مورد إلكتروني
v-Src accelerates spontaneous motility via phosphoinositide 3-kinase, phospholipase C and phospholipase D, but abrogates chemotaxis in Rat-1 and MDCK cells.
| العنوان: | v-Src accelerates spontaneous motility via phosphoinositide 3-kinase, phospholipase C and phospholipase D, but abrogates chemotaxis in Rat-1 and MDCK cells. |
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| المصدر: | Journal of cell science, 117 (Pt 20 |
| بيانات النشر: | 2004-09 |
| تفاصيل مُضافة: | Platek, Anna Mettlen, Marcel Camby, Isabelle Kiss, Robert Amyere, Mustapha Courtoy, Pierre |
| نوع الوثيقة: | Electronic Resource |
| مستخلص: | In Rat-1 fibroblasts, v-Src causes a profound remodelling of cortical actin cytoskeleton. This transformation includes membrane ruffling, a hallmark of the leading edge in migrating cells, and results from activation of phosphoinositide 3-kinase (PI 3-kinase), phospholipase C (PLC) and phospholipase D (PLD). We therefore reexamined whether motility is constitutively triggered by v-Src and studied whether this response is controlled by the same signalling pathway. The study was performed using Rat-1/tsLA29 and MDCK/tsLA31 cells, each harbouring a different thermosensitive v-Src kinase, active at 34 degrees C but inactivated at 40 degrees C. In both cell lines, overnight v-Src activation induced transformation and accelerated spontaneous motility by approximately twofold, as evidenced by wound-healing assay and by single-cell track, time-lapse recording in Dunn chambers. Inhibitors of PI 3-kinase, PLC and PLD selectively abrogated acceleration of motility by v-Src. Since mechanisms that co-ordinate spontaneous, as distinct from oriented, cell migration are separable, we further analysed in Dunn chambers chemotactic response of Rat-1/tsLA29 cells to PDGF and of MDCK/tsLA31 cells to EGF. In both cases, v-Src decreased the steady-state level of growth factor receptors at the cell surface twofold, and abrogated movement directionality at comparable level of occupancy as in non-transformed cells. The burst of pinocytosis in response to growth factors was also abolished by v-Src. Altogether, these results indicate that v-Src triggers motility in a PI 3-kinase-, PLC- and PLD-dependent manner, but abrogates directionality by suppressing polarised signalling downstream of growth factor receptors. Journal Article Research Support, Non-U.S. Gov't info:eu-repo/semantics/published |
| مصطلحات الفهرس: | Sciences bio-médicales et agricoles, 1-Phosphatidylinositol 3-Kinase -- metabolism, Actins -- metabolism, Animals, Butanols -- metabolism, Cell Line, Cell Movement -- physiology, Chemotaxis -- physiology, Cytoskeleton -- metabolism, Endocytosis, Enzyme Inhibitors -- metabolism, Fibroblasts -- cytology, Fibroblasts -- metabolism, Growth Substances -- metabolism, Mice, Oncogene Protein pp60(v-src) -- genetics, Oncogene Protein pp60(v-src) -- metabolism, Phenotype, Phospholipase D -- metabolism, Protein Synthesis Inhibitors -- metabolism, Rats, Signal Transduction -- physiology, Type C Phospholipases -- metabolism, Cell migration, Chemotaxis, PI 3-kinase, PLC, PLD, v-Src, info:eu-repo/semantics/article, info:ulb-repo/semantics/articlePeerReview, info:ulb-repo/semantics/openurl/article |
| URL: | |
| الإتاحة: | Open access content. Open access content 2 full-text file(s): info:eu-repo/semantics/openAccess | info:eu-repo/semantics/restrictedAccess |
| ملاحظة: | 2 full-text file(s): application/pdf | application/pdf English |
| أرقام أخرى: | EQY oai:dipot.ulb.ac.be:2013/52118 uri/info:doi/10.1242/jcs.01359 uri/info:pii/jcs.01359 uri/info:pmid/15340010 uri/info:scp/7444247517 local/VX-001604 764586246 |
| المصدر المساهم: | UNIVERSITE LIBRE DE BRUXELLES From OAIster®, provided by the OCLC Cooperative. |
| رقم الأكسشن: | edsoai.ocn764586246 |
| قاعدة البيانات: | OAIster |
| الوصف غير متاح. |