Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.10.2 (focal adhesion kinase)
 44,029 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the present study the level of antimicrobial antibodies and the phagocytosis-promoting activity in immunoglobulin preparations produced for intravenous use were assessed. The level of antibodies directed against various microorganisms in six immunoglobulin preparations was determined by using an enzyme-linked immunosorbent assay (ELISA) and was shown to be either equal to or higher than that of pooled normal human serum. All preparations were able to promote phagocytosis of Staphylococcus aureus, Escherichia coli K12, and Streptococcus pyogenes by human granulocytes. Substantial differences among the various preparations in antibody activity were noted. In particular, Intraglobulin, chemically modified by beta-propiolactone treatment, exhibited little activity in both the ELISA and the phagocytosis assay. In contrast, IVIG SRC, Gamimmune, Sandoglobulin (treated at low pH in presence or absence of trace amounts of pepsin), and Gammagard (treated by ion-exchange chromatography) showed good activity in both assays. Comparison of the results of the ELISA and phagocytosis assay for the various preparations indicated a good correlation except for S. aureus with a moderate (strain 42D) or high (strain Cowan I) protein A content. These data indicate that the antibody activity of immunoglobulin preparations against various microorganisms determined by ELISA can be used to predict their opsonic activity.
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PMID:Comparison of antibody activity against various microorganisms in intravenous immunoglobulin preparations determined by ELISA and opsonic assay. 830 Dec

Signals from the extracellular matrix can modulate cellular differentiation and gene expression. We have shown previously that in contrast to other extracellular matrix molecules pepsin-solubilized collagen VI (CVI) can stimulate DNA synthesis of various mesenchymal cell types, apparently independent of integrin-mediated signal transduction. In order to further elucidate collagen VI-induced signaling events, we exposed mouse 3T3 fibroblasts and human HT1080 fibrosarcoma cells to soluble CVI. CVI induced tyrosine phosphorylation of proteins that associate with focal adhesions, such as paxillin, focal adhesion kinase (FAK), and p130CAS. Furthermore, it activated the mitogen-activated protein kinase, erk2. Kinetic analysis showed that these phosphorylations were transient, reaching a maximum after 5 min for transformed HT1080 cells and 30 min for 3T3 fibroblasts. These effects were partly inhibited by a beta1-integrin function blocking antibody and by single chains of CVI. Our results indicate that soluble fragments of native collagen VI, a ubiquitous component of the interstitial extracellular matrix, can mediate stimulation of DNA synthesis via tyrosine phosphorylation of paxillin, FAK, p130CAS, and erk2 in the absence of classical growth factors. Thus, CVI may serve as a matrix-derived sensor that allows for rapid reconstitution of a tissue defect by activating nearby mesenchymal cells.
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PMID:Soluble collagen VI induces tyrosine phosphorylation of paxillin and focal adhesion kinase and activates the MAP kinase erk2 in fibroblasts. 1041 7