Licase Ecm16.ACKNOWLEDGMENTSWe thank M. Anjos for assistance with subcloning ecm16 mutations, C. Wang for anti-Bud23 antibody, and G. Dieci for Rps8 antibody. This work was supported by NIH grants RO1GM53655 and RO1GM108823 to A.W.J.Canonical and Noncanonical G-Protein Signaling Helps Coordinate Actin Dynamics To Promote Macrophage Phagocytosis of ZymosanNing-Na Huang,a Steven Becker,b Cedri
G human lung cells [145]. Lee and co-workers have explored the application of another biological pore, listeriolysin O (LLO), from the pathogenic bacterium Listeria monocytogenes, as a delivery vehicle for macromolecules such as proteins into cells both in vitro and in vivo [40,96?8,146?48]. These studies exploited that a relatively high proton concentration (pH range of 4.9?.7) triggers the membr
Ogether with desmocollin-3, syndecan-4 (SDC4), perlecan, fibulin-2 and laminin-332 as substrates, our data support the hypothesis that MMP10 is involved in the control of keratinocyte migration by breakdown of adhesion com-Molecular Cellular Proteomics 14.MMP10 Substrate Degradomics in KeratinocytesMMPDifferentiationMMP9 DMKNDesmocollinMigration Proliferation AdhesionSyndecan IntegrinsCYR61 4Lam
Ogether with desmocollin-3, syndecan-4 (SDC4), perlecan, fibulin-2 and laminin-332 as substrates, our data support the hypothesis that MMP10 is involved in the control of keratinocyte migration by breakdown of adhesion com-Molecular Cellular Proteomics 14.MMP10 Substrate Degradomics in KeratinocytesMMPDifferentiationMMP9 DMKNDesmocollinMigration Proliferation AdhesionSyndecan IntegrinsCYR61 4Lam
D hemolymph (Table II). HP8 and PAP3 identified at 70 ?80 kDa may represent their catalytic domains in complex with serpin-6 (19). Since most serpin-HP complexes resided in gel slice-4 (70 ?80 kDa), we were unable to distinguish them or identify their components in this analysis. Serpin-9 displayed interesting changes: its level was higher in na e plasma and became lower after the challenge (Table
D hemolymph (Table II). HP8 and PAP3 identified at 70 ?80 kDa may represent their catalytic domains in complex with serpin-6 (19). Since most serpin-HP complexes resided in gel slice-4 (70 ?80 kDa), we were unable to distinguish them or identify their components in this analysis. Serpin-9 displayed interesting changes: its level was higher in na e plasma and became lower after the challenge (Table
Y between tenascin C and tenascin XB, this protein and its interactions may represent a novel target to follow disease and, in particular, to act on in order to favor the enhancement of vascular repair mechanisms, known to be down-regulatedwith age and in pathological conditions (18). Importantly, decreased tenascin XB levels are associated with various problems of mitral and tricuspid valves (16)
Ously(13). Peptides were analyzed using a linear ion trap (LTQ) mass spectrometer (Thermo Fisher Scientific) in positive ion mode. An in-house software package, RAWDistiller v. 1.0, was used to convert the resulting .raw files to .ms2 files. MS/MS spectra were then matched to 29,375 human protein sequences (National Center of Biotechnology Information, November 2010 release) using the SEQUEST algo