scholarly journals The cAMP-binding Popdc proteins have a redundant function in the heart

2014 ◽  
Vol 42 (2) ◽  
pp. 295-301 ◽  
Author(s):  
Thomas Brand ◽  
Subreena L. Simrick ◽  
Kar Lai Poon ◽  
Roland F.R. Schindler

Popdc (Popeye-domain-containing) genes encode membrane-bound proteins and are abundantly present in cardiac myocytes and in skeletal muscle fibres. Functional analysis of Popdc1 (Bves) and Popdc2 in mice and of popdc2 in zebrafish revealed an overlapping role for proper electrical conduction in the heart and maintaining structural integrity of skeletal muscle. Popdc proteins mediate cAMP signalling and modulate the biological activity of interacting proteins. The two-pore channel TREK-1 interacts with all three Popdc proteins. In Xenopus oocytes, the presence of Popdc proteins causes an enhanced membrane transport leading to an increase in TREK-1 current, which is blocked when cAMP levels are increased. Another important Popdc-interacting protein is caveolin 3, and the loss of Popdc1 affects caveolar size. Thus a family of membrane-bound cAMP-binding proteins has been identified, which modulate the subcellular localization of effector proteins involved in organizing signalling complexes and assuring proper membrane physiology of cardiac myocytes.

1981 ◽  
Vol 59 (4) ◽  
pp. 335-341 ◽  
Author(s):  
C. M. Thomson ◽  
W. F. Dryden

The effects of Co2+, Mn2+, and La3+ (2 mM) and verapamil (5 × 10−6 M) on membrane conductance (Gm) and resting potential (Em) were studied in chick skeletal muscle fibres developing in culture. Cobalt and manganese had no effect on Gm at any time during myogenesis but verapamil caused a decrease in Gm in immature myotubes. This effect diminished with time and was absent by 3 days after myoblast fusion. Lanthanum caused an increase in Gm at all stages of development. All the agents studied caused a significant depolarization of Em. It is concluded that there is no resting calcium conductance in developing skeletal muscle but that there may be a resting sodium conductance which declines with maturation. Lanthanum may increase Gm by displacing membrane-bound calcium and destabilizing membrane structure. All the agents studied were thought to induce depolarization by an inhibitory action on (Na+ + K+)-ATPase.


1989 ◽  
Vol 504 (2) ◽  
pp. 306-310 ◽  
Author(s):  
Inger Nennesmo ◽  
Tomas Olsson ◽  
Åke Ljungdahl ◽  
Krister Kristensson ◽  
Peter H. Van der Meide

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