Effects of ondansetron on chemotherapy-induced acute and delayed emesis--a pilot study.
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Adult↗
Biomedical subjects
S Johansson
Publications and source records attributed to S Johansson.
IgE-binding components in Pityrosporum orbiculare identified by an immunoblotting technique.
IgE-binding components in crude extracts of Pityrosporum orbiculare were separated by sodium dodecylsulphate polyacrylamide gel electrophoresis and transferred to Immobilon membrane. The components were detected by P. orbiculare radioallergosorbent (RAST) positive sera (class 2-4) from 37 patients with atopic dermatitis and visualized by enzyme-labelled anti-human IgE antibodies in chromogenic substrate. Numerous IgE-binding compounds were demonstrated in the molecular weight (MW) range of 14-94 kD. Eight of them were characterized to molecular size, frequency of reacting sera and intensity of bands. Six of the defined components were found to be major allergens reacting with more than 50% of the sera. They had MWs 86, 76, 67, 28, 17 and 13 kD. Thirty-six of the 37 patients had elevated total serum IgE. Two other patient categories were studied; 11 patients with lymphatic filariasis (high total serum IgE, greater than 1,300 kU/l) and 15 pityriasis versicolor patients (normal total serum IgE, less than 122 kU/l). The P. orbiculare RAST values for these sera showed good accordance with the reactivity in immunoblotting experiments.
Adult↗
Single-channel and whole-cell currents in rat cerebellar granule cells.
The patch-clamp technique was used to study both whole-cell and single-channel currents in cultured rat cerebellar granule cells. In whole-cell recordings under voltage-clamp conditions 3 types of current were found; a transient inward sodium current and a transient and a sustained outward potassium current. Single-channel currents were recorded from both inside-out and outside-out membrane patches. Three types of potassium channel were identified; two non-inactivating channels with unit conductances of 160 and 60 pS and one inactivating channel of 20 pS. No calcium currents were detected.
Action Potentials↗
Graded action potentials in small cultured rat hippocampal neurons.
The 'all-or-nothing' principle has been central to neurobiology since the beginning of this century. We here demonstrate that action potentials in small cultured neurons from the hippocampus of rat embryos clearly depend on stimulus strength and thus deviate from this principle. We also demonstrate that similar stimulus-dependent action potentials can be predicted from computations based on voltage-clamp measurements. The findings suggest that amplitude modulation of the action potential may be a principle for information processing in the mammalian nervous system.
Action Potentials↗
[Ethics in conflict with the law in connection to home care. Personnel often sacrifice, their interests].
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Ethics, Medical↗
[To withdraw life-saving treatment--clear guidelines are needed].
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Aged↗
Characterization of a laminin receptor on rat hepatocytes.
The interaction of rat hepatocytes with laminin was studied. The cells were found to adhere to the distal half of the long arm in the laminin molecule (fragment E8), in addition to the previously identified site in the central cross of laminin (fragment P1). Attachment to laminin and to each of the two cell-binding fragments was inhibited by antibodies against the integrin beta 1-subunit of the fibronectin receptor, but not by the cell-binding peptide of fibronectin (Gly-Arg-Gly-Asp-Ser-Cys). By affinity chromatography on laminin-Sepharose in the presence of 2 mM Mn2+, the beta 1-subunit was isolated together with an alpha-subunit with an unreduced Mr of 180,000. This laminin-binding integrin did not bind to Sepharose conjugated with a 105-kDa cell-binding fragment of fibronectin and conversely, the fibronectin receptor of the cells (integrin alpha 5 beta 1) did not bind to the laminin-Sepharose. The 180-kDa protein was identified as the integrin subunit alpha 1 based on its specific reactivity with antibodies raised against a peptide of the N-terminal part of human alpha 1. Integrin alpha 1 beta 1 was found to bind at physiological ionic strength also to Sepharose conjugated with either one of the laminin fragments P1 or E8. Furthermore, integrin alpha 1 beta 1 isolated on one of the fragment columns could be shown to rebind to the other fragment-Sepharose. The results indicate that two structurally distinct domains of laminin may interact with the same type of receptor on hepatocytes.
Amino Acid Sequence↗
Comparison and functional characterization of C-CAM, glycoprotein IIb/IIIa and integrin beta 1 in rat platelets.
Three adhesion-related proteins in rat platelets were compared, namely C-CAM, gpIIb/IIIa, and integrin beta 1. These three proteins behaved as distinct components as judged by both biochemical and immunological analyses. GpIIb/IIIa bound to a GRGDSPC-peptide, but neither beta 1-containing integrins nor C-CAM had any affinity either for this peptide or for a large cell-binding fragment of fibronectin. C-CAM and integrin beta 1 behaved differently when platelets were labeled with 125I, solubilized by detergent, and immunoprecipitated. Significant amounts of labeled C-CAM was precipitated when the platelets were first solubilized with detergent and then 125I-labeled. Almost no labeled C-CAM could be precipitated when intact platelets, that were unactivated or activated by ADP, were labeled. In contrast, labeled integrin beta 1 was immunoprecipitated when unactivated platelets were surface-labeled. However, when platelets that were activated by ADP and calcium ions were labeled almost no labeled integrin beta 1 could be immunoprecipitated. These data indicate 1) that C-CAM in intact platelets is inaccessible to surface-labeling and 2) that beta 1 integrin is less accessible to surface-labeling after platelet activation in the presence of calcium ions.
Adenosine Triphosphatases↗
Similar induction of the hepatic EGF receptor in vivo by EGF and partial hepatectomy.
A 2-fold increase in the level of epidermal growth factor (EGF) receptor mRNA accompanied by a similar increase in newly synthesized ligand-binding EGF-receptors was observed 2-4 h after intraportal EGF-injections and 2-4 h after partial hepatectomy. After this initial increase, the EGF-receptor levels decreased back to control levels 6-8 h after EGF-injections and below control levels 6-8 h after partial hepatectomy. EGF was also found to influence the degradation of endocytosed [125I]-EGF 3 h after injection to a similar extent as partial hepatectomy. The similar effects of EGF and partial hepatectomy suggests that EGF or EGF-like factors may be mechanistically involved in the early "promotion" stage during the pre-replicative phase of liver regeneration. The EGF-induced effects are, however, at least not alone responsible for the replicative process.
Animals↗
Pretranslational and posttranslational regulation of the EGF receptor during the prereplicative phase of liver regeneration.
We studied the regulation of the epidermal growth factor receptor mRNA and the number of epidermal growth factor binding sites in subcellular compartments involved in the biosynthesis and endocytosis of the epidermal growth factor receptor during the prereplicative phase of liver regeneration. The epidermal growth factor receptor mRNA, quantified by solution hybridization, decreased after partial hepatectomy, with a nadir of about 35% 18 hr after hepatectomy. An even stronger decrease in the number of epidermal growth factor binding sites after partial hepatectomy was observed in a Golgi-enriched low-density membrane fraction, reflecting available newly synthesized epidermal growth factor receptors. It is suggested that this decrease in newly synthesized available epidermal growth factor receptors is caused primarily, but not entirely, by decreased epidermal growth factor receptor mRNA levels and the additional down-regulation of epidermal growth factor binding sites may involve posttranslational mechanisms such as intracellular occupation by transforming growth factor-alpha. The observation that the number of specific epidermal growth factor binding sites after partial hepatectomy was only moderately reduced in prelysosomal endosomes and in lysosomes, compared with the newly synthesized receptors, may indicate that a pool of receptors targeted for lysosomes exists and these receptors are regulated in a different manner than the receptor pool targeted for the cell surface. Furthermore, at least two separable endocytic subcompartments are involved in the transport of the epidermal growth factor/epidermal growth factor receptor complex in the liver.(ABSTRACT TRUNCATED AT 250 WORDS)
Animals↗
Influences of maternal smoking and fetal sex on maternal serum oestriol, prolactin, hCG, and hPI levels.
A total of 222 pregnant women had repeated hormone assays between 20 weeks and delivery; 86 of the women were smokers. The maternal hormone balance appeared to be affected by smoking. Smoking affected maternal serum levels of hPL and hCG in pregnancies with a female fetus whereas maternal serum concentrations of oestriol and prolactin were affected in pregnancies with a male fetus. Significantly higher hCG levels were found in mothers who smoked and had a girl than in those who smoked and had a boy. On the basis of our results we feel that smoking mainly affects the placenta.
Adult↗
Inhibition of neural crest cell migration by aggregating chondroitin sulfate proteoglycans is mediated by their hyaluronan-binding region.
We have recently shown that the large hyaluronan-aggregating chondroitin sulfate proteoglycan from cartilage (PG-LA) is unfavorable as a substrate for neural crest cell migration in vitro and that this macromolecule inhibits cell dispersion on fibronectin substrates when included in the medium (R. Perris and S. Johansson, 1987, J. Cell Biol. 105, 2511-2521). In this study we present data on the specificity of the migration-repressing activity of PG-LA and data on the molecular mechanisms by which the proteoglycan might impair neural crest cell motility. Soluble PG-LA potently impaired cell migration on substrates of laminin/laminin-nidogen, vitronectin, and collagen types I, III, IV, and VI. When tested in solid-phase binding assays, PG-LA bound avidly to substrates of collagen types I-III and V. Conversely, minimal amounts of the proteoglycan bound to substrates of laminin-nidogen, vitronectin, collagen types IV and VI, and fibronectin or to a proteolytic fragment encompassing its cell-binding domain (105 kDa). Preincubation of these substrates with soluble PG-LA prior to plating of the cells had no effect on their locomotory behavior. These results indicate that PG-LA affects neural crest cell movement primarily through an interaction with the cell surface, rather than by association with the cell motility-promoting substrate molecules. The molecular interaction of soluble PG-LA with neural crest cells was further examined by analyzing the effects of isolated domains of the proteoglycan on cell migration on fibronectin. Addition of chondroitin sulfate chains, the core protein free of glycosaminoglycans, the isolated hyaluronan-binding region (HABr), or a proteolytic fragment corresponding to the keratan sulfate-enriched domain of the PG-LA to neural crest cells migrating on fibronectin or the 105-kDa fibronectin fragment had no significant effect on their motility. After reduction and alkylation, PG-LA was considerably less efficient in perturbing cell movement on fibronectin substrates and virtually ineffective in altering migration on the 105-kDa fragment. In the presence of hyaluronan fragments of 16-30 monosaccharides in length, or an antiserum against the HABr, the migration repressing activity of PG-LA was reduced in a dose-dependent fashion. Furthermore, the inhibitory action of PG-LA was significantly reduced by treatment of the cells with Streptomyces hyaluronidase.(ABSTRACT TRUNCATED AT 400 WORDS)
Ambystoma↗
Enzyme-linked immunosorbent assay (ELISA) for detection of antibodies against Pityrosporum orbiculare.
IgG antibodies to Pityrosporum orbiculare were detected by an enzyme-linked immunosorbent assay (ELISA) in sera from 10 healthy adults and five healthy 6-month-old children. The ELISA showed 17-80 times higher antibody levels in adults than were found by an indirect immunofluorescence technique (IIF) used in earlier studies. Low titres of antibody were detected in the children.
Adult↗
IgE antibodies to Pityrosporum orbiculare in children with atopic diseases.
IgE antibodies to Pityrosporum orbiculare and 16 other species of fungi were measured with the radioallergosorbent test (RAST) in sera of 131 children. The children were 7-18 years old, suffered from atopic diseases and showed a varied allergic profile on a skin prick test (SPT). IgE antibodies to P. orbiculare were found in the sera of 26 of the 131 children. A higher proportion of the P. orbiculare RAST positive children than of the negative ones had current eczema (p less than 0.0001). In a stepwise logistic regression analysis of SPT and RAST data, the occurrence of serum IgE antibodies to P. orbiculare had the highest explanatory value for current eczema. Ten of 15 children with current atopic eczema and total serum IgE of greater than 500 kU/l had serum IgE antibodies to P. orbiculare. Twenty-four of the 26 P. orbiculare RAST positive children harboured serum IgE antibodies to other fungi. The strong relationship between atopic eczema and the occurrence of IgE antibodies to P. orbiculare indicates that these antibodies may be pathogenetically important in at least some patients with atopic eczema and this gives another dimension to this common skin disease.
Adolescent↗
Separation and identification of growth hormone variants with high performance liquid chromatography techniques.
Liquid chromatography techniques were used to separate and identify human growth hormone (hGH) variants. N-terminal modified forms, such as des-Phe (2-191) and methionyl-hGH (met-1-191), were separated from recombinant human growth hormone (rhGH (1-191] by hydrophobic interaction chromatography (HIC). A proteolytically cleaved ('clip') form of rhGH which has a break in the polypeptide chain between Thr(142) and Tyr(143), also proved to be separable from rhGH by HIC. In addition, a mutated form of rhGH with only two amino acid substitutions, Glu(65) to Val(65) and Glu(66) to Lys(66), on a random coil domain of the molecule, was separated from rhGH by HIC, indicating that these substitutions altered the hydrophobicity of the molecule. Treatment of rhGH with hydrogen peroxide led to sulphoxide formation in two methionine residues Met(14) and Met(125); it was not possible to oxidize Met(170). The oxidized forms of rhGH were readily separated from rhGH(1-191) by reversed-phase chromatography. Analyses of rhGH batches showed very low levels (less than 0.3%) of oxidized rhGH, indicating that rhGH is highly resistant to oxidative reactions. Deamidations were induced in rhGH by heat treatment. The primary deamidation site was found to be Asn(149). Monodesamido rhGH and didesamido rhGH were efficiently separated from rhGH(1-191) by anion-exchange chromatography.
Chromatography, High Pressure Liquid↗
Localization of two fibronectin-binding glycoproteins in rat liver and primary hepatocytes. Co-distribution in vitro of integrin (alpha 5 beta 1) and non-integrin (AGp110) receptors in cell-substratum adhesion sites.
We have compared the localization of integrin alpha 5 beta 1 and AGp110 (apical glycoprotein of Mr 110 x 10(3]] in rat liver parenchyma and in primary hepatocyte cultures. Integrin alpha 5 beta 1 is a heterodimeric fibronectin receptor. AGp110 is a newly described monomeric glycoprotein of the apical (bile canalicular) membrane domain of liver parenchyma that binds in an RGD-independent manner to fibronectin and mediates spreading of hepatocytes onto fibronectin-coated substrata. Using Western blotting of fractionated liver membranes and immunocytochemistry of liver sections at light- and electron-microscope levels, we have confirmed that AGp110 is a canalicular glycoprotein and have established that integrin is located in approximately equal proportions in the sinusoidal, lateral and canalicular membrane domains. In the canalicular surface domain both glycoproteins are associated with microvilli. Examination of immunolabelled primary hepatocytes spread on fibronectin-coated substrata by light and laser scanning confocal microscopy revealed colocalization of AGp110, integrin, actin and vinculin in substratum-attached microextensions at the periphery of the basal cell surface. Actin filaments that terminated at these cell processes originated from circular sub-cortical actin fibres. Interference reflection microscopy revealed focal adhesive contacts at the edge of the basal cell periphery at the same location where AGp110 and integrin were observed by immunofluorescence. In vitro, a proportion of the primary hepatocytes seeded onto fibronectin-coated substrata aggregated into colonies of several cells with intercellular contacts between neighbouring cells. Cell-substratum contacts containing integrin, AGp110, actin and vinculin followed the contours of these colonies in the same manner as they delineated the basal periphery of single, substratum-attached cells. We conclude that both integrin and AGp110 contribute to hepatocyte-fibronectin adhesive interactions and that intercellular adhesion and cooperation among hepatocytes in their response to fibronectin matrices leads to colony formation and morphological differentiation of parenchymal cell monolayers in vitro.
Actins↗
Intraoperative collection of shed blood with citrated compresses for autotransfusion. An experimental study in pigs.
Six pigs were used to study whether the collection of shed blood by means of surgical compresses instead of suction traumatizes such blood. In an in vivo part of the study, the whole blood volume of the pigs was retransfused after treatment with citrated compresses, and in an in vitro part the blood was treated extensively with compresses and analyzed. All animals survived, with a minor fall in hemoglobin after 48 hours and a rise in serum citrate concentration at the end of the experiment. A study of the coagulation system revealed no important change after retransfusion of compress-treated blood. In the in vitro part of the study, repeatedly squeezing blood from the compresses increased the concentration of free hemoglobin to a maximum of 5 g/l after ten squeezes, whereas platelets were numerically unchanged. The study indicates that collecting shed blood by means of surgical compresses may be a safe and efficient method.
Animals↗
Isolation and characterization of a glycosylated form of human insulin-like growth factor I produced in Saccharomyces cerevisiae.
Expression and secretion of human insulin-like growth factor-I (IGF-I) in Saccharomyces cerevisiae was achieved by linking an actin (ACT) promoter to an MF alpha 1 prepro leader peptide/IGF-I gene fusion. Purified human IGF-I from yeast culture media was found to contain, in addition to the native form, also a glycosylated variant. Structural studies showed that both IGF-I forms were processed identically, resulting in 70-amino-acid long polypeptides, with intact N-terminal and C-terminal residues of glycine and alanine, respectively. The glycosylation site was determined to threonine-29 (Thr29), by 1H NMR spectroscopy and protein sequence analysis of an isolated tryptic peptide(22-36). No other glycosylation sites were found. Only mannose was detected in the sugar analysis, with an estimated content of 4.5% w/w corresponding to 2 mannose residues per molecule of IGF-I. The carbohydrate structure, determined by 1H and 13C NMR spectroscopy, was found to be alpha-D-Manp(1----2)alpha-D-Manp(1----3)Thr corresponding to an O-linked glycoprotein structure. No other post-translational modifications could be identified in the glycosylated IGF-I form. Furthermore, this form was highly active, comparable to native IGF-I, exhibiting a specific activity of 20,500 units/mg, as determined by a radio-receptor assay.
Actins↗