Intracranial administration of transforming growth factor-β3 increases fat oxidation in rats

Yamazaki, Hiroyuki; Arai, Mikiro; Matsumura, Shigenobu; Inoue, Kazuo; Fushiki, Tohru

doi:10.1152/ajpendo.00094.2001

Cited by 26 publications

(36 citation statements)

References 35 publications

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“…Although the three TGF␤s share 60 -80% identity, they are encoded by distinct genes, and their expression is controlled by a different regulatory sequence or promoter (4 -6). They also show different physiological and pathological activities in certain cell types and systems (7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17). Because the expression of TGF␤ is controlled by an auto-feedback loop (18), TGF␤ is an important mechanism for amplifying its own expression and production.…”

Section: Tgf␤mentioning

confidence: 99%

Requirement of Smad3 and CREB-1 in Mediating Transforming Growth Factor-β (TGFβ) Induction of TGFβ3 Secretion

Liu

Ding

Neiman

et al. 2006

Journal of Biological Chemistry

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Because increased transforming growth factor-␤ (TGF␤) production by tumor cells contributes to cancer progression through paracrine mechanisms, identification of critical points that can be targeted to block TGF␤ production is important. Previous studies have identified the precise signaling components and promoter elements required for TGF␤ induction of TGF␤1 expression in epithelial cells (Yue, J., and Mulder, K. M. (2000) J. Biol. Chem. 275, 30765-30773). To determine how regulation of TGF␤3 expression differs from that of TGF␤1, we identified the precise signaling pathways and transcription factor-binding sites that are required for TGF␤3 gene expression. By using mutational analysis in electrophoresis mobility shift assays (EMSAs), we demonstrated that the c-AMP-responsive element (CRE) site in the TGF␤3 promoter was required for TGF␤-inducible TGF␤3 expression. Electrophoresis mobility supershift assays indicated that CRE-binding protein 1 (CREB1) and Smad3 were the major components present in this TGF␤-inducible complex. Furthermore, by using chromatin immunoprecipitation assays, we demonstrated that CREB-1, ATF-2, and c-Jun bound constitutively at the TGF␤3 promoter (؊100 to ؉1), whereas Smad3 bound at this site only after TGF␤ stimulation. In addition, inhibition of JNK and p38 suppressed TGF␤ induction of TGF␤3 transactivation, whereas inhibition of ERK and protein kinase A had no effect. Small interfering RNA-CREB1 and small interfering RNA-Smad3 significantly inhibited TGF␤ stimulation of TGF␤3 promoter reporter activity and TGF␤3 production. Our results indicate that TGF␤ activation of the TGF␤3 promoter CRE site, which leads to TGF␤3 production, is required for TGF␤RII, JNK, p38, and Smad3 but was independent of protein kinase A, ERK, and Smad4.

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Section: Tgf␤mentioning

confidence: 99%

Requirement of Smad3 and CREB-1 in Mediating Transforming Growth Factor-β (TGFβ) Induction of TGFβ3 Secretion

Liu

Ding

Neiman

et al. 2006

Journal of Biological Chemistry

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“…A CSF outflow component was omitted for simplification. The surgical approach for cannula implantation into the cisterna magna has been described previously ( 9 ). Briefly, the rats were anesthetized with isoflurane (2.0-2.5%, by inhalation) and fixed to a stereotaxic apparatus.…”

Section: Surgerymentioning

confidence: 99%

“…The respiratory exchange ratio (RER) was measured by indirect calorimetry as previously described ( 9 ). In brief, a respiratory gas analysis system (ARCO-2000, Arcosystem Inc., Chiba, Japan) consisting of 12 acrylic chambers (21 ϫ 10 ϫ 13 cm), a mass spectrometer for CO 2 and O 2 , and a switching system for collecting samples from and serially changing the airflow in each metabolic chamber was used.…”

Section: Surgerymentioning

confidence: 99%

“…Determination of SMA of rats was done according to the method of Yamazaki et al ( 9 ). Briefly, the SMA of the rats was examined for 2 h after injection of samples with a Supermex (Muromachi Kikai, Tokyo, Japan).…”

Section: Surgerymentioning

confidence: 99%

“…A fraction of active TGF-␤ increased in rat CSF after exhaustion by exercise ( 8 ). Intracisternal administration of TGF-␤ to sedentary animals caused depression of spontaneous motor activity (SMA) in mice ( 8 ) and enhancement of fatty acid oxidation in rats ( 9 ). The former was considered as a fatigue-like behavior and the latter as a regulatory action on whole-body metabolism for endurance during exercise.…”

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confidence: 99%

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Blood Lactate Functions as a Signal for Enhancing Fatty Acid Metabolism during Exercise via TGF-^|^beta; in the Brain

Yamada

Iwaki

Kitaoka

et al. 2012

J Nutr Sci Vitaminol

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Summary Moderate-intensity running (treadmill velocity of 21 m/min) increased blood lactate and actived transforming growth factor-␤ (TGF-␤ ) concentration in rat cerebrospinal fluid (CSF). On the other hand, low-intensity running (15 m/min) did not increase blood lactate and caused no change in CSF TGF-␤ . Intraperitoneal (i.p.) administration of lactate to anesthetized rats caused an increase in blood lactate similar to that observed after a 21 m/min running exercise and increased the level of active TGF-␤ in CSF. Intraperitoneal administration of lactate at the same dose to awake and unrestricted rats caused a decrease in the respiratory exchange ratio, that is, enhancement of fatty acid oxidation and depression of spontaneous motor activity (SMA). Given that intracisternal administration of TGF-␤ to rats has been reported to enhance fatty acid metabolism and to depress SMA, we surmise that the observed changes caused by i.p. lactate administration in this study were mediated, at least in part, by TGF-␤ in the brain. Key Words lactate, TGF-␤ , exercise, respiratory gas analysis, spontaneous motor activity Recently, lactate has been recognized as a good energy source for the central nervous system. Wyss et al.( 1 ) demonstrated that lactate instead of glucose could maintain neuronal activities, and that when both substrates are available, the brain preferentially utilizes lactate. The study, however, implies that lactate is not a direct cause of feelings of fatigue by acting on the brain, and negated the classical view of lactate as a fatigue substance. Blood lactate increases during physical exercise, with skeletal muscles being the major sites of lactate production [see Bergersen ( 2 ) for review]. Increased lactate concentration serves as a signal indicating an increase in the relative ratio of glycolytic energy production, and this signal may function to induce changes in whole-body energy metabolism. Lactate directly acts on neurons and affects their activities. The activities of some neurons in the ventromedial hypothalamus are affected by glucose, whereas some neurons show increased firing rate upon lactate administration ( 3 ). Patil and Briski ( 4 , 5 ) reported the activation of catecholaminergic neurons in the hindbrain by blocking the supply of lactate into the brain with ␣ -cyano-4-hydroxycinnamic acid. These findings indicate that lactate functions as an index for monitoring the energy metabolism status of peripheral organs.We developed a model (Sim-Ex) that simulates physical exercise by inducing skeletal muscle contraction through electrical stimulation in the hindlimbs of anesthetized rats ( 6 ). Sim-Ex with a frequency of 2 Hz could reproduce an exercise load that corresponded to lowintensity exercise. We reported significant increases in the concentrations of blood lactate and active transforming growth factor-␤ (TGF-␤ ) in cerebrospinal fluid (CSF) 5 and 10 min after the onset of Sim-Ex, respectively ( 7 ). A fraction of active TGF-␤ increased in rat CSF after exhaustion by exercise ( 8 ). ...

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Determination of lipoprotein lipase activity in post heparin plasma of streptozotocin‐induced diabetic rats by high‐performance liquid chromatography with fluorescence detection

Chou

Tsai

Chen

et al. 2008

Biomedical Chromatography

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The activity of lipoprotein lipase (LPL), an enzyme responsible for lipoprotein metabolism, would vary in diseases and metabolic disorders. For determination of LPL activity, a highly sensitive high performance liquid chromatography (HPLC) method using a fluorescent reagent, 4-nitro-7-piperazino-2,1,3-benzoxadiazole (NBD-PZ) was applied to determinate the oleic acid (OA) generated from triolein by LPL activity without multiple solvents extraction step. We studied the optimal conditions of the reaction including the effect of emulsifiers, deproteinizing solvents, and the concentration of bovine serum albumin (BSA). Ten millimolar concentrations of triolein, 5% of BSA, 1% of Gum arabic (GA), and acetonitrile showed the optimum conditions for measuring the LPL activity. The accuracy values for the determination of LPL activity in 10 microL of rat post heparin plasma were 108.73 approximately 114.36%, and the intra- and inter-day precision values were within 1.28% and 2.91%, respectively. The limit of detection was about 4.53 nM (signal-to-noise ratio 3). The proposed method was applied to determination of LPL activity in post heparin plasma of normal and streptozotocininduced diabetic rats associated with 52.3% reduction. The established assay system could be used for determining LPL activity in different physiological and pathological conditions to clarify the relationship between LPL activity and diabetes mellitus.

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Intracranial administration of transforming growth factor-β3 increases fat oxidation in rats

Cited by 26 publications

References 35 publications

Requirement of Smad3 and CREB-1 in Mediating Transforming Growth Factor-β (TGFβ) Induction of TGFβ3 Secretion

Requirement of Smad3 and CREB-1 in Mediating Transforming Growth Factor-β (TGFβ) Induction of TGFβ3 Secretion

Blood Lactate Functions as a Signal for Enhancing Fatty Acid Metabolism during Exercise via TGF-^|^beta; in the Brain

Determination of lipoprotein lipase activity in post heparin plasma of streptozotocin‐induced diabetic rats by high‐performance liquid chromatography with fluorescence detection

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