Photoaffinity labeling and phosphorylation of the dihydropyridine binding ($alpha;1 subunit of the voltage-regulated Ca2+ channel from rabbit heart sarcolemma *1. Department of Pharmacology, Medical Sciences Bldg., University of Toronto, Toronto, Canada, M5S 1A8

1988 ◽  
Vol 20 ◽  
pp. 39
Keyword(s):  
Photoaffinity Labeling ◽  
Rabbit Heart ◽  
Medical Sciences ◽  
University Of Toronto ◽  
Heart Sarcolemma

scholarly journals The First J. C. Richardson Lecture: “That ‘I Am’ ”

1974 ◽  
Vol 1 (2) ◽  
pp. 86-91
Author(s):  
Denis Williams
Keyword(s):  
Senior Physician ◽  
Medical Sciences ◽  
National Hospital ◽  
University Of Toronto

The first J. C. Richardson lecture was given by Dr. Denis Williams, Editor of “Brain,” and The Senior Physician, The National Hospital, Queen Square, London W.C.I. It was presented in the Medical Sciences Building, University of Toronto on January 28th, 1974 and is printed here in its entirety.

Inhibition of Na+ and K+-stimulated ATPase of rabbit heart sarcolemma after administration of heparin

1978 ◽  
Vol 81 (1) ◽  
pp. 168-175 ◽  
Author(s):  
J.N. Karli ◽  
G.A. Karikas ◽  
G.M. Levis ◽  
S.N. Moulopoulos
Keyword(s):  
Rabbit Heart ◽  
Heart Sarcolemma

Calcium ions inhibit the allosteric interaction between the dihydropyridine and phenylalkylamine binding site on the voltage-gated calcium channel in heart sarcolemma but not in skeletal muscle transverse tubules

1990 ◽  
Vol 68 (11) ◽  
pp. 1389-1395 ◽  
Author(s):  
Brian J. Murphy ◽  
Balwant S. Tuana
Keyword(s):  
Skeletal Muscle ◽  
Calcium Channel ◽  
Binding Sites ◽  
Rabbit Heart ◽  
Negative Cooperativity ◽  
Channel Blockers ◽  
Transverse Tubules ◽  
High Affinity ◽  
Heart Sarcolemma ◽  
Negative Effect

Calcium channel blockers bind with high affinity to sites on the voltage-sensitive Ca2+ channel. Radioligand binding studies with various Ca2+ channel blockers have facilitated identification and characterization of binding sites on the channel structure. In the present study we evaluated the relationship between the binding sites for the Ca2+ channel blockers on the voltage-sensitive Ca2+ channel from rabbit heart sarcolemma and rabbit skeletal muscle transverse tubules. [3H]PN200-110 binds with high affinity to a single population of sites on the voltage-sensitive Ca2+ channel in both rabbit heart sarcolemma and skeletal muscle transverse tubules. [3H]PN200-110 binding was not affected by added Ca2+ whereas EGTA and EDTA noncompetitively inhibited binding in both types of membrane preparations. EDTA was a more potent inhibitor of [3H]PN200-110 binding than EGTA. Diltiazem stimulates the binding of [3H]PN200-110 in a temperature-sensitive manner. Verapamil inhibited binding of [3H]PN200-110 to both types of membrane preparations in a negative manner, although this effect was of a complex nature in skeletal muscle transverse tubules. The negative effect of verapamil on [3H]PN200-110 binding in cardiac muscle was completely reversed by Ca2+. On the other hand, Ca2+ was without effect on the negative cooperativity seen between verapamil and [3H]PN200-110 binding in skeletal muscle transverse tubules. Since Ca2+ did not affect [3H]PN200-110 binding to membranes, we would like to suggest that Ca2+ is modulating the negative effect of verapamil on [3H]PN200-110 binding through a distinct Ca2+ binding site. The differential effect of Ca2+ on the negative cooperativity between verapamil and [3H]PN200-110 binding in rabbit heart and skeletal muscle membrane may reflect molecular and functional differences between voltage-sensitive Ca2+ channels in these two types of tissue.Key words: Ca2+ channel, sarcolemma, calcium channel blockers.

scholarly journals The pyramids of Gizeh, reductionist research-based progress, unintended consequences and the complexity of medicine

2018 ◽  
Vol 41 ◽  
pp. 29-31
Author(s):  
Bing Siang Gan
Keyword(s):  
Cell Biology ◽  
Clinical Investigation ◽  
Health Centre ◽  
Unintended Consequences ◽  
Medical Sciences ◽  
Microsurgical Reconstruction ◽  
University Of Toronto ◽  
Medical Biophysics ◽  
University Of Calgary ◽  
Complex Wound

Bing graduated from the Medical Faculty at Erasmus University in Rotterdam, The Netherlands in 1988. He then completed a PhD in Medical Sciences (University of Calgary), internship (University of Regina) and surgical residency (University of Western Ontario) and post-residency clinical fellowships (University of Toronto and Harvard University) followed by a research post-doctoral fellowship (Department of Cell Biology, University of Toronto). Bing has been with the Roth | McFarlane Hand and Upper Limb Centre at St. Joseph’s Health Centre since 1998. He is a Professor of Surgery and Medical Biophysics at Western University. His clinical practice focuses on hand and wrist surgery, microsurgical reconstruction and complex wound reconstruction, with a particular clinical and research interest in patients with Dupuytren’s contracture. He is also interested in other fibrosing conditions, such as hypertrophic scarring. Bing was a Canadian Society for Clinical Investigation (CSCI) Member of Council 2004-2011and CSCI President 2009-2011.

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