results were used to separately determine the coupling free energy for binding TNI and Mg2+, or Ca2+ to TNC. The results yielded a total coupling free energy of -5.4 kcal. This free energy appeared evenly partitioned into the two species: TNI X TNC(Mg)2 or TNI X TNC(Ca)2, and TNI X TNC(Ca)4. The first two species were each stabilized by -2.6 kcal, with respect to the Ca2+ free TNI X TNC complex, and TNI X TNC(Ca)4 was stabilized by -2.8 kcal, respect to TNI X TNC(Ca)2 or TNI X TNC(Mg)2. The coupling free energy was shown to produce cooperatively complexes formed between TNI and TNC in which the high affinity sites were initially saturated as a function of free Ca2+ to yield TNI X TNC(Ca)4. This saturation occurred in the free Ca2+ concentration range 10(-7) to 10(-5) M. The cooperative strengthening of the linkage between TNI and TNC induced by Ca2+ binding to the Ca2+-specific sites of TNC may have a direct relationship to activation of actomyosin ATPase. The nature of the forces involved in the Ca2+-induced strengthening of the complex is discussed.

Animals↗
PubMedDate not supplied

Chemical composition and toxicity of Taiwanese betel quid extract.

In this genotoxic study, the Ames Salmonella microsome test showed that an aqueous extract of betel quid did not induce mutagenicity in Salmonella typhimurium strains TA98 and TA100. Mammalian cell studies (Chinese hamster ovary K1 cell; CHO-K1 cell) revealed that only higher concentrations (100 and 1000 microg/ml) of aqueous extract weekly increased the frequencies of sister-chromatid exchange (SCE) in the absence of S9. Animal (male Sprague-Dawley rat) studies showed that low-dose feeding (0.53 g dry aqueous extract/kg diet) significantly increased the activities of glutathione (GSH) peroxidase and cytoplasmic glutathione S-transferase (cGST) of liver, high-dose feeding (26.5 g dry aqueous extract/kg diet) lowered the contents of GSH and total glutathione. The effect of an aqueous extract of betel quid on the oxidation of 2'-deoxyguanosine (2'-dG) to 8-hydroxy-2'-deoxyguanosine (8-OH-dG) evaluated that this aqueous extract may act as a pro-oxidant at lower dosage and may be dependent on the iron ions in the model system. However, the aqueous extract of betel quid showed antioxidant activity at higher doses by the ability of the scavenging effect of the hydroxyl radicals.

Alkaloids↗
PubMedDate not supplied

Enhancement of a 252Cf-based neutron beam via subcritical multiplication for neutron capture therapy.

Previous studies indicated that an epithermal-neutron beam based on bare 252Cf is not feasible for neutron capture therapy (NCT). It was reported that a clinically useful epithermal-neutron beam requires a minimum of 1.0 g of 252Cf, which is more than twice the US current annual supply. However, it was reasoned that the required quantity of 252Cf could be dramatically reduced when used with a subcritical multiplying assembly (SMA). This reasoning is based on the assumption that the epithermal-neutron beam intensity for NCT is directly proportional to the fission neutron population, and that the neutron multiplying factor of the SMA can be estimated by 1/(1 - k(eff)). We have performed detailed Monte Carlo calculations to investigate the validity of the above reasoning. Our results show that 1/(1 - k(eff)) grossly overestimates the beam enhancement factor for NCT. For example, Monte Carlo calculations predict a beam enhancement factor of 6.0 for an optimized SMA geometry with k(eff) = 0.968. This factor is much less than 31 predicted by 1/(1 - k(eff)). The overestimation is due to the fact that most of the neutrons produced in the SMA are self-shielded, whereas self-shielding is negligible in a bare 252Cf source. Since the beam intensity of a 0.1 g 252Cf with the optimized SMA enhancement is still more than an order of magnitude too low compared to the existing reactor beams, we conclude that the enhancement via an SMA for a 252Cf-based epithermal-neutron beam is inadequate for NCT.

Californium↗
PubMedDate not supplied

Cell culture studies of a carborane cholesteryl ester with conventional and PEG liposomes.

A new cholesterol-carborane conjugate (BCH) has been synthesized as a potential targeting agent for boron neutron capture therapy (BNCT) of cancers. The compound is extremely water insoluble and was formulated in two liposomal formulations to determine if the compound could be adequately taken up by 9L rat glioma cells in cell culture. Several factors potentially affecting the cellular uptake were evaluated, such as concentration of BCH in the incubation medium, incubation time, cell confluence, and the addition of polyethylene glycol (PEG) phospholipids to the liposomal formulation. The studies indicated that the cellular uptakes of BCH in the conventional and PEG liposomal formulations were 49.1 and 45.9 microg boron/g cells, respectively. Therefore, this compound, formulated in both liposomal formulations, delivered sufficient levels of boron to cancer cells in vitro, indicating that BCH is a promising approach for use in BNCT. The uptake appeared to depend upon BCH concentration in the media as well as the confluence of the cells. The greater boron uptake by nonconfluent cells indicated that active growth of cells was a factor in the uptake of this compound.

Animals↗
PubMedDate not supplied

Dynamic contrast-enhanced subtraction and delayed MRI of gastric tumors: radiologic-pathologic correlation.

PURPOSE: Our goal was to determine whether dynamic MR subtraction images could be used to detect and stage gastric tumors. METHOD: Dynamic MR subtraction images were prospectively performed in 20 patients without gastric lesions and in 39 patients with gastric tumors. The flat- or depressed-type early gastric cancers were excluded. The MR findings were assessed for layered pattern of the normal gastric wall, detectability of tumors, enhanced pattern of tumor, and depth of the tumor invasion. Surgical specimens were obtained from 30 of the patients with tumors, and histopathologic sections were made in the dynamic MR scanning direction. RESULTS: The three-layered structure of the normal gastric wall was apparent in more of the dynamic MR subtraction images (60%) than of the nonsubtraction images (30%) in the control group. All 39 gastric tumors were detected by MRI. The intact inner layers overlying stromal tumors and outer layers interrupted by advanced gastric cancers were clear on the subtracted images. MRI accurately T-staged 88% of the gastric cancers. CONCLUSION: Dynamic MR subtraction images can be used to identify gastric tumors and to stage gastric cancers.

Adult↗