pubmed-article:10944166 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10944166 | lifeskim:mentions | umls-concept:C0007450 | lld:lifeskim |
pubmed-article:10944166 | lifeskim:mentions | umls-concept:C2334101 | lld:lifeskim |
pubmed-article:10944166 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:10944166 | lifeskim:mentions | umls-concept:C1523874 | lld:lifeskim |
pubmed-article:10944166 | pubmed:dateCreated | 2000-10-5 | lld:pubmed |
pubmed-article:10944166 | pubmed:abstractText | 1. Perforated patch recordings were used to determine how plating atrial cells on laminin alters beta-adrenergic receptor (beta-AR) regulation of L-type Ca2+ current (ICa,L). 2. Isoproterenol (isoprenaline; ISO; 0.01 microM), a non-selective beta-AR agonist, elicited a greater stimulation of ICa,L in cells plated on laminin (+79 +/- 16 %; n = 17) than on glass (+33 +/- 5 %; n = 23). Also, desensitization to ISO was greater in cells on laminin (-16 +/- 2 %) than on glass (-3 +/- 1 %). Atenolol (0.1 microM), a selective beta1-AR antagonist, inhibited the effects of ISO in cells on glass but not laminin. Conversely, 0.1 microM ICI 118,551, a selective beta2-AR antagonist, inhibited the effects of ISO in cells on laminin but not glass. With beta2-ARs blocked, ISO-induced stimulation of ICa,L was greater in cells on glass than laminin. 3. Zinterol (0.01-0.1 microM), a selective beta2-AR agonist, elicited a greater stimulation of ICa,L in cells on laminin than on glass. The effects of zinterol were blocked by ICI 118,551. 4. ISO-induced stimulation of ICa,L was greater in cells plated on an alphabeta1-integrin antibody than on glass. Also, addition of 20 microM cytochalasin D to cells on laminin prevented the enhanced effects of ISO typically elicited in cells on laminin alone. 5. We conclude that laminin binding to alphabeta1-integrins, in conjunction with the actin cytoskeleton, reduces beta1-AR and enhances beta2-AR signalling which regulates ICa,L. This novel mechanism may contribute to remodelling of beta-AR signalling in the failing heart. | lld:pubmed |
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pubmed-article:10944166 | pubmed:language | eng | lld:pubmed |
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pubmed-article:10944166 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10944166 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10944166 | pubmed:month | Aug | lld:pubmed |
pubmed-article:10944166 | pubmed:issn | 0022-3751 | lld:pubmed |
pubmed-article:10944166 | pubmed:author | pubmed-author:LipsiusS LSL | lld:pubmed |
pubmed-article:10944166 | pubmed:author | pubmed-author:SamarelA MAM | lld:pubmed |
pubmed-article:10944166 | pubmed:author | pubmed-author:WangY GYG | lld:pubmed |
pubmed-article:10944166 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10944166 | pubmed:day | 15 | lld:pubmed |
pubmed-article:10944166 | pubmed:volume | 527 Pt 1 | lld:pubmed |
pubmed-article:10944166 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10944166 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10944166 | pubmed:pagination | 3-9 | lld:pubmed |
pubmed-article:10944166 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:10944166 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10944166 | pubmed:articleTitle | Laminin binding to beta1-integrins selectively alters beta1- and beta2-adrenoceptor signalling in cat atrial myocytes. | lld:pubmed |
pubmed-article:10944166 | pubmed:affiliation | Loyola University Chicago, Stritch School of Medicine, Department of Physiology and The Cardiovascular Institute, Maywood, IL 60153, USA. | lld:pubmed |
pubmed-article:10944166 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10944166 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:10944166 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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