E milk and skim milk, which both contain milk-derived EV, indeed a considerable overlap was expected. Why in previous milk proteomics studies the milk-derived EV proteome was not completely unrevealed could be caused by the relative low number of EV in the whole milk analyzed. This is in contrast to our study, where EV were purified and concentrated. Additionally, milk-derived EV contain proteins
Rresponding gene knock-out mice. Processing of the new protein substrates by MMP-2 and MMP-9 identified here provides new mechanisms for gelatinase involvement in angiogenesis and carcinogenesis rather than extracellular matrix degradation (7, 51) and suggests new avenues for therapeutic intervention.Acknowledgments--We thank Dr. Wei Chen from the University of British Columbia Centre for Blood Re
Ortein FP (LEA) p-glycoprotein thioredoxin early nodulin-like protein (ENODL) natural resistance associated macrophage protein glycerophos. diester phosphodiesterase-like protein harpin-induced protein-like remorin Calcium-dependent protein kinase (CDPK) UDP-glycosyltransferase blue-copper-binding-protein Tetraspanin FP secretory carrier calcium-binding EF hand FP ENTH domain-containing protein re
Ortein FP (LEA) p-glycoprotein thioredoxin early nodulin-like protein (ENODL) natural resistance associated macrophage protein glycerophos. diester phosphodiesterase-like protein harpin-induced protein-like remorin Calcium-dependent protein kinase (CDPK) UDP-glycosyltransferase blue-copper-binding-protein Tetraspanin FP secretory carrier calcium-binding EF hand FP ENTH domain-containing protein re
Were then cryoprotected in increasing concentrations of sucrose in PBS (10, 20, and 30 ) over 3 d at 4 C. They were then snap frozen in liquid nitrogen, cryosectioned at 12 m, and mounted on slides. For labeling, sections from approximately bregma 0 (the level at which the septum and striatum are visible) or bregma 2.0 (hippocampus and thalamus are visible) were used; they were rehydrated in PBS,
Were then cryoprotected in increasing concentrations of sucrose in PBS (10, 20, and 30 ) over 3 d at 4 C. They were then snap frozen in liquid nitrogen, cryosectioned at 12 m, and mounted on slides. For labeling, sections from approximately bregma 0 (the level at which the septum and striatum are visible) or bregma 2.0 (hippocampus and thalamus are visible) were used; they were rehydrated in PBS,
Were then cryoprotected in increasing concentrations of sucrose in PBS (10, 20, and 30 ) over 3 d at 4 C. They were then snap frozen in liquid nitrogen, cryosectioned at 12 m, and mounted on slides. For labeling, sections from approximately bregma 0 (the level at which the septum and striatum are visible) or bregma 2.0 (hippocampus and thalamus are visible) were used; they were rehydrated in PBS,
Omplement components on their surfaces [96]. Thus, binding of this major alternative complement pathway inhibitor is related to serum resistance in Leptospira spirochetes. Interestingly, FH binding was shown to be dependent upon Lig proteins [97]. The multifunctional LigB protein also binds to C3b and C4b and interferes with complement activation [98]. Lsa30, a novel leptospiral adhesion protein,