{"title":"血小板源性生长因子和缓激素刺激ki -ras转化成纤维细胞的磷酸肌肽水解","authors":"Takahiko Kumada , Yoshiko Banno , Hideo Miyata , Yoshinori Nozawa","doi":"10.1016/0020-711X(94)90077-9","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Signal transduction in response to platelet-derived growth factor (PDGF)-BB and bradykinin (BK) have been examined by measuring inositol polyphosphate formation in NIH3T3 fibrobalst and v-Ki-<em>ras</em> -transformed NIH3T3 fibroblast (DT).</p></span></li><li><span>2.</span><span><p>2. The PDGF-induced inositol polyphosphate formation in NIH3T3 was greater than that in DT cells, in which autophosphorylation of PDGF receptor and tyrosine phosphorylation of phospholipase C (PLC)-γ 1 were suppressed when examined by immunoblotting with anti-phosphotyrosine antibody.</p></span></li><li><span>3.</span><span><p>3. On the other hand, BK-stimulation produced a much higher level of inositol polyphosphate in DT cells which have a greater number of BK receptors.</p></span></li><li><span>4.</span><span><p>4. These results indicate that in Ki-<em>ras</em> transformed cells the decrease (caused by PDGF) and the increase (caused by BK) in phosphoinositide hydrolysis are due to the defective autophosphorylation of PDGF receptors leading to a reduction in PLC-γ 1 tyrosine phosphorylation and the overexpression of BK receptors, respectively.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 8","pages":"Pages 1049-1054"},"PeriodicalIF":0.0000,"publicationDate":"1994-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90077-9","citationCount":"1","resultStr":"{\"title\":\"Phosphoinositide hydrolysis in Ki-ras-transformed fibroblasts stimulated by platelet-derived growth factor and bradykinin\",\"authors\":\"Takahiko Kumada , Yoshiko Banno , Hideo Miyata , Yoshinori Nozawa\",\"doi\":\"10.1016/0020-711X(94)90077-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. Signal transduction in response to platelet-derived growth factor (PDGF)-BB and bradykinin (BK) have been examined by measuring inositol polyphosphate formation in NIH3T3 fibrobalst and v-Ki-<em>ras</em> -transformed NIH3T3 fibroblast (DT).</p></span></li><li><span>2.</span><span><p>2. The PDGF-induced inositol polyphosphate formation in NIH3T3 was greater than that in DT cells, in which autophosphorylation of PDGF receptor and tyrosine phosphorylation of phospholipase C (PLC)-γ 1 were suppressed when examined by immunoblotting with anti-phosphotyrosine antibody.</p></span></li><li><span>3.</span><span><p>3. On the other hand, BK-stimulation produced a much higher level of inositol polyphosphate in DT cells which have a greater number of BK receptors.</p></span></li><li><span>4.</span><span><p>4. These results indicate that in Ki-<em>ras</em> transformed cells the decrease (caused by PDGF) and the increase (caused by BK) in phosphoinositide hydrolysis are due to the defective autophosphorylation of PDGF receptors leading to a reduction in PLC-γ 1 tyrosine phosphorylation and the overexpression of BK receptors, respectively.</p></span></li></ul></div>\",\"PeriodicalId\":13733,\"journal\":{\"name\":\"International Journal of Biochemistry\",\"volume\":\"26 8\",\"pages\":\"Pages 1049-1054\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0020-711X(94)90077-9\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Journal of Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0020711X94900779\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020711X94900779","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Phosphoinositide hydrolysis in Ki-ras-transformed fibroblasts stimulated by platelet-derived growth factor and bradykinin
1.
1. Signal transduction in response to platelet-derived growth factor (PDGF)-BB and bradykinin (BK) have been examined by measuring inositol polyphosphate formation in NIH3T3 fibrobalst and v-Ki-ras -transformed NIH3T3 fibroblast (DT).
2.
2. The PDGF-induced inositol polyphosphate formation in NIH3T3 was greater than that in DT cells, in which autophosphorylation of PDGF receptor and tyrosine phosphorylation of phospholipase C (PLC)-γ 1 were suppressed when examined by immunoblotting with anti-phosphotyrosine antibody.
3.
3. On the other hand, BK-stimulation produced a much higher level of inositol polyphosphate in DT cells which have a greater number of BK receptors.
4.
4. These results indicate that in Ki-ras transformed cells the decrease (caused by PDGF) and the increase (caused by BK) in phosphoinositide hydrolysis are due to the defective autophosphorylation of PDGF receptors leading to a reduction in PLC-γ 1 tyrosine phosphorylation and the overexpression of BK receptors, respectively.
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