Subcellular localization of phospholipase C isoforms in vascular smooth muscle
Autor: | Edward F. LaBelle, Erzsébet Polyák, Ken Wilson |
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Rok vydání: | 2002 |
Předmět: |
Male
Tail Gene isoform Agonist Vascular smooth muscle medicine.drug_class Phospholipase C beta Biology Muscle Smooth Vascular Rats Sprague-Dawley Norepinephrine Cytosol Cell surface receptor Centrifugation Density Gradient medicine Animals Molecular Biology Phospholipase C Phospholipase C gamma Cell Membrane Antibodies Monoclonal Arteries Cell Biology Smooth muscle contraction Subcellular localization Rats Cell biology Isoenzymes Biochemistry Type C Phospholipases Adrenergic alpha-Agonists Phospholipase C delta Subcellular Fractions |
Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1583:273-278 |
ISSN: | 1388-1981 |
DOI: | 10.1016/s1388-1981(02)00218-4 |
Popis: | The phospholipase C (PLC) isoform most important during agonist-activated IP(3) production in vascular smooth muscle is still unknown. When PLC activity in rat tail artery homogenate was determined, this activity was shown to be inhibited by an antibody directed against PLCbeta2. Antibodies directed against the gamma1, beta1, beta3 and delta1 isoforms of PLC failed to inhibit PLC activity in this tissue. Both PLCbeta2 and PLCgamma1 were isolated from rat tail artery by DEAE column chromatography and PLCbeta2 activity was shown to be 3-fold greater than PLCgamma1 activity. When rat tail artery was treated with norepinephrine (10 mM), PLCbeta2 was shown to translocate from cytosol to membranes. When subcellular fractions of rat tail artery were isolated by sucrose density gradient centrifugation, including nuclei, plasma membrane, and cytosol, PLCbeta2 was detected in the plasma membrane and the cytosol but not in the nuclei. PLCdelta1 and PLCgamma1 were found only in cytosol. This evidence is consistent with the model wherein an agonist such as norepinephrine can activate smooth muscle contraction via interaction with a plasma membrane receptor which can easily interact with a plasma membrane-associated isoform of PLC, such as PLCbeta2. |
Databáze: | OpenAIRE |
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