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#18496851   2008/07/23 Save this To Up

Statistical mixture modeling for cell subtype identification in flow cytometry.

Statistical mixture modeling provides an opportunity for automated identification and resolution of cell subtypes in flow cytometric data. The configuration of cells as represented by multiple markers simultaneously can be modeled arbitrarily well as a mixture of Gaussian distributions in the dimension of the number of markers. Cellular subtypes may be related to one or multiple components of such mixtures, and fitted mixture models can be evaluated in the full set of markers as an alternative, or adjunct, to traditional subjective gating methods that rely on choosing one or two dimensions. Four color flow data from human blood cells labeled with FITC-conjugated anti-CD3, PE-conjugated anti-CD8, PE-Cy5-conjugated anti-CD4, and APC-conjugated anti-CD19 Abs was acquired on a FACSCalibur. Cells from four murine cell lines, JAWS II, RAW 264.7, CTLL-2, and A20, were also stained with FITC-conjugated anti-CD11c, PE-conjugated anti-CD11b, PE-Cy5-conjugated anti-CD8a, and PE-Cy7-conjugated-CD45R/B220 Abs, respectively, and single color flow data were collected on an LSRII. The data were fitted with a mixture of multivariate Gaussians using standard Bayesian statistical approaches and Markov chain Monte Carlo computations. Statistical mixture models were able to identify and purify major cell subsets in human peripheral blood, using an automated process that can be generalized to an arbitrary number of markers. Validation against both traditional expert gating and synthetic mixtures of murine cell lines with known mixing proportions was also performed. This article describes the studies of statistical mixture modeling of flow cytometric data, and demonstrates their utility in examples with four-color flow data from human peripheral blood samples and synthetic mixtures of murine cell lines.

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#15096474   2004/05/20 Save this To Up

Functional comparison of the mouse DC-SIGN, SIGNR1, SIGNR3 and Langerin, C-type lectins.

The mouse (m) DC-SIGN family consists of several homologous type II transmembrane proteins located in close proximity on chromosome 8 and having a single carboxyl terminal carbohydrate recognition domain. We first used transfected non-macrophage cell lines to compare the polysaccharide and microbial uptake capacities of three of these lectins--DC-SIGN, SIGNR1 and SIGNR3--to another homologue mLangerin. Each molecule shares a potential mannose-recognition EPN-motif in its carbohydrate recognition domain. Using an anti-Tag antibody to follow Tag-labeled transfectants, we found that each molecule could be internalized, although the rates differed. However, mDC-SIGN was unable to take up FITC-dextran, FITC-ovalbumin, zymosan or heat-killed Candida albicans. The other three lectins showed distinct carbohydrate recognition properties, assessed by blocking FITC-dextran uptake at 37 degrees C and by mannan binding activity at 4 degrees C. Furthermore, only SIGNR1 was efficient in mediating the capture by transfected cells of Gram-negative bacteria, such as Escherichia coli and Salmonella typhimurium, while none of the lectins tested were competent to capture Gram-positive bacteria, Staphylococcus aureus. Interestingly, transfectants with SIGNR1 lacking the cytoplasmic domain were capable of binding FITC-zymosan in a manner that was abolished by EDTA or mannan, but not laminarin. In addition, resident peritoneal CD11b+ cells expressing SIGNR1 bound zymosan at 4 degrees C in concert with a laminarin-sensitive receptor. Therefore these homologous C-type lectins have distinct recognition patters for microbes despite similarities in the carbohydrate recognition domains.

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MOUSE ANTI BOVINE ROTAVIR Dengue Type 1 antibody, M Dengue Type 2 antibody, M Dengue Type 3 antibody, M Dengue Type 4 antibody, M ELISA grade mouse type I ELMsI ELISA grade mouse t ELMsI ELISA grade mouse t ELMGCI Mouse IgG anti chi Mouse anti-chick type I c Mouse anti-chick type I c ELMGBI Mouse IgG anti bov

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#9973505   1999/04/13 Save this To Up

The beta-glucan-binding lectin site of mouse CR3 (CD11b/CD18) and its function in generating a primed state of the receptor that mediates cytotoxic activation in response to iC3b-opsonized target cells.

Mouse leukocyte CR3 (Mac-1, alphaMbeta2 integrin) was shown to function as a receptor for beta-glucans in the same way as human CR3. Soluble zymosan polysaccharide (SZP) or pure beta-glucans labeled with FITC or 125I bound in a saturable and reversible manner to neutrophils, macrophages, and NK cells. This lectin activity was blocked by anti-CD11b mAb M1/70 or 5C6 and did not occur with leukocytes from CR3-/- (CD11b-deficient) mice. SZP preparations containing primarily mannose or glucose bound to CR3, and the binding of 125I-labeled beta-glucan to CR3 was competitively inhibited by beta-glucans from barley or seaweed, but not by yeast alpha-mannan. Also, as with human CR3, the lectin site of mouse CR3 was inhibited by alpha- or beta-methylglucoside (but not D-glucose), alpha- or beta-methylmannoside, and N-acetyl-D-glucosamine. Phagocytosis of zymosan and serum-opsonized zymosan was partially inhibited by anti-CR3 and was reduced to <40% of normal with leukocytes from CR3-/- mice. As with neutrophils from patients with CD18 deficiency, neutrophils from CR3-/- mice exhibited no phagocytosis of particulate beta-glucan. SZP or beta-glucans primed CR3 of neutrophils, macrophages, and NK cells for cytotoxicity of iC3b-opsonized tumor cells that otherwise did not trigger killing. beta-Glucan priming for cytotoxicity was inhibited by anti-CR3 and did not occur with leukocytes from CR3-/- mice. The primed state of macrophage and NK cell CR3 remained detectable for 18 to 24 h after pulsing with beta-glucans. The similarity of mouse and human CR3 in response to beta-glucans highlights the utility of mouse tumor models for development of therapeutic beta-glucans.

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#8157977   1994/05/13 Save this To Up

Physical association of complement receptor type 3 and urokinase-type plasminogen activator receptor in neutrophil membranes.

A previous study has shown that Fc gamma RIIIB (CD16), an extensively glycosylated glycosyl-phosphatidylinositol-linked neutrophil membrane protein, specifically co-caps with the iC3b R (CR3; CD11b/CD18). This study tests the possible physical interactions of another extensively glycosylated glycosyl-phosphatidylinositol-linked protein, the urokinase-type plasminogen activator receptor (uPAR), with CR3. Receptors were labeled using fluorochrome-conjugated F(ab')2 fragments of an anti-CR3 mAb. In some cases cells were capped using second step F(ab')2 fragments of an anti-mouse F(ab')2 antiserum. After 30 min at 37 degrees C, 65 +/- 4% of the cells exhibited CR3 caps whereas 61 +/- 2% demonstrated uPAR caps. When CR3-capped cells were probed with F(ab')2 fragments of anti-uPAR conjugated to a distinct fluorochrome, 45 +/- 3% of the cells co-capped uPAR. When uPAR was capped, 48 +/- 2% of the cells co-capped CR3. Similar levels of co-capping were observed using a DNP-conjugated anti-CR3 F(ab')2 and an anti-DNP second step F(ab')2 reagent for capping or using FITC-uPA as a probing reagent. Furthermore, CR3-uPAR co-capping and/or co-clustering was also observed using anti-CR3 IgM and Mn2+ as integrin aggregation stimuli. Significant co-capping of anti-CD14, anti-CD59, anti-Mo5, anti-HLA, or NBD-PE (a lipid probe) was not observed. Moreover, CR3 and uPAR co-capping was blocked by N-acetyl-D-glucosamine, but not by six other saccharides, suggesting that a lectin-like site may participate in co-capping. This suggests that CR3 may regulate adhesive events by several mechanisms, including the regulation of the spatial distribution of uPAR.

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