Disease relevance of Triftazin

• Trifluoperazine reversal of secretory diarrhea in pancreatic cholera [1].
• Neither catatonic rigidity nor akinesia before treatment was predictive of a parkinsonian response to trifluoperazine, but pretreatment tremor may have been [2].
• In the studies presented here, we found that several phenothiazines, including trifluoperazine, chlorpromazine, prochlorpromazine, and promethazine, blocked EBV infectivity of isolated adult human B cells as measured either by outgrowth of transformed cell colonies or by [3H]thymidine incorporation [3].
• The MTD of trifluoperazine was 60 mg/d, with dose-limiting toxicity being extrapyramidal side effects [4].
• Effect of malignant transformation, retinoic acid, trifluoperazine, and N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W7) on the sensitivity of rodent cells to Pseudomonas toxin [5].

Psychiatry related information on Triftazin

• Before and during a standardized course of trifluoperazine therapy, 18 schizophrenic patients underwent repeated examinations for extrapyramidal motor signs, clinical psychopathology, and urinary excretion of free and conjugated forms of dopamine and its metabolites [2].
• Effective short-term treatment of generalized anxiety disorder with trifluoperazine [6].
• After 2 weeks of treatment an inverted U-shaped relationship was found between change scores on the Brief Psychiatric Rating Scale and trifluoperazine plasma levels [7].
• Management of behavioral symptoms in disturbed elderly patients: comparison of trifluoperazine and haloperidol [8].
• A dose-response curve was established for the effect of i.p. injections of trifluoperazine (TFP) on spontaneous locomotor activity [9].

High impact information on Triftazin

• Stelazine, a phenothiozine which binds to calmodulin, prevented the interaction of CaM-RITC with mitochondrial sites [10].
• However, we find that antagonism of calmodulin by trifluoperazine does not prevent the association of the other cytosolic proteins with the chromaffin granule membrane [11].
• The calmodulin inhibitor trifluoperazine inhibited adhesion of MB6A cells more strongly than that of TA3 cells [12].
• The calmodulin antagonists, trifluoperazine (10(-5) M), pimozide (10(-5) M), and the naphthalene sulfonamides, W-7 and W-13 (10(-5) M), inhibited gastrin-stimulated HIP by 45.6 38.5, 42.3, and 37.2%, respectively [13].
• Trifluoperazine inhibits the contraction of cultured rat cardiac cells and the phosphorylation of myosin light chain [14].

Chemical compound and disease context of Triftazin

• Diarrhea in a patient with pancreatic cholera syndrome caused by a vasoactive intestinal polypeptide producing pancreatic islet-cell carcinoma responded rapidly and dramatically to the phenothiazine trifluoperazine [1].
• Bone resorption was reversibly inhibited by tamoxifen, 4-hydroxytamoxifen, and trifluoperazine with IC50 values of approximately 1 microM [15].
• Cyclosporin A and trifluoperazine inhibit this pore and block necrotic cell death in oxidative stress, Ca2+ ionophore toxicity, Reye-related drug toxicity, pH-dependent ischaemia/reperfusion injury and other models of cell injury [16].
• Treatment of human MCF-7 breast cancer cells with chemosensitizers (CS), such as verapamil, trifluoperazine or BSO, for 72 hr resulted in an enhanced sensitization of cells to Adriamycin, trifluoperazine being the most potent compound in the reversion of chemoresistance [17].
• Phase II trial of doxorubicin and trifluoperazine in metastatic breast cancer [18].

Biological context of Triftazin

• To determine the site of calcium's action in the toad urinary bladder, we examined the effect of trifluoperazine, a compound that binds specifically to the calcium binding protein, calmodulin, and thereby prevents activation of enzymes by the calcium- calmodulin complex [19].
• The mobility of LRB-CM in the cytoplasm was sensitive to treatment of the cells with trifluoperazine, which suggests that at least some of the intracellular binding sites are specific for calmodulin in the calcium-bound form [20].
• Current responses to AED were blocked by W7 or trifluoperazine, while exocytosis remained unaffected [21].
• Trifluoperazine inhibits phagocytosis in a macrophagelike cultured cell line [22].
• In addition, Stelazine inhibits an alternate pathway of endocytosis that does not involve coated vesicle formation [23].

Anatomical context of Triftazin

• Possible role for calmodulin in insulin release. Studies with trifluoperazine in rat pancreatic islets [24].
• In vitro antisecretory effects of trifluoperazine and other neuroleptics in rabbit and human small intestine [25].
• In human small intestinal mucosa, trifluoperazine (0.1-0.5 mM) inhibited electrical responses to VIP and theophylline almost completely [25].
• Trifluoperazine, a drug that binds to Ca2+-calmodulin and inhibits its interaction with other proteins, was found to inhibit growth and phagocytosis in a macrophagelike cell line, J774.16 [22].
• In brush borders treated with calcium and trifluoperazine to solubilize CM, precise arrangement and morphology of lateral bridges was unperturbed, but ATP treatment would no longer solubilize the 110-kdalton protein [26].

Associations of Triftazin with other chemical compounds

• The C-kinase inhibitors chlorpromazine and trifluoperazine inhibit the phorbol diester stimulated phosphorylation of site T3 in a dose-dependent manner [27].
• A preferential positional shift toward the cathode was observed which was inhibited by the calcium channel blocker D-600 and the calmodulin antagonist trifluoperazine [28].
• Mediation by protein kinase C is suggested by three findings: (a) 1-oleoyl-2-acetylglycerol also activated the antiport; (b) trifluoperazine, an inhibitor of protein kinase C, blocked the stimulation of Na+/H+ exchange; and (c) activation of countertransport was accompanied by increased phosphorylation of specific membrane proteins [29].
• Infiltration of compound eyes of crayfish, Cherax destructor, with the thiol protease inhibitor Ep-475 or with trifluoperazine prior to fixation for electron microscopy was found to stabilize an axial filament of 6-12 nm diam within each rhabdomeral microvillus of the photoreceptors [30].
• The CaM antagonists calmidazolium and trifluoperazine as well as the CaM-binding protein calcineurin inhibited the EDRF/NO synthesis by both the cytosolic and the particulate enzyme [31].

Gene context of Triftazin

• The combination of the MPT inhibitors, cyclosporin A, and trifluoperazine, protected Ad5IkappaB-infected hepatocytes from TNFalpha-mediated apoptosis [32].
• In contrast, trifluoperazine, an antagonist of calcium/calmodulin kinases, completely blocked H(2)O(2)-induced eIF4E phosphorylation [33].
• Relationship between expression of P-glycoprotein and efficacy of trifluoperazine in multidrug-resistant cells [34].
• NGMMA and NG-nitro-arginine, competitive inhibitors of NOS, diminished the accumulation of nitrite, but calmodulin antagonists (trifluoperazine, W-5 and W-7) had little or no inhibitory effect [35].
• A high-copy suppressor gene, HST1, for the TFP and Ca2+ sensitivities of ssd1 null mutant was cloned and sequenced [36].

Analytical, diagnostic and therapeutic context of Triftazin

• Trifluoperazine, W-7, cytochalasin D, and taxol also block DNA synthesis in response to EGF as measured by autoradiography using [3H]thymidine [37].
• Previous studies showed that, upon Ca2+ binding, calsequestrin undergoes a conformational change, burying the trifluoperazine-binding site, folding into a more compact structure that is trypsin-resistant, and increasing the negative ellipticity of the circular dichroism spectrum [38].
• Microcalorimetric titrations of calmodulin with Ca2+ and trifluoperazine (TFP) at various molar ratios have been carried out at 25 degrees C and at pH 7 [39].
• The two proteins were purified by TFP affinity chromatography [40].
• Previous sequence analysis suggested that calsequestrin may contain a hydrophobic binding site for the drug trifluoperazine, a site shared by the calmodulin family and shown to play a role in calmodulin/calmodulin receptor interaction [38].

References