ExperientiaPub Date : 1996-06-15DOI: 10.1007/BF01969742
A R Dluzewski, C R Garcia
{"title":"Inhibition of invasion and intraerythrocytic development of Plasmodium falciparum by kinase inhibitors.","authors":"A R Dluzewski, C R Garcia","doi":"10.1007/BF01969742","DOIUrl":"https://doi.org/10.1007/BF01969742","url":null,"abstract":"<p><p>We have examined the effects of seven protein kinase inhibitors (staurosporine, genistein, methyl 2,5-dihydroxycinnamate, tyrphostins B44 and B46, lavendustin A and R03) on the erythrocytic cycle of the malaria parasite, Plasmodium falciparum. One (staurosporine) strongly inhibits serine/threonine kinases, but the remainder all exhibit a strong preference for tyrosine kinases. We have been able to discriminate between effects on invasion and on intraerythrocytic development. All reagents impeded development of intraerythrocytic parasites, though at widely differing concentrations, from the sub-micromolar to the millimolar. Several inhibitors, including staurosporine, also reduced invasion. The phosphatase inhibitor, okadaic acid, had a strong inhibitory effect both on invasion and development. The regulation of malaria development by phosphorylation or dephosphorylation reactions at several points in the blood-stage cycle is implied.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"621-3"},"PeriodicalIF":0.0,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969742","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19671350","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ExperientiaPub Date : 1996-06-15DOI: 10.1007/BF01969723
L Fucci, U Galderisi, M Piscopo, R del Gaudio, G Geraci
{"title":"In situ hybridization analysis of globin mRNAs in the primitive erythroid cells of the chick embryo.","authors":"L Fucci, U Galderisi, M Piscopo, R del Gaudio, G Geraci","doi":"10.1007/BF01969723","DOIUrl":"https://doi.org/10.1007/BF01969723","url":null,"abstract":"<p><p>The possibility that the minor embryonic chick hemoglobins might be present in a particular subgroup of primitive erythroid cells has been investigated by in situ hybridization. Probe to detect the mRNA for the alpha A globin chain of the minor embryonic hemoglobin was used, and the results of the hybridization were compared with those obtained using as probes the cDNAs for total globin mRNAs. All erythroid cells circulating in a 4-day-old chick embryo gave positive signals with both probes at an approximately constant ratio. This shows that all cells contain a similar assortment of hemoglobin types, excluding the possibility that a subgroup might contain the minor primitive hemoglobins exclusively. However, the cells are not homogeneous, since about 10% of them show a distinctly higher concentration of mRNA of all globin types.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"535-9"},"PeriodicalIF":0.0,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969723","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19672220","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ExperientiaPub Date : 1996-06-15DOI: 10.1007/BF01969734
M W Wichmann, R Zellweger, C M DeMaso, A Ayala, I H Chaudry
{"title":"Increased melatonin levels after hemorrhagic shock in male and female C3H/HeN mice.","authors":"M W Wichmann, R Zellweger, C M DeMaso, A Ayala, I H Chaudry","doi":"10.1007/BF01969734","DOIUrl":"https://doi.org/10.1007/BF01969734","url":null,"abstract":"<p><p>Although hemorrhagic shock leads to significant alterations of several hormones, e.g. ACTH, corticosterone and beta-endorphin, it is not known whether plasma melatonin levels are affected under this condition and if so, whether the effects are comparable in males and females. Using a radioimmunoassay, it was found that plasma melatonin levels were significantly increased in male and proestrus female C3H/HeN mice immediately after hemorrhagic shock. However, in male mice, by two hours after hemorrhage and resuscitation, plasma melatonin returned to levels comparable to those seen in control and sham-operated animals. Proestrus female mice, on the other hand, showed significantly increased plasma melatonin levels at two hours after surgery when compared to unoperated control animals. Although the significance and biological role of the transient increased plasma melatonin levels after hemorrhagic shock remain to be determined, it appears that the pineal gland and/or an extrapineal source of melatonin, of both male and proestrus female mice responds to severe hypotension by increased release of melatonin.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"587-90"},"PeriodicalIF":0.0,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969734","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19671343","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ExperientiaPub Date : 1996-06-15DOI: 10.1007/BF01969741
A B Attygalle, S R Smedley, T Eisner, J Meinwald
{"title":"Tocopheryl acetates from the pupal exocrine secretion of the squash beetle, Epilachna borealis (Coccinellidae).","authors":"A B Attygalle, S R Smedley, T Eisner, J Meinwald","doi":"10.1007/BF01969741","DOIUrl":"https://doi.org/10.1007/BF01969741","url":null,"abstract":"<p><p>The oily droplets on the pupal integumental hairs of the squash beetle Epilachna borealis contain a mixture of alpha-, beta-, gamma-, and delta-tocopheryl acetates as major constituents. In addition, the secretion contains a number of minor components that appear to be dehydrocongeners of the major components. This is the first report of the occurrence of acetate esters of any tocopherol in nature.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"616-20"},"PeriodicalIF":0.0,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969741","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19671349","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ExperientiaPub Date : 1996-06-15DOI: 10.1007/BF01969730
R G Duggleby, H L Peng, H Y Chang
{"title":"An improved assay for UDPglucose pyrophosphorylase and other enzymes that have nucleotide products.","authors":"R G Duggleby, H L Peng, H Y Chang","doi":"10.1007/BF01969730","DOIUrl":"https://doi.org/10.1007/BF01969730","url":null,"abstract":"<p><p>UDPglucose pyrophosphorylase catalyses the interconversion UDPglucose plus pyrophosphate and glucose 1-phosphate plus UTP. Several assay methods for this enzyme have been described but the only one that can be used to investigate the specificity with respect to various UDPsugars is based on coupling to UTP formation. This assay employs phosphoglycerate kinase to catalyse the formation 1,3- bisphosphoglycerate which is then used to oxidise NADH in the presence of glyceraldehyde 3-phosphate dehydrogenase. We have found that the activity of phosphoglycerate kinase towards UTP is low which limits the usefulness of the assay to very low rates, in agreement with the published recommendation of Hansen et al. Here it is shown that the dynamic range of the assay is increased by more than five fold on addition of nucleoside diphosphate kinase and ADP, which convert UTP to the preferred phosphoglycerate kinase substrate, ATP. It is also shown that the improved assay is suitable for enzymes with other nucleotide triphosphate products.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"568-72"},"PeriodicalIF":0.0,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969730","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19672102","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ExperientiaPub Date : 1996-06-15DOI: 10.1007/BF01969747
D A Lightner, D L Holmes, A F McDonagh
{"title":"Dissociation constants of water-insoluble carboxylic acids by 13C-NMR. pK(a)s of mesobiliverdin-XIII alpha and mesobilirubin-XIII alpha.","authors":"D A Lightner, D L Holmes, A F McDonagh","doi":"10.1007/BF01969747","DOIUrl":"https://doi.org/10.1007/BF01969747","url":null,"abstract":"<p><p>High-field 13C-NMR of 13C-enriched compounds in dilute aqueous d6-Me2-SO solutions provides a simple, accurate method for measuring pK(a)s of sparingly soluble carboxylic acids. Using this method, we found the pK(a)s of mesobilirubin-XIII alpha to be 4.2 and 4.9, much lower values than reported recently for bilirubin, and of mesobiliverdin-XIII alpha to be 3.9 and 5.3.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"639-42"},"PeriodicalIF":0.0,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969747","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19671351","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ExperientiaPub Date : 1996-06-15DOI: 10.1007/BF01969731
H Haraguchi, H Ishikawa, S Sakai, B P Ying, I Kubo
{"title":"Inhibition of lipid peroxidation by diterpenoid from Podocarpus nagi.","authors":"H Haraguchi, H Ishikawa, S Sakai, B P Ying, I Kubo","doi":"10.1007/BF01969731","DOIUrl":"https://doi.org/10.1007/BF01969731","url":null,"abstract":"<p><p>A diterpenoid, totarol (1), from Podocarpus nagi was evaluated as an antioxidant. This diterpenoid inhibited autoxidation of linoleic acid. Mitochondrial and microsomal lipid peroxidation induced by Fe(III)-ADP/NADH or Fe(III)-ADP/NADPH were also inhibited. Nagilactone E (2), a norditerpene lactone isolated from the same source, had no antioxidative activity. Furthermore, totarol protected red cells against oxidative hemolysis. This diterpene was shown to be effective in protecting biological systems against oxidative stresses.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"573-6"},"PeriodicalIF":0.0,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969731","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19672103","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ExperientiaPub Date : 1996-06-15DOI: 10.1007/BF01969722
I K Takeuchi, Y K Takeuchi, Y Murashima, A Seto-Ohshima
{"title":"Altered axon terminals containing concentric lamellar bodies of cerebellar Purkinje cells in Mongolian gerbil.","authors":"I K Takeuchi, Y K Takeuchi, Y Murashima, A Seto-Ohshima","doi":"10.1007/BF01969722","DOIUrl":"https://doi.org/10.1007/BF01969722","url":null,"abstract":"<p><p>Altered axon terminals containing concentric lamellar bodies were observed in cerebellar and vestibular nuclei of the Mongolian gerbil. The terminals increased in number from 30 days of age onward, and reached about tenfold at 360 days. The numbers were the same in two gerbil strains with different susceptibility to spontaneous motor seizures by various stimuli, but about threefold those in Slc:Wistar rat.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"531-4"},"PeriodicalIF":0.0,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969722","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19672219","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ExperientiaPub Date : 1996-06-15DOI: 10.1007/BF01969729
H Haraguchi, I Ohmi, H Masuda, Y Tamura, K Mizutani, O Tanaka, W H Chou
{"title":"Inhibition of aldose reductase by dihydroflavonols in Engelhardtia chrysolepis and effects on other enzymes.","authors":"H Haraguchi, I Ohmi, H Masuda, Y Tamura, K Mizutani, O Tanaka, W H Chou","doi":"10.1007/BF01969729","DOIUrl":"https://doi.org/10.1007/BF01969729","url":null,"abstract":"<p><p>Astilbin and neoastilbin, dihydroflavonol rhamnosides from Engelhardtia chrysolepis, showed potent inhibition of lens aldose reductase. Kinetic analysis showed astilbin exhibited uncompetitive inhibition against both dl-glyceraldehyde and NADPH. These taxifolin glycosides were selective inhibitors of aldose reductase with no inhibition of NADH oxidase.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"564-7"},"PeriodicalIF":0.0,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969729","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19672101","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ExperientiaPub Date : 1996-06-15DOI: 10.1007/BF01969732
P de Martino Rosaroll, P Venditti, S Di Meo, T De Leo
{"title":"Effect of cold exposure on electrophysiological properties of rat heart.","authors":"P de Martino Rosaroll, P Venditti, S Di Meo, T De Leo","doi":"10.1007/BF01969732","DOIUrl":"https://doi.org/10.1007/BF01969732","url":null,"abstract":"<p><p>Male rats exposed to the cold (4 degrees C) for five or ten days exhibited modifications in their thyroid state, as documented by increases in serum thyroid hormone levels, to which differently graded modifications of heart weight/body weight ratio, heart rate, and resting metabolic rate were associated. The values of the above mentioned thyroid state indicators returned to those of the control when the animals, kept at cold for ten days, were re-exposed to room temperature (24 degrees C) for an additional 10 days. The configuration of action potentials, recorded in vitro at 26 degrees C from fibres of anterior papillary muscles, was different in control rats of different age and was affected by prolonged cold exposure. In fact, the action potential duration (APD) increased after ten days of cold exposure. In the re-exposed group the APD was not different from that of the controls. Such a pattern was not significantly modified when the stimulation frequency increased from 1 Hz to 5 Hz. The above results suggest that in cold exposure, as in experimental hyperthyroidism, thyroid hormone might exert a cardiac chronotropic effect by modifying heart electrophysiological properties. Thus thyroid hormone should play a basic role during the exposure to cold environment, stimulating the body metabolism and increasing heart rate as a response to the requirement for greater tissue perfusion.</p>","PeriodicalId":12087,"journal":{"name":"Experientia","volume":"52 6","pages":"577-82"},"PeriodicalIF":0.0,"publicationDate":"1996-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01969732","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19672104","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}