Role of regucalcin as an activator of sarcoplasmic reticulum Ca2+-ATPase activity in rat heart muscle

2002 ◽  
Vol 86 (1) ◽  
pp. 184-193 ◽  
Author(s):  
Masayoshi Yamaguchi ◽  
Rie Nakajima
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Heart Muscle ◽  
Rat Heart

scholarly journals Brain natriuretic peptide secretion in adult rat heart muscle cells: The role of calcium channels

2008 ◽  
Vol 101 (7-8) ◽  
pp. 459-463 ◽  
Author(s):  
Laurence Nader ◽  
Viviane Smayra ◽  
Victor Jebara ◽  
Patrick Bois ◽  
Daniel Potreau ◽  
...  
Keyword(s):  
Calcium Channels ◽  
Brain Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Heart Muscle ◽  
Rat Heart ◽  
Muscle Cells ◽  
Adult Rat ◽  
Heart Muscle Cells ◽  
Peptide Secretion

Role of cholesterol in the Ca2+ uptake and ATPase activity of fragmented sarcoplasmic reticulum

1972 ◽  
Vol 274 (1) ◽  
pp. 158-170 ◽  
Author(s):  
W. Drabikowski ◽  
M.G. Zarzała ◽  
A. Wroniszewska ◽  
E. Łagwińska ◽  
B. Drzewiecka
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Atpase Activity

scholarly journals Role of Calcium Binding by Sarcoplasmic Reticulum in the Contraction and Relaxation of Uterine Smooth Muscle

1969 ◽  
Vol 53 (4) ◽  
pp. 414-426 ◽  
Author(s):  
Mary E. Carsten
Keyword(s):  
Smooth Muscle ◽  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Calcium Binding ◽  
Sucrose Density Gradient ◽  
Differential Centrifugation ◽  
Uterine Smooth Muscle ◽  
Fraction I ◽  
Contraction And Relaxation

The binding of calcium by isolated sarcoplasmic reticulum from cow uterus was studied. Sarcoplasmic reticulum was prepared by differential centrifugation. Three fractions were obtained: I, sedimented between 2,500–15,000 x g; II at 40,000 x g; and III, at 150,000 x g. Fraction II was further purified on a sucrose density gradient. All three fractions contained considerable amounts of intrinsic calcium, mostly in fraction I. Calcium binding in the presence of ATP1 and Mg also was greatest in fraction I, followed by fraction II, with less in fraction III. Without ATP no calcium was taken up. 5 and 10 mM sodium azide partially inhibited calcium binding in fraction I, but not in fraction II, suggesting the presence of some mitochondria or mitochondrial fragments in fraction I. Calcium binding in fraction II was completely inhibited by 3 mM salyrgan; this fraction thus appears to be sarcoplasmic reticulum. ATPase activity was found in all three fractions, highest in fraction II. It is computed that calcium binding in fractions I and II, on the basis of a 50% yield of protein, is sufficient to elicit contraction by supplying calcium to the contractile proteins of the smooth muscle cell and to regulate relaxation and contraction.

scholarly journals Pyruvate carboxylation in the rat heart. Role of biotin-dependent enzymes

1989 ◽  
Vol 257 (3) ◽  
pp. 913-916 ◽  
Author(s):  
K E Sundqvist ◽  
J K Hiltunen ◽  
I E Hassinen
Keyword(s):  
Heart Muscle ◽  
Malic Enzyme ◽  
Rat Heart ◽  
Pyruvate Carboxylase ◽  
Mass Action ◽  
Kinetic Properties ◽  
Biotin Deficiency ◽  
Perfused Rat Heart ◽  
Pyruvate Carboxylation

Pyruvate carboxylation in the isolated perfused rat heart was studied under steady-state conditions. A biotin deficiency resulting in a 90% decrease in myocardial pyruvate carboxylase left the pyruvate carboxylation rate unchanged. Pyruvate carboxylation in heart muscle must therefore take place by means of an enzyme which does not contain biotin. The kinetic properties and mass-action ratio of the NADP-linked malic enzyme in heart muscle can be taken as circumstantial evidence in favour of the role of malic enzyme in pyruvate carboxylation in myocardium.

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