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J Physiol Volume 527, Number 1, 3-9, August 15, 2000
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The Journal of Physiology (2000), 527.1, pp. 3-9
© Copyright 2000 The Physiological Society

Laminin binding to beta1-integrins selectively alters beta1- and beta2-adrenoceptor signalling in cat atrial myocytes

Yong Gao Wang, Allen M. Samarel and Stephen L. Lipsius

Loyola University Chicago, Stritch School of Medicine, Department of Physiology and The Cardiovascular Institute, Maywood, IL 60153, USA

  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 µM), 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 µM), a selective beta1-AR antagonist, inhibited the effects of ISO in cells on glass but not laminin. Conversely, 0·1 µM 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 µM), 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 µM 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.



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