scholarly journals Changes in the phospholipid catabolism of mitochondria and microsomes during the development of rat liver

1981 ◽  
Vol 200 (3) ◽  
pp. 521-528 ◽  
Author(s):  
J K Pollak ◽  
W Harsas
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Rat Liver ◽  
Acid Formation ◽  
Liver Fatty Acid ◽  
Adult Rat ◽  
Degree Of Unsaturation ◽  
Esterified Fatty Acids

The lipolytic activities of mitochondrial and microsomal fractions (‘microsomes’) isolated from foetal, suckling and adult rat liver were compared. The catabolism of endogenous phospholipids was followed by measuring the loss of phospholipids and the appearance of non-esterified fatty acids and lysophosphatides. The rate of mitochondrial phospholipid catabolism does not change significantly during development, but the rate of lipolysis of microsomal phospholipids increases 3-fold during development. Balance studies showed that, in mitochondria and microsomes of foetal, suckling and adult rat liver, fatty acid formation is greatly in excess of the fatty acids that can be accounted for by measuring phospholipid disappearance and lysophosphatide appearance. The hypothesis that this excess fatty acid formation resulted from the lipolysis of mitochondrial and microsomal triacylglycerols were tested and confirmed by preliminary experiments. Mitochondria and microsomes isolated from all developmental ages investigated had phospholipases with A1 and A2 activities. The degree of unsaturation of the fatty acids derived from the phospholipids of mitochondria did not vary significantly during development.

Effect of Adrenalectomy on the Incorporation of Acetate Into Fatty Acids, Cholesterol and Acetoacetic Acid by Rat Liver Slices

1955 ◽  
Vol 184 (1) ◽  
pp. 59-62 ◽  
Author(s):  
W. F. Perry ◽  
Helen F. Bowen
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Rat Liver ◽  
Acid Formation ◽  
Acetoacetic Acid ◽  
Adrenalectomized Animal ◽  
Liver Slices ◽  
Adrenalectomized Rats

The incorporation of C14 acetate into fatty acids, cholesterol, acetoacetic acid and CO2 by liver slices of intact and adrenalectomized rats was studied, the slices being incubated in bicarbonate and phosphate buffers. It was found that in both buffer systems incorporation into fatty acids and cholesterol was depressed while incorporation into acetoacetic acid was unaffected by adrenalectomy. However, total acetoacetic acid formation by the slices tended to be higher in preparations from adrenalectomized animals. The amount of acetate carbon appearing as CO2 was similar with slices from both types of animals. Bicarbonate was found to be a more favorable medium than PO4 for fatty acid formation, while PO4 was the more favorable medium for cholesterogenesis, though the differences between adrenalectomized and intact animals persisted in either buffer. Forced feeding with glucose increased the incorporation of acetate into fat and cholesterol in both buffer systems in adrenalectomized as well as in intact animals. However, the adrenalectomized preparation still incorporated acetate to a lesser extent than the controls. It was concluded that while the depressed incorporation of acetate into fatty acid and cholesterol by adrenalectomized liver slices was consistent with a depressed synthesis of these lipids, there was also the possibility that it reflected an increased turnover of lipids in the liver of the adrenalectomized animal.

FATTY ACID INHIBITION OF CHOLESTEROL SYNTHESIS

1956 ◽  
Vol 34 (1) ◽  
pp. 861-868 ◽  
Author(s):  
J. D. Wood ◽  
B. B. Migicovsky
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Chain Length ◽  
Rat Liver ◽  
Cholesterol Synthesis ◽  
Rapid Decrease ◽  
Acid Inhibition ◽  
Degree Of Unsaturation ◽  
Liver Homogenates ◽  
Fatty Acid Inhibition

Fatty acids inhibit cholesterol synthesis by rat liver homogenates. Inhibition occurs with acids containing either an even or an odd number of carbon atoms in the chain, and with saturated and unsaturated acids, the inhibition increasing with the degree of unsaturation of the acid. In the case of acids with an even number of carbon atoms the inhibition increases with chain length to a maximum at 12 carbons after which a rapid decrease occurs. The presence of fatty acid during cholesterol synthesis increases the acetate incorporated into fatty acids to a slight extent. This increase is small compared with the decrease in the amount incorporated into cholesterol. A possible mechanism for the inhibition is discussed.

FATTY ACID INHIBITION OF CHOLESTEROL SYNTHESIS

1956 ◽  
Vol 34 (5) ◽  
pp. 861-868 ◽  
Author(s):  
J. D. Wood ◽  
B. B. Migicovsky
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Chain Length ◽  
Rat Liver ◽  
Cholesterol Synthesis ◽  
Rapid Decrease ◽  
Acid Inhibition ◽  
Degree Of Unsaturation ◽  
Liver Homogenates ◽  
Fatty Acid Inhibition

Fatty acids inhibit cholesterol synthesis by rat liver homogenates. Inhibition occurs with acids containing either an even or an odd number of carbon atoms in the chain, and with saturated and unsaturated acids, the inhibition increasing with the degree of unsaturation of the acid. In the case of acids with an even number of carbon atoms the inhibition increases with chain length to a maximum at 12 carbons after which a rapid decrease occurs. The presence of fatty acid during cholesterol synthesis increases the acetate incorporated into fatty acids to a slight extent. This increase is small compared with the decrease in the amount incorporated into cholesterol. A possible mechanism for the inhibition is discussed.

Isoforms of Rat Liver Fatty Acid Binding Protein Differ in Structure and Affinity for Fatty Acids and Fatty Acyl CoAs†

Biochemistry ◽  
1997 ◽  
Vol 36 (21) ◽  
pp. 6545-6555 ◽  
Author(s):  
Andrey Frolov ◽  
Tae-Hyeon Cho ◽  
Eric J. Murphy ◽  
Friedhelm Schroeder
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acyl ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Studies on fatty acid-binding proteins. The binding properties of rat liver fatty acid-binding protein

1987 ◽  
Vol 247 (2) ◽  
pp. 485-488 ◽  
Author(s):  
T C Wilkinson ◽  
D C Wilton
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Unsaturated Fatty Acids ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Wide Range

1. The fluorescent fatty acid probe 11-(dansylamino)undecanoic acid binds to rat liver fatty acid-binding protein with a 1:1 stoichiometry. 2. The binding of the fluorescent probe is competitive with long-chain fatty acids. 3. Binding displacement studies were performed with a wide range of fatty acids and other ligands and identified C16 and C18 fatty acids as the preferred fatty acids for rat liver fatty acid-binding protein. No preference was observed for unsaturated fatty acids within this group. 4. Fatty acyl-CoA binds less well than the corresponding fatty acid.

scholarly journals Intracellular sterol distribution in transfected mouse L-cell fibroblasts expressing rat liver fatty acid-binding protein.

1991 ◽  
Vol 266 (9) ◽  
pp. 5486-5496
Author(s):  
J R Jefferson ◽  
J P Slotte ◽  
G Nemecz ◽  
A Pastuszyn ◽  
T J Scallen ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
L Cell
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