Expression of Plasma Membrane Calcium ATPases in Phenotypically Distinct Canine Vascular Smooth Muscle Cells
| Autor: | Thorunn Helgason, Joel Abramowitz, Timothy Odebunmi, Julius C. Allen, Aslihan Aydemir-Koksoy, Sandra Jemelka, Charles L. Seidel |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Male
Gene isoform DNA Complementary Vascular smooth muscle Molecular Sequence Data Gene Expression Calcium-Transporting ATPases Muscle Smooth Vascular Calcium in biology Wortmannin Plasma Membrane Calcium-Transporting ATPases chemistry.chemical_compound Dogs Downregulation and upregulation Adventitia medicine Animals Humans Saphenous Vein Amino Acid Sequence RNA Messenger Enzyme Inhibitors Cation Transport Proteins Molecular Biology Cells Cultured DNA Primers Messenger RNA Phosphoinositide 3-kinase Base Sequence Sequence Homology Amino Acid biology Cell Membrane Molecular biology Androstadienes Alternative Splicing Carotid Arteries Phenotype medicine.anatomical_structure chemistry biology.protein Female Cardiology and Cardiovascular Medicine |
| Zdroj: | Journal of Molecular and Cellular Cardiology. 32:777-789 |
| ISSN: | 0022-2828 |
| Popis: | Our laboratory has identified at least two types of vascular smooth muscle cells (VSMCs) that exist in canine arteries and veins: type 1 cells, located in the media express muscle specific proteins but do not proliferate in culture; and type 2 cells, located in both media and adventitia, do not express muscle specific protein but proliferate in culture. Plasma membrane Ca(2+)-ATPases (PMCAs) have been implicated in proliferation control. The present study examines the expression of PMCA isoforms and calmodulin-binding domain splice variants in these two types of canine VSMCs. PMCA protein was found in both type 1 and type 2 cells. Reverse transcriptase-polymerase chain reaction assays were developed for canine PMCA calmodulin-binding domain splice variants. We cloned and sequenced isolates corresponding to PMCA1b, 4a and 4b from canine VSMCs. PMCA 2 and 3 were not detected. Freshly isolated type 1 cells expressed PMCA 1b, 4a and 4b, while freshly isolated type 2 cells expressed PMCA1b and 4b. Upon placement in culture, type 2 cells originating from either carotid artery or saphenous vein demonstrated a time-dependent upregulation of PMCA4a mRNA. Treatment with the phosphoinositide 3-kinase inhibitor wortmannin produced concentration-dependent inhibition of both PMCA4a upregulation and [(3)H]thymidine incorporation. These findings suggest a role for phosphoinositide 3-kinase in regulating PMCA expression, which may be important in the control of Ca(2+)-sensitive VSMC functions. |
| Databáze: | OpenAIRE |
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