Ed according to the underside of the substrate, the center of the cell, and an upper portion touching the cell bound. n � �� �, * p av-951 Tivozanib- WT SHIP-/-A Unlk fertilization liable fMLP C WT SHIP1-/ – + – + – + – + WT-PTEN / – WT PTEN / – Unlk fertilization liable fMLP B p-Akt act 0 10 20 30 40 50 60 70 80 90 0 5 10 15 20 25 30 35 WT SHIP1-/-top low intensity interval t Z-Azis 0 10 20 30 40 50 60 70 80 90 top bottom center SHIP1-/-Relative WT Akt-PH intensity t D * band 23 1 April 2012 in SHIP1 Zelladh sion and migration | 1225 high speed in both conditions. In contrast, SHIP1 eutrophils � a 0.1% BSA � Glasobjekttr hunter �c oated k nnte The chemotactic gradient and migration attempt to capture, but chemotaxis was very inefficient, with a speed of 1.
4 PI-103 m / s However, when the surface surface coated with BSA 2% in order to reduce the adhesion, the cell migration adversely chtigt partly free, with a big s population of cells that migrate along the entire L length of the channel with an average speed 5.67m / s fMLP stimulation of GPCR-mediated signaling from the inside out s leads to activation of integrins. Activated integrins can then bind to the extracellular Re matrix proteins By interactions with RGD motifs. To investigate whether the reduced Zelladh recession W While k of cell migration Can M Ngel rescue in cell migration SHIP1 EUR eutrophils, we tested the F Ability of neutrophils to a gradient of fMLP on a Glasoberfl che migrate with fibronectin in a buffer containing 1 g / ml coated RGD.
The RGD peptide reduced the buffer Zelladh recession � ubstratum �s by binding to activated integrins and preventing their association with fibronectin. We found that, in the absence of RGD in the buffer, the migration of SHIP1 � eutrophils changed greatly VER. Could detect these cells to start the chemotactic gradient, and chemotaxis, but the adhesive requires limited cell migration. However, in the presence of a g / ml RGD peptide in the buffer, SHIP1 EUR eutrophils k nnte Migrate much more efficiently, at a rate of 6.8 compared to 2.9 m / s in the absence of RGD peptide. The speed of migration of neutrophils wild-type cells in the absence or presence of RGD peptide in the buffer was 10.2 and 8.75 m / s, respectively.
These results indicate that cell migration M Deficiencies in SHIP1 EUR eutrophils an effect of increased Hten Zelladh Commission and can be saved by reducing the Zelladh recession � ubstratum �s. Altered production of reactive oxygen species in SHIP1 EUR eutrophils neutrophil NADPH oxidase is an enzyme that consists of several components of the membrane and cytosolic proteins that remain unassembled in resting cells Including t. Membrane components include flavocytochrome B558 heterodimer, which is composed of two subunits: p22phox and gp91. Cytosolic components include four L Soluble factors � �p 67phox, p47phox, p40phox and Rac GTPase. To the activation of the receptors on the cell Che, cytosolic factors translocation to the membrane, where NADPH oxidase is mounted and big e quantities of superoxide anions, which tests to glass, the Objekttr hunter with either 0.
1% coated bovine serum albumin, f promotes the mission Zelladh, or 2% BSA, the Zelladh recession reduced. We found that wild-type neutrophils could migrate FIGURE 5: Defective chemotaxis in SHIP1 � eutrophils can be saved by reducing the Zelladh mission. Neutrophils from wild-type and SHIP1 � ice were to Deckgl Fibers with 0.1-coated% to 2% BSA or fibronectin were plated in the presence or absence of RGD peptide in the buffer memory in a device single-cab scanning and to a chemotactic gradient shallow by adding 1 the fMLP exposed generated. Migrating neutrophils were evaluated for speed and direction of migration, as described in Materials and Methods. Tracks of cells migrating wild-type and SHIP1 Neutrophils were obtained from the captured images to reconsider so that all cells from the same point started and plotted. 0 2 4 6 8 10 12 14 WT SHIP1-/-Fib Fib with RGD 0 2 4 6 8 10 12 14 16 WT% BSA, 2% BSA SHIP1-/-0.1 fMLP CB fMLP A speed WT 0.1