H1 and H2 histamine receptors mediate the production of inositol phosphates but not cAMP in human breast epithelial cells
Objective: In the present work we studied the H1 and H2 histamine receptor expression and function in HBL- 100 and MCF-10A cells, derived from non-tumorigenic human breast epithelia, and in MCF-10T, the H-ras-transfected MCF-10A counterpart. The signal transduction pathways associated with these rec...
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2002
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10233830_v51_n1_p1_Davio http://hdl.handle.net/20.500.12110/paper_10233830_v51_n1_p1_Davio |
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paper:paper_10233830_v51_n1_p1_Davio2023-06-08T16:00:08Z H1 and H2 histamine receptors mediate the production of inositol phosphates but not cAMP in human breast epithelial cells Mladovan, Alejandro G. Shayo, Carina C. C-los C-myc Human breast epithelial cells Signal transduction cyclic AMP histamine H1 receptor histamine H2 receptor inositol phosphate mepyramine pertussis toxin phosphatidylinositide tiotidine cyclic AMP guanine nucleotide binding protein histamine H1 receptor histamine H2 receptor inositol phosphate article binding site breast epithelium cell growth controlled study gene expression human human cell oncogene c fos oncogene c myc proto oncogene regulatory mechanism signal transduction biosynthesis breast cell culture epithelium cell female metabolism oncogene oncogene myc physiology signal transduction Breast Cells, Cultured Cyclic AMP Epithelial Cells Female Genes, fos Genes, myc GTP-Binding Proteins Humans Inositol Phosphates Receptors, Histamine H1 Receptors, Histamine H2 Signal Transduction Objective: In the present work we studied the H1 and H2 histamine receptor expression and function in HBL- 100 and MCF-10A cells, derived from non-tumorigenic human breast epithelia, and in MCF-10T, the H-ras-transfected MCF-10A counterpart. The signal transduction pathways associated with these receptors, and the expression of proto-oncogenes c-los, c-myc and c-jun at the mRNA and protein levels, were examined. Results: Saturation analysis using intact cells, showed two binding sites for [3H]tiotidine and [3H]mepyramine. Pretreatment of purified membrane with guanosine 5′-y thiotriphosphate resulted in the loss of the low affinity component for [3H]tiotidine binding, and of the high affinity component for [3H]mepyramine. In both cases, there was no modification in the total number of sites for both ligands. Neither H1 nor H2 agonists stimulated cyclic AMP production, though this pathway is functional in these cells. On the other hand, both H1 and H2 agonists enhanced phosphoinositide turnover in a dose-dependent fashion, and this induction is pertussis toxin-insensitive. H1 and H2 agonists did not influence the expression of c-myc or c-fos mRNA, nor their encoded proteins. Conclusions: These results indicate that the three cell lines examined showed functional H1 and H2 histamine receptors, which are involved in the metabolic turnover of inositol phosphates but are ineffective in the modulation of the cyclic AMP response. The fact that H2 receptors have lost their ability to stimulate cyclic AMP production would imply the loss of a regulatory mechanism of cell growth. Fil:Mladovan, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Shayo, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2002 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10233830_v51_n1_p1_Davio http://hdl.handle.net/20.500.12110/paper_10233830_v51_n1_p1_Davio |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
C-los C-myc Human breast epithelial cells Signal transduction cyclic AMP histamine H1 receptor histamine H2 receptor inositol phosphate mepyramine pertussis toxin phosphatidylinositide tiotidine cyclic AMP guanine nucleotide binding protein histamine H1 receptor histamine H2 receptor inositol phosphate article binding site breast epithelium cell growth controlled study gene expression human human cell oncogene c fos oncogene c myc proto oncogene regulatory mechanism signal transduction biosynthesis breast cell culture epithelium cell female metabolism oncogene oncogene myc physiology signal transduction Breast Cells, Cultured Cyclic AMP Epithelial Cells Female Genes, fos Genes, myc GTP-Binding Proteins Humans Inositol Phosphates Receptors, Histamine H1 Receptors, Histamine H2 Signal Transduction |
| spellingShingle |
C-los C-myc Human breast epithelial cells Signal transduction cyclic AMP histamine H1 receptor histamine H2 receptor inositol phosphate mepyramine pertussis toxin phosphatidylinositide tiotidine cyclic AMP guanine nucleotide binding protein histamine H1 receptor histamine H2 receptor inositol phosphate article binding site breast epithelium cell growth controlled study gene expression human human cell oncogene c fos oncogene c myc proto oncogene regulatory mechanism signal transduction biosynthesis breast cell culture epithelium cell female metabolism oncogene oncogene myc physiology signal transduction Breast Cells, Cultured Cyclic AMP Epithelial Cells Female Genes, fos Genes, myc GTP-Binding Proteins Humans Inositol Phosphates Receptors, Histamine H1 Receptors, Histamine H2 Signal Transduction Mladovan, Alejandro G. Shayo, Carina C. H1 and H2 histamine receptors mediate the production of inositol phosphates but not cAMP in human breast epithelial cells |
| topic_facet |
C-los C-myc Human breast epithelial cells Signal transduction cyclic AMP histamine H1 receptor histamine H2 receptor inositol phosphate mepyramine pertussis toxin phosphatidylinositide tiotidine cyclic AMP guanine nucleotide binding protein histamine H1 receptor histamine H2 receptor inositol phosphate article binding site breast epithelium cell growth controlled study gene expression human human cell oncogene c fos oncogene c myc proto oncogene regulatory mechanism signal transduction biosynthesis breast cell culture epithelium cell female metabolism oncogene oncogene myc physiology signal transduction Breast Cells, Cultured Cyclic AMP Epithelial Cells Female Genes, fos Genes, myc GTP-Binding Proteins Humans Inositol Phosphates Receptors, Histamine H1 Receptors, Histamine H2 Signal Transduction |
| description |
Objective: In the present work we studied the H1 and H2 histamine receptor expression and function in HBL- 100 and MCF-10A cells, derived from non-tumorigenic human breast epithelia, and in MCF-10T, the H-ras-transfected MCF-10A counterpart. The signal transduction pathways associated with these receptors, and the expression of proto-oncogenes c-los, c-myc and c-jun at the mRNA and protein levels, were examined. Results: Saturation analysis using intact cells, showed two binding sites for [3H]tiotidine and [3H]mepyramine. Pretreatment of purified membrane with guanosine 5′-y thiotriphosphate resulted in the loss of the low affinity component for [3H]tiotidine binding, and of the high affinity component for [3H]mepyramine. In both cases, there was no modification in the total number of sites for both ligands. Neither H1 nor H2 agonists stimulated cyclic AMP production, though this pathway is functional in these cells. On the other hand, both H1 and H2 agonists enhanced phosphoinositide turnover in a dose-dependent fashion, and this induction is pertussis toxin-insensitive. H1 and H2 agonists did not influence the expression of c-myc or c-fos mRNA, nor their encoded proteins. Conclusions: These results indicate that the three cell lines examined showed functional H1 and H2 histamine receptors, which are involved in the metabolic turnover of inositol phosphates but are ineffective in the modulation of the cyclic AMP response. The fact that H2 receptors have lost their ability to stimulate cyclic AMP production would imply the loss of a regulatory mechanism of cell growth. |
| author |
Mladovan, Alejandro G. Shayo, Carina C. |
| author_facet |
Mladovan, Alejandro G. Shayo, Carina C. |
| author_sort |
Mladovan, Alejandro G. |
| title |
H1 and H2 histamine receptors mediate the production of inositol phosphates but not cAMP in human breast epithelial cells |
| title_short |
H1 and H2 histamine receptors mediate the production of inositol phosphates but not cAMP in human breast epithelial cells |
| title_full |
H1 and H2 histamine receptors mediate the production of inositol phosphates but not cAMP in human breast epithelial cells |
| title_fullStr |
H1 and H2 histamine receptors mediate the production of inositol phosphates but not cAMP in human breast epithelial cells |
| title_full_unstemmed |
H1 and H2 histamine receptors mediate the production of inositol phosphates but not cAMP in human breast epithelial cells |
| title_sort |
h1 and h2 histamine receptors mediate the production of inositol phosphates but not camp in human breast epithelial cells |
| publishDate |
2002 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10233830_v51_n1_p1_Davio http://hdl.handle.net/20.500.12110/paper_10233830_v51_n1_p1_Davio |
| work_keys_str_mv |
AT mladovanalejandrog h1andh2histaminereceptorsmediatetheproductionofinositolphosphatesbutnotcampinhumanbreastepithelialcells AT shayocarinac h1andh2histaminereceptorsmediatetheproductionofinositolphosphatesbutnotcampinhumanbreastepithelialcells |
| _version_ |
1768544649926934528 |