scholarly journals Distribution of the integral plasma membrane glycoprotein CE9 (MRC OX-47) among rat tissues and its induction by diverse stimuli of metabolic activation

1995 ◽  
Vol 310 (2) ◽  
pp. 693-698 ◽  
Author(s):  
C L Nehme ◽  
B E Fayos ◽  
J R Bartles
Keyword(s):  
Adipose Tissue ◽  
Plasma Membrane ◽  
Brown Adipose Tissue ◽  
Plasma Membranes ◽  
Metabolic Activation ◽  
Blast Transformation ◽  
Rat Tissues ◽  
Membrane Glycoprotein ◽  
Brown Adipose ◽  
Different Tissues

We have compared the levels of the integral plasma membrane glycoprotein CE9 (MRC OX-47) in different tissues of the rat and have ascertained that the levels of CE9 protein and mRNA in selected tissues and cells exhibit moderate increases in response to diverse stimuli of metabolic activation. When normalized on the basis of total protein, the level of CE9 detected in the different tissues was found to vary over a 50-fold range. In addition, the apparent molecular mass of CE9 was observed to vary from 40 kDa to 68 kDa as a consequence of tissue-specific glycosylation. The highest level of CE9 was detected in brown adipose tissue, where the protein was found to be localized to the plasma membranes of the adipocytes. The metabolic activation of brown adipose tissue that occurs upon exposure of rats to the cold was found to be accompanied by 3.0 +/- 0.4-fold and 1.7 +/- 0.2-fold increases in the levels of CE9 mRNA and protein respectively. An intermediate level of CE9 was detected in the liver, where the protein is known to be expressed within the basolateral domain of the hepatocyte plasma membrane. The metabolic activation of hepatocytes that occurs upon administration of thyroid hormone to euthyroid rats was found to be accompanied by 2.2 +/- 0.3-fold and 1.9 +/- 0.3-fold increases in the levels of CE9 mRNA and protein respectively. A low level of CE9 was detected in the lymphoid organs, such as thymus and spleen. The metabolic activation of isolated rat splenocytes that occurs upon concanavalin A-mediated blast transformation in culture was found to be accompanied by 2.1 +/- 0.2-fold and 1.6 +/- 0.2-fold increases in the levels of CE9 mRNA and protein respectively. On the basis of these and other observations, we suggest that the level, and possibly also the localization, of the integral plasma membrane glycoprotein CE9 may be correlated in a positive fashion with metabolic activity in a diverse array of cell types.

scholarly journals The decrease in the short variant of gsalpha protein is associated with an increase in [3H]CGP12177 binding, [3H]ouabain binding and Na, K-ATPase activity in brown adipose tissue plasma membranes of cold-acclimated hamsters

1999 ◽  
Vol 22 (1) ◽  
pp. 55-64 ◽  
Author(s):  
L Bourova ◽  
J Novotn ◽  
P Svoboda
Keyword(s):  
Adipose Tissue ◽  
Plasma Membrane ◽  
Atpase Activity ◽  
Brown Adipose Tissue ◽  
Binding Sites ◽  
Plasma Membranes ◽  
Immunoblot Analysis ◽  
Ouabain Binding ◽  
Brown Adipose ◽  
Sds Page

Sucrose density gradient purified plasma membranes isolated from brown adipose tissue of cold-acclimated hamsters (4-10 weeks at 0-4 degreesC) were analysed for the content of the short (GsalphaS) and long (GsalphaL) variants of Gsalpha protein (the alpha subunit of the stimulatory G protein) and compared with the membranes isolated from control animals. The relative ratio between the two variants (GsalphaS/GsalphaL) decreased from 0.48 to 0.24 (P<0.01). This result, obtained by electrophoretic resolution of membrane proteins by standard SDS-PAGE and an immunoblot analysis with an antiserum oriented against an internal sequence of Gsalpha, was verified by resolution on urea-containing gels and an antiserum oriented against the C-terminus decapeptide of Gsalpha. Under these conditions, the GsalphaS/GsalphaL ratio was decreased from 0.41 to 0.31 (P<0.05). The total amount of both isoforms (GsalphaS plus GsalphaL) decreased to 83% (P<0.05) or 68% (P<0.01) by standard or urea SDS-PAGE respectively. These data demonstrate that cold-acclimation of hamster brown adipose tissue is associated with preferential decrease in the plasma membrane density of the short variant of the Gsalpha protein.%This decrease was paralleled by an increase in the other plasma membrane constituents, [3H]CGP12177 binding sites, [3H]ouabain binding sites and Na,K-ATPase activity to 147%, 212% and 191% respectively.

scholarly journals Resolution and identification of Gq/G11alpha and Gialpha/Goalpha proteins in brown adipose tissue: effect of cold acclimation

1999 ◽  
Vol 23 (2) ◽  
pp. 223-229 ◽  
Author(s):  
L Bourova ◽  
J Novotny ◽  
P Svoboda
Keyword(s):  
Adipose Tissue ◽  
Plasma Membrane ◽  
Brown Adipose Tissue ◽  
Cold Acclimation ◽  
Plasma Membranes ◽  
Brown Adipose ◽  
Guanine Nucleotide Binding ◽  
G 11 ◽  
Carboxy Terminal ◽  
Nucleotide Binding Proteins

Levels of guanine nucleotide-binding proteins G(q)alpha and G(11)alpha, which produce receptor regulation of phospholipase C, were measured immunologically in purified plasma membrane fractions of hamster brown adipose tissue (BAT). This was achieved by immunoblotting with antisera (CQ series) that identify these two polypeptides equally, following separation of the plasma membranes using SDS-PAGE in the presence of 6 M urea, i.e. conditions that can resolve G(q)alpha and G(11)alpha. The ratio of levels of G(q)alpha to G(11)alpha was 1:1. A similar approach was used for resolution and identification of G(o)1alpha and G(o)2alpha, the latter representing the prevailing form of G(o)alpha proteins in this tissue. Although clearly recognized in brain microsomes, which were used as positive controls, no detected levels of G(o)*alpha protein were noted. Using specific anti-peptide antibodies directed against the carboxy-terminal decapeptide of G(i)3alpha, this G protein was also found to be expressed in BAT tissue. Cold acclimation resulted in reduction of the plasma membrane levels of all these Galpha proteins.

scholarly journals Effects of stem cells from inducible brown adipose tissue on diet-induced obesity in mice

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Enrique Calvo ◽  
Noelia Keiran ◽  
Catalina Núñez-Roa ◽  
Elsa Maymó-Masip ◽  
Miriam Ejarque ◽  
...  
Keyword(s):  
Stem Cells ◽  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Therapeutic Option ◽  
Metabolic Activation ◽  
Diet Induced Obesity ◽  
Brown Adipose ◽  
Obesity In Mice ◽  
Treatment Of Obesity ◽  
Visceral Adipose

AbstractAdipose-derived mesenchymal stem cells (ASCs) are a promising option for the treatment of obesity and its metabolic co-morbidities. Despite the recent identification of brown adipose tissue (BAT) as a potential target in the management of obesity, the use of ASCs isolated from BAT as a therapy for patients with obesity has not yet been explored. Metabolic activation of BAT has been shown to have not only thermogenic effects, but it also triggers the secretion of factors that confer protection against obesity. Herein, we isolated and characterized ASCs from the visceral adipose tissue surrounding a pheochromocytoma (IB-hASCs), a model of inducible BAT in humans. We then compared the anti-obesity properties of IB-hASCs and human ASCs isolated from visceral white adipose tissue (W-hASCs) in a murine model of diet-induced obesity. We found that both ASC therapies mitigated the metabolic abnormalities of obesity to a similar extent, including reducing weight gain and improving glucose tolerance. However, infusion of IB-hASCs was superior to W-hASCs in suppressing lipogenic and inflammatory markers, as well as preserving insulin secretion. Our findings provide evidence for the metabolic benefits of visceral ASC infusion and support further studies on IB-hASCs as a therapeutic option for obesity-related comorbidities.

scholarly journals Immunochemical studies with soluble and mitochondrial pyruvate carboxylase activities from rat tissues

1970 ◽  
Vol 119 (4) ◽  
pp. 735-742 ◽  
Author(s):  
F. J. Ballard ◽  
R. W. Hanson ◽  
Lea Reshef
Keyword(s):  
Adipose Tissue ◽  
Mammary Gland ◽  
Brown Adipose Tissue ◽  
Rat Liver ◽  
White Adipose Tissue ◽  
Pyruvate Carboxylase ◽  
Specific Activity ◽  
Rat Liver Mitochondria ◽  
Rat Tissues ◽  
Brown Adipose

1. Pyruvate carboxylase (EC 6.4.1.1), purified from rat liver mitochondria to a specific activity of 14 units/mg, was used for the preparation of antibodies in rabbits. 2. Tissue distribution studies showed that pyruvate carboxylase was present in all rat tissues that were tested, with considerable activities both in gluconeogenic tissues such as liver and kidney and in tissues with high rates of lipogenesis such as white adipose tissue, brown adipose tissue, adrenal gland and lactating mammary gland. 3. Immunochemical titration experiments with the specific antibodies showed no differences between the inactivation of pyruvate carboxylase from mitochondrial or soluble fractions of liver, kidney, mammary gland, brown adipose tissue or white adipose tissue. 4. The antibodies were relatively less effective in reactions against pyruvate carboxylase from sheep liver than against the enzyme from rat tissues. 5. Pyruvate carboxylase antibodies did not inactivate either propionyl-CoA carboxylase or acetyl-CoA carboxylase from rat liver. 6. It is concluded that pyruvate carboxylase in lipogenic tissues is similar antigenically to the enzyme in gluconeogenic tissues and that the soluble activities of pyruvate carboxylase detected in many rat tissues do not represent discrete enzymes but are the result of mitochondrial damage during tissue homogenization.

Control mechanisms in brown adipose tissue plasma membrane

1984 ◽  
Vol 62 (7) ◽  
pp. 631-636 ◽  
Author(s):  
N. Bégin-Heick ◽  
H. M. C. Heick
Keyword(s):  
Adipose Tissue ◽  
Plasma Membrane ◽  
Adenylate Cyclase ◽  
Brown Adipose Tissue ◽  
Heat Production ◽  
Metabolic Effects ◽  
Maximal Response ◽  
Obese Mouse ◽  
Control Mechanisms ◽  
Brown Adipose

It is generally agreed that the site of heat production during nonshivering thermogenesis is the brown adipose tissue (BAT) and that the triggering event for heat production is the interaction of noradrenaline (NA) with its receptor on the plasma membrane. Following this initial event, several changes occur which result in increased rates of cAMP synthesis, redistribution of ions across the membrane, enhanced rates of lipolysis, and increased mitochondrial oxidation of substrates. BAT is also a target for the anabolic effect of insulin. Available evidence shows that insulin receptors are present on the BAT plasma membrane and that insulin can oppose the metabolic effects of catecholamine on BAT. We have studied more particularly the response of BAT adenylate cyclase to catecholamines in an animal model (the ob/ob mouse) which has a defective thermogenic response. The capacity of adenylate cyclase to be stimulated by catecholamines was significantly less in the tissue of obese mice than in lean controls. To produce a response equal to the half-maximal response in the lean mouse, a 10-fold increase in the NA concentration was required in the BAT of the obese mouse. These results are in harmony with those of others showing that the lipolytic response to catecholamines is abnormal in the BAT of the obese mouse. The adenylate cyclase activity can be altered by changes in the lipid composition of the diet and by manipulation of hormone levels. It is likely that the alteration in adenylate cyclase responsiveness is one of the contributing factors in the impaired thermogenesis and obesity in this animal.

Conversion of thyroxine to 3,5,3'-triiodothyronine in several rat tissues in vivo: the effect of hypothyroidism

1986 ◽  
Vol 113 (1) ◽  
pp. 59-64 ◽  
Author(s):  
Jaap van Doom ◽  
Ferdinand Roelfsema ◽  
Daan van der Heide
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Rat Tissues ◽  
Isotopic Equilibrium ◽  
Brown Adipose ◽  
Tissue Homogenates ◽  
The Mean ◽  
Layer Chromatography ◽  
Infusion Period

Abstract. The local conversion of thyroxine (T4) to 3,5,3'-triiodothyronine (T3) has been recognized as a source of T3 at various sites in euthyroid rats. The present study was designed to evaluate the effect of hypothyroidism on the source and quantity of T3 at several of these sites (liver, cerebral cortex (Cx), thymus, testis, brown adipose tissue). For this purpose intact euthyroid rats and radiothyroidectomized (RTx) rats received a continuous iv infusion of [125I]T4 and [131I]T3 until isotopic equilibrium was attained. In addition to the labelled iodothyronines, RTx rats received a continuous iv infusion of 0.75 μg T4/day, in order to maintain a defined hypothyroid state. At the end of the infusion period the animals were bled and perfused, and homogenates of the various organs were prepared. The mean plasma T4 and T3 levels in T4-maintained RTx rats, as measured by RIA, were 1.5 μg/dl and 15 ng/dl (euthyroid values: 5.2 μg/dl and 48 μg/dl, respectively). The plasma and tissue homogenates were processed for thin layer chromatography and the [125I]T4, [125I]T3 and [131I]T3 levels determined. From these data the concentrations of T4, total T3 and T3 derived from local T4 to T3 conversion (LcT3(T4)) in tissue could be calculated. The relative mean contribution of LcT3(T4) to the total T3 in Cx (75%), thymus (31%), testis (43%) and brown adipose tissue (65%) from hypothyroid rats was higher than that determined for euthyroid animals (66%, 19%, 29% and 27%, respectively). The reverse was found for the liver (15% vs 39%). As a consequence, hypothyroidism led to a substantial loss of intracellular T3 in the liver (about 80%), whereas in all other tissues investigated the decrease in total T3 was less. In spite of the low intracellular T4 levels in hypothyroid rats, the quantity of LcT3(T4) in brown adipose tissue had increased significantly. This was not the case in the other tissues investigated. However, as found for brown adipose tissue, the ratio between LcT3(T4) and T4 found for Cx, thymus and (although not statistically significant) testis was higher in hypothyroid rats than in euthyroid animals, again suggesting a higher degree of in vivo T4 to T3 conversion in the hypothyroid state. These results strongly suggest that local factors play an important role in the regulation of intracellular T3 levels.

Altered effect of insulin and catecholamines in brown adipose tissue of cold-acclimated rats

1979 ◽  
Vol 57 (3) ◽  
pp. 320-324 ◽  
Author(s):  
Nicole Bégin-Heick ◽  
Iris Noland ◽  
Marthe Dalpé ◽  
H. M. C. Heick
Keyword(s):  
Adipose Tissue ◽  
Plasma Membrane ◽  
Adenylate Cyclase ◽  
Brown Adipose Tissue ◽  
Cold Acclimation ◽  
Inhibitory Action ◽  
Cyclase Activity ◽  
Relative Response ◽  
Brown Adipose ◽  
Glucose Incorporation

Data are presented indicating that in brown adipose tissue (BAT) of cold-acclimated (CA), but not cold-exposed (CE) rats, there was an alteration in the relative response to catecholamines and insulin as evidenced by increased binding of alprenolol and decreased binding of insulin to plasma membrane enriched fractions. In addition, the stimulatory effect of insulin on glucose incorporation into glycogen and its inhibitory action on adenylate cyclase activity were both blunted in the CA tissues. It is proposed that shifts in the capacity of BAT to respond to catecholamines and insulin may be involved in the mechanism of cold acclimation.

scholarly journals Modulation in vivo of β-adrenergic-receptor subtypes in rat brown adipose tissue by the thermogenic agonist Ro 16–8714

1992 ◽  
Vol 286 (3) ◽  
pp. 743-746 ◽  
Author(s):  
J P Revelli ◽  
P Muzzin ◽  
J P Giacobino
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Plasma Membranes ◽  
State Level ◽  
Zucker Rats ◽  
Receptor Subtypes ◽  
Interscapular Brown Adipose Tissue ◽  
Brown Adipose ◽  
Beta Adrenergic Agonist

The number of beta 3-adrenergic receptors (AR) in plasma membranes from interscapular brown adipose tissue (IBAT) was decreased by 62% in lean Zucker rats treated with the thermogenic beta-adrenergic agonist Ro 16-8714 as compared with controls after 72 h of treatment. The loss of beta 3-AR number was preceded by a 93% decrease in the steady-state level of beta 3-AR mRNA at 30 h. Similar results were obtained in obese (fa/fa) Zucker rats. Ro 16-8714 had no effect on the number of beta 1- and beta 2-ARs in IBAT. This is the first report to demonstrate that the beta 3-AR in IBAT can be specifically down-regulated in vivo by exposure to a thermogenic agonist.

scholarly journals Persistence of the effect of insulin on pyruvate dehydrogenase activity in rat white and brown adipose tissue during the preparation and subsequent incubation of mitochondria

1984 ◽  
Vol 217 (2) ◽  
pp. 441-452 ◽  
Author(s):  
R M Denton ◽  
J G McCormack ◽  
S E Marshall
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Dehydrogenase Activity ◽  
Pyruvate Dehydrogenase ◽  
Plasma Membranes ◽  
Pyruvate Dehydrogenase Kinase ◽  
Epididymal Adipose Tissue ◽  
Short Term ◽  
Interscapular Brown Adipose Tissue ◽  
Brown Adipose

Increases in the amount of the active non-phosphorylated form of pyruvate dehydrogenase in rat epididymal adipose tissue, as a result of incubation with insulin, persist not only during the preparation of mitochondria but also during subsequent incubation of coupled mitochondria in the presence of respiratory substrates. No effect on insulin was found if the hormone was added directly to mitochondria in the presence or absence of added plasma membranes. Concentrations of several possible regulators of pyruvate dehydrogenase kinase (ATP, ADP, NADH, NAD+, acetyl-CoA, CoA and potassium) were measured in rat epididymal-adipose-tissue mitochondria incubated under conditions where differences in pyruvate dehydrogenase activity persist as a result of insulin action. No alterations were found, and it is suggested that inhibition of the kinase is not the principal means by which insulin activates pyruvate dehydrogenase. The intramitochondrial concentration of magnesium was also unaffected. Differences in pyruvate dehydrogenase activity in interscapular brown adipose tissue associated with manipulation of plasma insulin concentrations of cold-adapted rats were also shown to persist during the preparation and subsequent incubation of mitochondria in the presence or absence of GDP. It is pointed out that the persistence of the effect of insulin on pyruvate dehydrogenase in incubated mitochondria will facilitate the recognition of the mechanism of this action of the hormone. Evidence that the short-term action of insulin involves an increase in pyruvate dehydrogenase phosphate phosphatase activity rather than inhibition of that of pyruvate dehydrogenase kinase is discussed.

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