Report on sampling and analysis of exhaust air at the 221-T and 2706-T buildings

Stauffer, Mark T.

doi:10.2172/313367

Cited by 3 publications

(6 citation statements)

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“…The GFP-PLC␦ PH domain expression vector was coexpressed with PIPKI␣ by microinjection. In the serum-free condition, the PLC␦ PH domain is primarily cytosolic, consistent with previous reports, whereas PIPKI␣ is predominantly plasma membrane-associated when overexpressed (16,44). Upon stimulation with PDGF, the PLC␦ PH domain rapidly reorganized and colocalized with PIPKI␣ at actin foci (Fig.…”

Section: Fig 2 Pipki␣ Localizes To Pdgf-induced Membrane Rufflessupporting

confidence: 90%

“…Scale bar, 50 m. PIP 2 induce actin remodeling independent of PI3K. In support of direct modulation by PIP 2 , we used a PLC inhibitor, U73122, to block PIP 2 hydrolysis (44). With this inhibitor, the extent of actin foci generation by PIPKI␣ and PDGF stimulation was enhanced, supporting PIP 2 modulation of actin foci assembly (data not shown).…”

Section: Fig 5 Pipki␣ Induces Actin Remodeling Dependent Upon Pdgf mentioning

confidence: 77%

“…To verify that PIP 2 was produced at sites of actin remodeling, a GFP-PLC␦ PH domain was used to detect local changes in PIP 2 (36,44). The GFP-PLC␦ PH domain expression vector was coexpressed with PIPKI␣ by microinjection.…”

Section: Fig 2 Pipki␣ Localizes To Pdgf-induced Membrane Rufflesmentioning

confidence: 99%

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Membrane Ruffling Requires Coordination between Type Iα Phosphatidylinositol Phosphate Kinase and Rac Signaling

Doughman

Firestone

Wojtasiak

et al. 2003

Journal of Biological Chemistry

105

104

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Membrane ruffle formation requires remodeling of cortical actin filaments, a process dependent upon the small G-protein Rac. Growth factors stimulate actin remodeling and membrane ruffling by integration of signaling pathways that regulate actin-binding proteins. Phosphatidylinositol 4,5-bisphosphate (PIP 2 ) regulates the activity of many actin-binding proteins and is produced by the type I phosphatidylinositol phosphate kinases (PIPKIs). Here we show in MG-63 cells that only the PIPKI␣ isoform is localized to platelet-derived growth factor (PDGF)-induced membrane ruffles. Further, expression of kinase dead PIPKI␣, which acts as a dominant negative mutant, blocked membrane ruffling, suggesting that PIPKI␣ and PIP 2 participate in ruffling. To explore this, PIPKI␣ was overexpressed in serumstarved cells and stimulated with PDGF. In serumstarved cells, PIPKI␣ expression did not stimulate actin remodeling, but when these cells were stimulated with PDGF, actin rapidly reorganized into foci but not membrane ruffles. PIPKI␣-mediated formation of actin foci was independent of both Rac1 and phosphatidylinositol 3-kinase activities. Significantly, coexpression of dominant active Rac1 with PIPKI␣ in PDGF-stimulated cells resulted in membrane ruffling. The PDGF-and Rac1-stimulated ruffling was inhibited by expression of kinase-dead PIPKI␣. Combined, these data support a model where the localized production of PIP 2 by PIPKI␣ is necessary for actin remodeling, whereas formation of membrane ruffles required Rac signaling.

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Section: Fig 2 Pipki␣ Localizes To Pdgf-induced Membrane Rufflessupporting

confidence: 90%

Section: Fig 5 Pipki␣ Induces Actin Remodeling Dependent Upon Pdgf mentioning

confidence: 77%

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Membrane Ruffling Requires Coordination between Type Iα Phosphatidylinositol Phosphate Kinase and Rac Signaling

Doughman

Firestone

Wojtasiak

et al. 2003

Journal of Biological Chemistry

105

104

View full text Add to dashboard Cite

show abstract

“…At each time point, the fluorescence intensity values (pixels) from the cytoplasm (5 µm in from the plasma membrane on each side of the cell) were averaged, and this value was subtracted from the values of all data points. This is essentially the method used by Stauffer et al [13]. of the fusion protein in cells that had been stimulated with insulin for 15 min before the addition of wortmannin.…”

Section: Quantitative Analysis Of Ph(pkb)gfp Binding To Plasma Membranesmentioning

confidence: 99%

“…Other well characterized PH domains, such as that found in phospholipase Cδ-1, bind PtdIns(4,5)P # with higher affinity than the 3-phosphoinositides [13]. A third group of proteins possesses PH domains that appear to be highly specific for PtdIns(3,4,5)P $ ; for example, the PH domain of GRP1 has an affinity for the Ins(1,3,4)P $ headgroup configuration that is at least 100-fold weaker than that for the Ins(1,3,4,5)P % headgroup that occurs in PtdIns(3,4,5)P $ [5].…”

Section: Introductionmentioning

confidence: 99%

The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo

1999

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Seal bond characterization of laminated plastic food cups by scanning electron and optic microscopes

Ayhan

2004

Packag Technol Sci

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Heat seals of laminated semi-rigid food cups were evaluated to characterize the seal bond. Laminated lidding material was sealed at temperatures of 160-180°C to thermoformed cups. Various seal regions of the cups with different ultrasonic signal strengths (%) were sectioned at the rim and examined using optical and scanning electron microscopes (SEM). Ultrasonic signals were able to pinpoint seal defects; however, the magnitude of the signals did not relate to the actual seal condition or seal quality affected by the sealing process. This was attributed to the very short seal width and non-parallel surface of the heat seal, which possibly resulted in signal loss by reflection and scattering from the seal surface. C-scan of ultrasound, SEM and optical microscopic images provided the information that the heatsealing process was unstable, due to insufficient and non-uniform heat-seal temperature or pressure, misalignment of the sealing jaws or non-parallel sealing or cutting unit configuration.

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Report on sampling and analysis of exhaust air at the 221-T and 2706-T buildings

Cited by 3 publications

References 0 publications

Membrane Ruffling Requires Coordination between Type Iα Phosphatidylinositol Phosphate Kinase and Rac Signaling

Membrane Ruffling Requires Coordination between Type Iα Phosphatidylinositol Phosphate Kinase and Rac Signaling

The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo

Seal bond characterization of laminated plastic food cups by scanning electron and optic microscopes

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