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J Pick

Publications and source records attributed to J Pick.

At least 19 recordsLinked to original sources
PubMed2006

Lamotrigine for schizophrenia.

BACKGROUND: Treating the 20-30% of people with schizophrenia whose symptoms are resistant to treatment can be problematic. Adding lamotrigine to ongoing antipsychotic treatment has shown to be of benefit in preliminary studies. OBJECTIVES: To evaluate the effects of adjuvant lamotrigine for people with schizophrenia and schizophrenia-like psychoses. SEARCH STRATEGY: We searched the Cochrane Schizophrenia Group's Register (February 2006) and inspected references of all identified studies for further trials. We contacted relevant authors of trials for additional information. SELECTION CRITERIA: We included all clinical randomised trials comparing lamotrigine with placebo or other antipsychotic augmentation strategies. DATA COLLECTION AND ANALYSIS: We extracted data independently. For homogenous dichotomous data we calculated random effects relative risk (RR), 95% confidence intervals (CI) and, where appropriate, numbers needed to treat (NNT) on an intention-to-treat basis. For continuous data, we calculated weighted mean differences (WMD). MAIN RESULTS: We found five relevant trials (total n=537), but no usable data on service outcomes, general functioning, behaviour, engagement with services, satisfaction with treatment or economic outcomes. Overall, reporting of data was poor. Those data we were able to use suggested that equal proportions of people allocated lamotrigine or placebo had no global response (n=208, 1 RCT, RR 1.06 CI 0.73 to 1.54). There was no significant difference between groups in the proportions of people whose mental state did not improve (n=297, 3 RCT, RR 1.26 CI 0.81 to 1.97). There was, however, a significant reduction in the PANSS total scores (n=67, 2 RCT, WMD -16.88 CI -8.57 to -25.18, p=0.0001), positive symptom sub-scale scores (n=65, 2 RCTs, WMD -5.10 CI -8.86 to -1.34) and negative symptom sub-scale scores (n=67, 2 RCTs, WMD -5.25, CI -7.07 to -3.43). Most cognitive measures showed no differences (n=329, 2 RCTs, RR not attaining BACS composite score of 0.5 1.10 CI 0.59 to 2.04). The proportion of participants leaving studies was about 25% at 12 weeks (n=537, 5 RCTs, RR 0.96 CI 0.71 to 1.29). The lamotrigine group did experience the outcome of any adverse effects significantly more frequent than people allocated placebo (n=429, 2 RCTs, RR 1.19 CI 1.02 to 1.38, NNH 10 CI 5 to 90). Among the many effects listed, only nausea was found to be significantly more (9%) in the lamotrigine group compared with placebo (n=465, 3 RCTs, RR 2.26 CI 1.05 to 4.88). AUTHORS' CONCLUSIONS: Evidence for use of lamotrigine as an adjuvant for people with schizophrenia is not robust and large well-designed, conducted and reported real-world randomised trials are needed to determine its place in everyday clinical practice.

Antipsychotic Agents↗
PubMed1998

Rat mucosal mast cells: the cultured bone marrow-derived mast cell is biochemically and functionally analogous to its counterpart in vivo.

Mast cells (MC) are biochemically and functionally heterogeneous and the mixture of MC phenotypes varies according to anatomical location. Intestinal mucosal MC (IMMC) have been used to study the mucosal MC subset in the rat, but they are difficult to isolate in sufficient numbers and with consistent purity and viability. Bone marrow-derived MC (BMMC), with an apparent mucosal MC phenotype, can be cultured in large numbers and with high purity from normal rat bone marrow using supernatants from mesenteric lymph node cells of rats infected with the nematode, Nippostrongylus brasiliensis. We have compared serine proteinase content, tumour necrosis factor-alpha (TNF-alpha) storage and secretion, and TNF-alpha-dependent cytotoxicity of IMMC and BMMC to assess the appropriateness of BMMC as in vitro models of mucosal MC. Two-dimensional gel electrophoretic analysis revealed that the overall protein constituents of BMMC and IMMC were highly homologous. Immunoblotting confirmed that both MC types expressed the MMC-associated enzyme, rat mast cell proteinase-2 (RMCP-2), but not RMCP-1, mast cell proteinase-5 (MCP-5) or carboxypeptidase A (CPA), which characterize the connective tissue MC in the rat and which were detected in a representative of this subset, namely, the periotoneal MC (PMC). BMMC demonstrated levels of TNF-alpha-dependent cytotoxicity that were equivalent to those of IMMC. Like IMMC, BMMC contained little stored TNF-alpha, in comparison with PMC, but both MC types generated substantial amounts of TNF-alpha 6 hr following IgE-mediated activation. Pretreatment of PMC with recombinant rat interferon-gamma (IFN-gamma) for 20 hr inhibited anti-immunoglobulin E (anti-IgE)-mediated release of the granule-associated enzyme, beta-hexosaminidase, whereas identically treated BMMC were unresponsive to this cytokine. Similar results have previously been reported for IMMC. Rat BMMC, unlike their more immature and less phenotypically committed counterparts in the mouse, appear therefore to be more appropriate models for studies on the mucosal MC.

Animals↗
PubMed1997

Expression of the nonstructural protein NS1 of equine influenza A virus: detection of anti-NS1 antibody in post infection equine sera.

The nucleotide sequence of the nonstructural protein NS1 of the influenza virus A/equine 2/Suffolk/89 was determined and found to be 97% identical to that of A/equine 2/Miami/63. A similar level of identity was shown for the deduced NS1 amino acid sequence. The NS1 gene was expressed, in its entirety and in part, as fusion proteins with glutathione S-transferase using the pGEX-3X expression vector. Antibodies to NS1 protein were detected in serum samples from ponies experimentally infected with influenza virus, but not in animals vaccinated with whole inactivated virus or in unprimed control animals. The antigenic determinant(s) of NS1 protein appear to be located in the C-terminal half of the protein. The implications of these findings are discussed with reference to the use of NS1 protein as a differential diagnostic marker for influenza virus infection in the presence of high levels of circulating antibody to influenza haemagglutinin generated by recent vaccination.

Amino Acid Sequence↗
PubMed1995

Proteinases of rat mast cells. Peritoneal but not intestinal mucosal mast cells express mast cell proteinase 5 and carboxypeptidase A.

Six basic proteins of 26 to 38 kDa with isoelectric points (pI) > or = 8.5 were abundant in proteins separated by two-dimensional SDS-PAGE from adult rat peritoneal mast cells (MC). One was identified previously as rat mast cell proteinase (RMCP) 1, a chymase of 26 to 28 kDa, pI > 9.0. Microsequence analyses showed that two polypeptides of about 29 and 30 kDa had NH2 terminal amino acid sequences homologous to mouse MC proteinase 5 (MCP-5), whereas the amino terminals of the 33, 35, and 36 kDa proteins were homologous to MC carboxypeptidase A (MC-CPA). Rabbit Abs produced against synthetic peptides of the identified NH2 terminal sequences were used in immunoblot studies. At least three proteins reacted with Abs to MC-CPA, whereas Abs to MCP-5 detected three adjacent polypeptides, rather than just the two identified by using microsequence analysis. Removal of oligosaccharide side chains using peptide:N-glycosidase F reduced the heterogeneity of each set of three polypeptides (MCP-5 and MC-CPA) to a band of each protein of a lower M(r). The serine proteinase inhibitor [3H]diisopropylfluorophosphate ([3H]DFP) bound to a proteinase of 30 to 35 kDa, which is probably MC tryptase (pI < or = 6.0). Immunoblot analysis of proteins from intestinal mucosal mast cells showed RMCP-2, but not RMCP-1, MCP-5, or MC-CPA. This is the first report of MCP-5 in the rat and of clearly distinguishable glycosylated forms of MC CPA. These proteinases appear to be restricted in their distribution to selected MC populations, but little is known about their functions.

Amidohydrolases↗
PubMed1993

[Blood products stored in plastic bags: release of plasticizers from the bag material].

The plasticizer di-(2-ethyl-hexyl)phthalate (DEHP) is slowly leached from the wall of the PVC blood bags into the blood products. It will be partly incorporated into the membranes of the blood cells, and finally will be transfused together with the blood products into the recipient, where DEHP might exert toxic effects. DEHP content was determined by HPLC in different blood products stored in plastic bags manufactured by different firms (Medicor--Hungary, MacoPharma--France, Terumo--Japan, Baxter--USA). In whole blood DEHP is present mainly in the plasma and blood bags of different firms show similar results. 1 unit of whole blood contains 20-50 mg DEHP on day 14 of storage, and 30-55 mg on day 28, while red blood cells resuspended in plasma contained only 2-15 mg on day 14. 15-20 mg DEHP was found in 1 unit of plasma stored for 4 days at +4 degrees C. Only 1-4 mg DEHP was detected in 1 unit of erythrocytes (cca. 200 ml) even on day 14 of storage. The supernatant of platelet concentrates contained the relatively highest amount of DEHP (even 50-65 mg was found in 1 unit of platelet concentrates on day 5 of storage). When platelet concentrates were studied, essential differences were recorded between the bags manufactured by different firms. Platelet reactivity is better maintained in storage bags manufactured without DEHP.

Blood↗
PubMed1986

Gangliosides in acute myeloid leukaemia (AML) and non-Hodgkin's lymphoma (NHL).

Gangliosides of human acute myelomonocytic leukaemia (AMMoL), acute monocytic leukaemia (AMoL) and lymphoblastoid (pre-B) lymphoma cells were analysed by overpressured thin-layer chromatography (OPTLC) followed by scanning densitometry. AMMoL cells were found to contain four gangliosides, viz. GM3 (47.2%), GM1 (31.8%), GD1a (7.5%) and an unidentified compound migrating between GM1 and GD1a (13.5%). In AMoL cells, six components were identified (GM3:51.3%, GM1:13.4%, GD3:7.8%, GD1a:4.7%, GD1b:6%, and an unidentified compound migrating between GM2 and GM1). The total gangliosides extracted from pre-B lymphoma cells of the hand-mirror variant were composed of 10 species (GM3:50.8%, GM2:11.2%, GM1:7.8%, GD3:2.3%, GD1a:1.1%, GD1b:2.2%, GT1:1.6%, and three unidentified components with chromatographic mobilities between GM2 and GD1a). Additional studies must still be performed to clarify the question as to whether ganglioside GD3 represent a qualitative glycolipid marker for AMoL and pre-B lymphoblastic lymphoma.

Chromatography, Thin Layer↗
PubMed1986

Ganglioside composition in common acute lymphoblastic leukaemia.

Human leukaemic lymphocytes of the common acute lymphoblastic leukaemia (cALL) subtype were analysed for ganglioside composition by over pressured layer chromatography-densitometry. Two major ganglioside components, GM3 (58.0-77.8% of the total sialic acid content) and GM1 (20.7%-29.2%), and some minor compounds, GM2 (trace amounts to 9.6%) and unidentified gangliosides with chromatographic mobility between GM1 and GD1a (trace to 12.6%), were isolated from these cells. The relative amount of GM3 in cALL cells was found to be about double that in normal lymphocytes (65.7% vs. 37.7%), but lower than in chronic lymphocytic leukaemia (CLL) cells (65.7% vs. 81.5%). The cALL cells contained trace amounts of the ganglioside GD3, a compound present in CLL cells (5.6%) but absent in normal lymphocytes.

Adolescent↗
PubMed1985

Gangliosides in human chronic lymphocytic leukaemia.

Gangliosides were analysed by elaborated overpressured thin-layer chromatography (OPTLC) in 6 cell samples from 5 patients with chronic lymphocytic leukaemia (CLL) of B-cell origin, and 4 individual lymphocyte preparations from normal blood donors. The principal difference in the ganglioside profile between these two counterparts appears to be the presence of GD3 and the predominance of the less polar compounds (GM3, GM2, GM1) in CLL cells. Qualitatively, GD3 accounted for about 5.5% of the total CLL gangliosides, whereas it was not detectable in normal lymphocytes. Quantitatively, GM3 constituted more than 81% of the total CLL gangliosides, a proportion more than twice as high as that found in normal lymphocytes. Three other minor gangliosides were isolated from CLL cells; these were shown to be GM2 (trace amounts), GM1 (7.7%), and GD1 (4%). The expression of individual gangliosides varied greatly among the various CLL samples obtained from different patients, and even from the same patient, if examined at different times. No gangliosides were found in the supernatant collected from CLL cells subjected to a temperature shift (0 degrees C to 37 degrees C) or in the cell-free medium harvested from the CLL cells kept in overnight culture.

Aged↗