scholarly journals Lipoprotein lipase activity of rat cardiac muscle. The intracellular distribution of the enzyme between fractions prepared from cardiac muscle and cells isolated from the hearts of fed and starved animals

1979 ◽  
Vol 181 (1) ◽  
pp. 83-93 ◽  
Author(s):  
P Chohan ◽  
A Cryer
Keyword(s):  
Cardiac Muscle ◽  
Lipoprotein Lipase ◽  
Diethyl Ether ◽  
Lipase Activity ◽  
Microsomal Fraction ◽  
Specific Activity ◽  
Lipoprotein Lipase Activity ◽  
Powder Preparation ◽  
Isolated Cells ◽  
Relative Specific Activity

1. Subcellular fractions, characterized by using morphological, compositional and enzymic markers, were prepared from rat heart tissue and cells isolated from the hearts of fed and 24 h-starved rats. 2. The lipoprotein lipase activity of fractions from whole tissue and isolated cells was determined in either fresh fractions or in acetone/diethyl ether powders of the fractions. 3. Lipoprotein lipase activity was present in all the fractions from tissue and cells, but was found to be of highest relative specific activity in the microsomal () fractions. 4. In fractions prepared from the isolated cells of hearts from starved rats the proportion of the total lipoprotein lipase present and its relative specific activity in the microsomal fraction were greater than in the equivalent fractions from fed animals. 5. The enhancement of lipoprotein lipase activity as a result of the acetone/diethyl ether powder preparation of fractions was most extensive in the microsomal fractions. 6. Investigation of the microsomal fraction showed that the lipoprotein lipase activity present was in two pools, one of which was within endoplasmic-reticulum vesicles. 7. The observations were consistent with the possibility that the cardiac-muscle cell could be the origin of the lipoprotein lipase activity functional in triacylglycerol uptake by the heart.

scholarly journals Lipoprotein Lipase Activity and mRNA Are Up-Regulated by Refeeding in Adipose Tissue and Cardiac Muscle of Sheep

2000 ◽  
Vol 130 (4) ◽  
pp. 749-756 ◽  
Author(s):  
Muriel Bonnet ◽  
Christine Leroux ◽  
Yannick Faulconnier ◽  
Jean-François Hocquette ◽  
François Bocquier ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Cardiac Muscle ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipoprotein Lipase Activity

scholarly journals The lipoprotein lipase (clearing-factor lipase) activity of cells isolated from rat cardiac muscle

1978 ◽  
Vol 174 (2) ◽  
pp. 663-666 ◽  
Author(s):  
P Chohan ◽  
A Cryer
Keyword(s):  
Cardiac Muscle ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipoprotein Lipase Activity ◽  
Cell Type ◽  
Cardiac Muscle Cells ◽  
Adult Rat ◽  
Rat Hearts ◽  
Major Cell Type ◽  
Total Lipoprotein

The total lipoprotein lipase activity recovered in suspension of cells prepared from adult rat hearts was unaffected by the nutritional state of the animals used. The enzyme activity present in the cell suspensions was almost exclusively associated with the cardiac muscle cells present as the major cell type.

scholarly journals Lipoprotein lipase activity of rat cardiac muscle. Changes in the enzyme activity during incubations of isolated cardiac-muscle cells in vitro

1980 ◽  
Vol 186 (3) ◽  
pp. 873-879 ◽  
Author(s):  
P Chohan ◽  
A Cryer
Keyword(s):  
Enzyme Activity ◽  
Cardiac Muscle ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Muscle Cells ◽  
Total Activity ◽  
Lipoprotein Lipase Activity ◽  
Cardiac Muscle Cells ◽  
Intracellular Enzyme

1. Isolated cardiac-muscle cells from the hearts of adult rats were shown to retain a high amount of viability during 4 h of incubation when viability was assessed by Trypan Bue stain exclusion and intracellular enzyme leakage. 2. The cells also retained their ability to take up O2 and utilize added substrates over the period of incubation at both 25 and 30 degrees C. 3. When cells from the hearts of fed rats were incubated in a buffered-salts solution at pH 7.4 in the presence of amino acids and heparin, lipoprotein lipase activity in the medium increased progressively. 4. During these incubations the intracellular activity of the enzyme remained constant and the total activity of lipoprotein lipase in the system (cells plus medium) increased by 80% over the 4 h of incubation at 25 degrees C. 5. In the absence of heparin only low amounts of enzyme activity were detectable in the medium and the total lipoprotein lipase activity in the system remained constant. 6. The measurement of lipoprotein lipase activity in either fresh homogenates of the cells or in homogenates of acetone/diethyl ether-dried powders of the cells had no effect on the overall pattern of activity change during the incubations, although as reported previously the total activity detected with acetone/diethyl either-dried preparations was approx. 3-fold higher than with fresh cell homogenates. 7. The observations were compared with published data on lipoprotein lipase activity changes in neonatal heart cell cultures maintained in vitro.

scholarly journals Retention of glucose by N-linked oligosaccharide chains impedes expression of lipoprotein lipase activity: effect of castanospermine.

1992 ◽  
Vol 33 (9) ◽  
pp. 1343-1349
Author(s):  
H Masuno ◽  
EJ Blanchette-Mackie ◽  
CJ Schultz ◽  
AE Spaeth ◽  
RO Scow ◽  
...  
Keyword(s):  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipoprotein Lipase Activity ◽  
Activity Effect
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