Protein kinases in brown adipose tissue of developing rats: substrate specificities, separation, and changes in activity during development

1978 ◽  
Vol 56 (9) ◽  
pp. 869-874 ◽  
Author(s):  
Josef P. Skala ◽  
Brian L. Knight
Keyword(s):  
Adipose Tissue ◽  
Protein Kinase ◽  
Brown Adipose Tissue ◽  
Kinase Activity ◽  
Specific Activity ◽  
Brown Fat ◽  
Supernatant Fraction ◽  
Protein Kinase Activity ◽  
Nonhistone Proteins ◽  
Brown Adipose

Protein kinase activity in the 100 000 × g supernatant fraction of brown adipose tissue was assayed with various proteins as substrates. Greatest activity was obtained with histone subfraction f2b and the lowest activity with protamine. cAMP stimulated the phosphorylation of histones but not that of the other proteins. The specific activity of protein kinase in brown fat of rats changed during infancy, and the pattern of changes was different with different protein substrates.Electrophoresis of the tissue-soluble extract gave nine major bands of protein kinase activity. These were assayed on the gels under the optimal conditions for each substrate. Five of the bands were histone kinases and gave little activity with nonhistone proteins. Two bands gave their greatest activity with phosvitin or casein. Protamine and arginine-rich histone were particularly good substrates for the two remaining bands. The activity in each band exhibited a different and distinct pattern of ontogenic development, which was not affected by the nature of the protein used for the assay. There was a reasonable similarity between the overall developmental profile for the rate of phosphorylation of each substrate calculated from the sum of activities determined on the individual bands and the profile directly determined in the whole soluble fraction.Both the direct assay and the electrophoretic results indicate that brown fat contains a number of protein kinase activities that can be distinguished by their specificities for protein substrate and by the pattern of changes in their activities during development. There were three main patterns of ontogenic changes in activity: one decreased progressively from high values in late foetuses; the second showed a marked fall in activity during the 3rd week after birth; and in the third, the activity rose after birth and then remained constant. The greatest changes in kinase activity thus occur during the periods when there are pronounced changes in the rates of proliferation and differentiation in brown fat, in its capacity to produce heat, and in the diet of the animal. It seems possible that the different types of protein kinase carry out phosphorylations involved in the regulation of different processes in brown fat.

scholarly journals A protein kinase inhibitor in brown adipose tissue of developing rats

1974 ◽  
Vol 138 (2) ◽  
pp. 195-199 ◽  
Author(s):  
Josef P. Skala ◽  
George I. Drummond ◽  
Peter Hahn
Keyword(s):  
Adipose Tissue ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Brown Adipose Tissue ◽  
Inhibitory Activity ◽  
Kinase Inhibitor ◽  
Protein Kinase Inhibitor ◽  
Supernatant Fraction ◽  
Brown Adipose ◽  
Tissue Homogenates

A heat-stable protein was extracted from brown adipose tissue of infant rats that inhibited both purified bovine heart protein kinase and a crude preparation of protein kinase from brown fat. It did not act as an adenosine triphosphatase nor did it exert its effect by proteolytic action. Inhibition of protein kinase was affected in both the presence and the absence of cyclic AMP. Most of the inhibitory activity was present in the 100000g supernatant fraction of tissue homogenates. Inhibitory activity was highest perinatally and it declined 10 days after birth. It is suggested that the protein kinase inhibitor may play a role in regulating cyclic AMP actions.

142-OR: Unique Role of the a4 Component for S6-Kinase Activity in Metabolic Regulation and Anti-apoptotic Effect in Brown Adipose Tissue

Diabetes ◽  
2019 ◽  
Vol 68 (Supplement 1) ◽  
pp. 142-OR
Author(s):  
MASAJI SAKAGUCHI ◽  
SHOTA OKAGAWA ◽  
SAYAKA KITANO ◽  
TATSUYA KONDO ◽  
EIICHI ARAKI
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Metabolic Regulation ◽  
Kinase Activity ◽  
S6 Kinase ◽  
Unique Role ◽  
Brown Adipose ◽  
Apoptotic Effect

scholarly journals The Saccharomyces cerevisiae YAK1 gene encodes a protein kinase that is induced by arrest early in the cell cycle.

1991 ◽  
Vol 11 (8) ◽  
pp. 4045-4052 ◽  
Author(s):  
S Garrett ◽  
M M Menold ◽  
J R Broach
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Kinase Activity ◽  
Specific Activity ◽  
S Phase ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Protein Levels ◽  
Cycle Arrest ◽  
Dependent Protein

Null mutations in the gene YAK1, which encodes a protein with sequence homology to known protein kinases, suppress the cell cycle arrest phenotype of mutants lacking the cyclic AMP-dependent protein kinase (A kinase). That is, loss of the YAK1 protein specifically compensates for loss of the A kinase. Here, we show that the protein encoded by YAK1 has protein kinase activity. Yak1 kinase activity is low during exponential growth but is induced at least 50-fold by arrest of cells prior to the completion of S phase. Induction is not observed by arrest at stages later in the cell cycle. Depending on the arrest regimen, induction can occur either by an increase in Yak1 protein levels or by an increase in Yak1 specific activity. Finally, an increase in Yak1 protein levels causes growth arrest of cells with attenuated A kinase activity. These results suggest that Yak1 acts in a pathway parallel to that of the A kinase to negatively regulate cell proliferation.

Effect of noradrenaline chronic administration on brown fat phospholipids

1988 ◽  
Vol 8 (5) ◽  
pp. 465-469 ◽  
Author(s):  
Gérard Mory ◽  
Myriam Gawer ◽  
Jean-Claude Kader
Keyword(s):  
Adipose Tissue ◽  
Fatty Acid Composition ◽  
Fatty Acid ◽  
Brown Adipose Tissue ◽  
Acid Composition ◽  
Cold Exposure ◽  
Chronic Administration ◽  
Sympathetic Tone ◽  
Brown Fat ◽  
Brown Adipose

Chronic cold exposure of rats (9 days at 5°C) induces an alteration of the fatty acid composition of phospholipids in brown adipose tissue. The alteration is due to an increase of the unsaturation degree of these lipids. The phenomenon can be reproduced by 10−7 mole. h−1 administration of noradrenaline for 9 days in rats kept at 25°C. Thus, phospholipid alteration in brown fat of cold exposed rats is most probably a consequence of the increase of sympathetic tone which occurs in this tissue during exposure to cold.

The development of insulin resistance in brown adipose tissue may impair the acute cold-induced activation of thermogenesis in genetically obese (ob/ob) mice

1984 ◽  
Vol 4 (11) ◽  
pp. 933-940 ◽  
Author(s):  
Stewart W. Mercer ◽  
Paul Trayhurn
Keyword(s):  
Insulin Resistance ◽  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Cold Exposure ◽  
Brown Fat ◽  
Acute Cold Exposure ◽  
Brown Adipose

Genetically obese (ob/ob) mice develop insulin resistance in brown adipose tissue during the fifth week of life. Prior to this, at 26 days of age, oh/oh mice show a substantial increase in GDP binding to brownadipose-tissue mitochondria during acute cold exposure. When insulin resistance in brown fat develops, by 35 days of age, the increase in GDP binding in response to cold is markedly reduced. Studies with 2-deoxyglucose suggest that insulin resistance in brown adipose tissue could impair thermogenic responsiveness during acute cold exposure by limiting the ability of the tissue to take up glucose.

OBSERVATIONS ON PEROXISOMES IN BROWN ADIPOSE TISSUE OF THE RAT

1971 ◽  
Vol 19 (11) ◽  
pp. 670-675 ◽  
Author(s):  
IRÉNE AHLABO ◽  
TUDOR BARNARD
Keyword(s):  
Hydrogen Peroxide ◽  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Single Unit ◽  
Brown Fat ◽  
Unit Membrane ◽  
Peroxisomal Enzyme ◽  
Brown Adipose ◽  
Homogeneous Matrix ◽  
Physiologic Activity

During cytochemical studies of brown adipose tissue from rat, cytoplasmic organelles that apparently show peroxidative activity have been observed. The majority of the organelles have a diameter of 0.1-0.8 µ and a finely granular homogeneous matrix and are delimited by a single unit membrane. No sign of a "crystalloid" was seen. In order to demonstrate the peroxidative activity of the peroxisomal enzyme catalase in the organelles, brown adipose tissue was incubated in a medium containing 3,3'-diaminobenzidine tetrahydrochloride, after prefixation in 3% glutaraldehyde. The activity was blocked by 3-amino-l,2,4-triazole (an inhibitor of catalase) but not by KCN. Omission of exogenous hydrogen peroxide did not inhibit the reaction in the organelles. It is concluded that rat brown adipose tissue contains peroxisomes and, since the abundance of these organelles varies according to the physiologic activity of the tissue, peroxisomes may have a role in the thermogenic metabolism of brown fat.

Diet, lighting, and food intake affect norepinephrine turnover in dietary obesity

1987 ◽  
Vol 252 (2) ◽  
pp. R402-R408 ◽  
Author(s):  
T. Yoshida ◽  
J. S. Fisler ◽  
M. Fukushima ◽  
G. A. Bray ◽  
R. A. Schemmel
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
High Fat Diet ◽  
Brown Fat ◽  
Light Cycle ◽  
High Fat ◽  
Interscapular Brown Adipose Tissue ◽  
Norepinephrine Turnover ◽  
Brown Adipose ◽  
Dietary Obesity

The effects of dietary fat content, lighting cycle, and feeding time on norepinephrine turnover in interscapular brown adipose tissue, heart, and pancreas, and on blood 3-hydroxybutyrate, serum glucose, insulin, and corticosterone have been studied in two strains of rats that differ in their susceptibility to dietary obesity. S 5B/Pl rats, which are resistant to dietary obesity, have a more rapid turnover of norepinephrine in interscapular brown adipose tissue and heart and a greater increase in the concentration of norepinephrine in brown fat when eating a high-fat diet than do Osborne-Mendel rats, which are sensitive to fat-induced obesity. Light cycle and feeding schedule are important modulators of sympathetic activity in heart and pancreas but not in brown fat. Rats of the resistant strain also have higher blood 3-hydroxybutyrate concentrations and lower insulin and corticosterone levels than do rats of the susceptible strain. A high-fat diet increases 3-hydroxybutyrate concentrations and reduces insulin levels in both strains. These studies show, in rats eating a high-fat diet, that differences in norepinephrine turnover, particularly in brown adipose tissue, may play an important role in whether dietary obesity develops and in the manifestations of resistance to this phenomenon observed in the S 5B/Pl rat.

Brown adipose tissue in cafeteria-fed hamsters

1985 ◽  
Vol 248 (2) ◽  
pp. E230-E235
Author(s):  
R. J. Schimmel ◽  
L. McCarthy
Keyword(s):  
Adipose Tissue ◽  
Weight Gain ◽  
Brown Adipose Tissue ◽  
Brown Fat ◽  
Cafeteria Diet ◽  
Tissue Protein ◽  
Dietary Regulation ◽  
Isolated Mitochondria ◽  
Brown Adipose ◽  
Thermogenic Capacity

Hamsters consuming a “cafeteria diet” had more brown adipose tissue than did chow-fed hamsters. The growth of the brown fat depots in cafeteria-fed hamsters was accompanied by increases in tissue protein and cytochrome oxidase. To assess the thermogenic capacity of brown fat mitochondria, the binding of GDP to isolated mitochondria was measured. Mitochondrial GDP binding was not affected by feeding the cafeteria diet for 4 wk, but more prolonged cafeteria feeding for 8 wk did, however, increase the binding of GDP to isolated mitochondria. The morphology of brown adipose tissue was altered during cafeteria feeding. The brown adipose tissue of cafeteria-fed hamsters had more large unilocular cells than did the brown adipose tissue of chow-fed hamsters. In addition, the average adipocyte diameter was greater in brown adipose tissue of cafeteria-fed hamsters. These data support the presence of a dietary regulation of brown adipose tissue growth in hamsters. The growth of brown adipose tissue in hamsters eating the cafeteria diet appears to result largely from proliferation of adipocytes, as evidenced by the increases in tissue protein and cytochrome oxidase during cafeteria feeding, but some hypertrophy of the adipocytes also occurs. A dietary regulation of brown fat thermogenic capacity is also apparent but this regulation is evident only after more prolonged periods of cafeteria feeding. Hamsters eating a cafeteria diet increase their caloric intake but have the same or greater body weight gain efficiency as do chow-fed animals. The absence of dietary stimulation of thermogenesis may underlie the similar efficiencies of weight gain in chow- and cafeteria-fed hamsters.

Abnormal brown adipose tissue in hamsters with muscular dystrophy

1980 ◽  
Vol 239 (1) ◽  
pp. C18-C22 ◽  
Author(s):  
J. Himms-Hagen ◽  
C. Gwilliam
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Cytochrome Oxidase ◽  
Specific Activity ◽  
Purine Nucleotides ◽  
Interscapular Brown Adipose Tissue ◽  
Cardiomyopathic Hamster ◽  
Brown Adipose ◽  
Cardiomyopathic Hamsters ◽  
Wet Weight

The size (wet weight, total protein, total cytochrome oxidase) of interscapular brown adipose tissue is reduced to about one-half of normal in the cardiomyopathic hamster (BIO 14.6). The mitochondria are normal in binding of purine nucleotides [guanosine 5'-diphosphate (GDP)] and in proportion of polypeptides in the region of 32,000, both indices of the thermogenic proton conductance pathway, and in specific activity of cytochrome oxidase. Brown adipose tissue of the cardiomyopathic hamster can grow during acclimation to 4 degrees C, but its size remains smaller than in cold-acclimated normal hamsters. Mitochondrial polypeptide composition is not altered by acclimation to cold, but a large increase in mitochondrial GDP binding occurs in both normal and cardiomyopathic hamsters. The reduced calorigenic response of cardiomyopathic hamsters to catecholamines (Horwitz, B.A., and G.E. Hanes, Proc. Soc. Exp. Biol. Med. 147: 393-395, 1974) may, at least in part, be explained by a reduction in the amount of brown adipose tissue, the major site of this response. A defect in control of growth of this tissue in the cardiomyopathic hamster is suggested.

scholarly journals Changes in protein kinase activity in rat testes during development

1977 ◽  
Vol 162 (2) ◽  
pp. 465-467 ◽  
Author(s):  
E A Bernard ◽  
G F Wassermann
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Specific Activity ◽  
Protein Kinase Activity ◽  
Embryonic Life ◽  
Old Rats

Protein kinase activity in rat testes remained fairly constant from day 16 1/2 of embryonic life up to 10 days after birth. At the 21st postnatal day a nadir of activity was observed, and after an increase at 35 days of age a decrease in activity at 60 days was seen. The enzyme reached maximal specific activity in the testes of 90-day-old rats.

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