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  • Spaceflight regulates ryanodine receptor subtype 1 in portal vein myocytes in the opposite way of hypertension. 22096120

    Gravity has a structural role for living systems. Tissue development, architecture, and organization are modified when the gravity vector is changed. In particular, microgravity induces a redistribution of blood volume and thus pressure in the astronaut body, abolishing an upright blood pressure gradient, inducing orthostatic hypotension. The present study was designed to investigate whether isolated vascular smooth muscle cells are directly sensitive to altered gravitational forces and, second, whether sustained blood pressure changes act on the same molecular target. Exposure to microgravity during 8 days in the International Space Station induced the decrease of ryanodine receptor subtype 1 expression in primary cultured myocytes from rat hepatic portal vein. Identical results were found in portal vein from mice exposed to microgravity during an 8-day shuttle spaceflight. To evaluate the functional consequences of this physiological adaptation, we have compared evoked calcium signals obtained in myocytes from hindlimb unloaded rats, in which the shift of blood pressure mimics the one produced by the microgravity, with those obtained in myocytes from rats injected with antisense oligonucleotide directed against ryanodine receptor subtype 1. In both conditions, calcium signals implicating calcium-induced calcium release were significantly decreased. In contrast, in spontaneous hypertensive rat, an increase in ryanodine receptor subtype 1 expression was observed as well as the calcium-induced calcium release mechanism. Taken together, our results shown that myocytes were directly sensitive to gravity level and that they adapt their calcium signaling pathways to pressure by the regulation of the ryanodine receptor subtype 1 expression.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • Administration of estradiol-17beta increases anterior pituitary IGF-I and relative amounts of serum and anterior pituitary IGF-binding proteins in barrows. 11831520

    Two experiments were conducted to determine whether 1) administration of estradiol-173 (E2) implants to barrows elevates serum concentrations of E2 to levels similar to those of adult boars and subsequently affects the anterior pituitary gland IGF system and 2) administration of E2 to barrows increases serum concentrations of E2, serum and anterior pituitary concentrations of IGF-I, and relative amounts of serum and anterior pituitary IGF-binding proteins (IGFBP), vs boars and unimplanted barrows. In Exp. 1, 20 crossbred barrows (150 +/- 6 d, 103 +/- 8 kg) were administered varying number of E2 implants (0, 2, 3, 4; n = 5/group) on d 1. Blood samples were collected weekly by jugular venipuncture, beginning on d 1. Pigs were killed on d 36 when a blood sample and anterior pituitary were collected. Serum concentrations of E2 were increased (P 0.05) in pigs with 2,3, and 4 implants vs 0 implants, but no difference (P > 0.05) was detected in serum concentrations of E2 among pigs with 2, 3, and 4 implants. Orthogonal contrasts identified that three or four E2 implants were necessary to increase serum concentrations of E2 to that similar to boars. Serum and anterior pituitary concentrations of IGF-I were increased (P 0.05) in pigs with 2, 3, and 4 implants vs 0 implants. Relative amounts of anterior pituitary IGFBP-2 and - 5 increased (P 0.05) in response to administration of E2. In Exp. 2, three treatment groups were randomly allotted by litter; boars (n = 11), E2-implanted barrows (n = 9), and unimplanted barrows (n = 12). A blood sample was taken from all pigs on d 1 and every 14 d thereafter. Implanted pigs received four implants on d 1. Pigs were killed on d 91, when a blood sample and anterior pituitary were collected. Mean serum concentrations of E2 were greater (P 0.05) in implanted pigs vs boars. Mean serum concentrations of IGF-I (ng/mL) were greater (P 0.05) in boars (238.7 +/- 6.8) than in implanted barrows (170.2 +/- 8.9) and unimplanted (150.4 +/- 6.7) pigs and tended to be greater (P = 0.08) in implanted vs unimplanted pigs. Mean anterior pituitary concentrations of IGF-I (ng/mg tissue) were greater (P 0.05) in implanted (773.6 +/- 57.0) pigs than boars (251.9 +/- 51.6) and unimplanted (185.6 +/- 49.4) pigs. Relative amounts of serum IGFBP-2 were greater (P 0.05) in implanted pigs vs boars. Relative amounts of anterior pituitary IGFBP-2 and -5 were greater (P 0.05) in boars than in implanted and unimplanted pigs. These data suggest that E2 may influence components of the porcine IGF system in the serum and anterior pituitary. Other gonadal factors present in boars may additionally affect the serum and anterior pituitary IGF system.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple

  • Modification of the primary tumor microenvironment by transforming growth factor alpha-epidermal growth factor receptor signaling promotes metastasis in an orthotopic col ... 18583324

    The transforming growth factor alpha (TGFalpha)/epidermal growth factor receptor (EGFR) signaling pathway appears to play a critical role in colon cancer progression, but the cellular and molecular mechanisms that contribute to metastasis remain unknown. KM12C colon cancer cell clones expressing high (C9) or negligible (C10) levels of TGFalpha were implanted into the cecal walls of nude mice. C9 tumors formed autocrine and paracrine EGFR networks, whereas C10 tumors were unable to signal through EGFR. The tumor microenvironment of C9, but not C10, contained cells enriched in vascular endothelial growth factor (VEGF) A, interleukin-8, and matrix metalloproteinases-2 and -9 and had a high vascular surface area. C9 tumors recruited a macrophage population that co-expressed F4/80 and lymphatic vessel endothelial hyaluronic acid receptor and produced VEGFC. The mean lymphatic density of C9 tumors was threefold higher than that of C10 tumors. C9, but not C10, tumor cells metastasized to regional lymph nodes in all mice and to the liver in 5 of 10 mice. Forced expression of TGFalpha in C10 tumor cells led to the generation of autocrine and paracrine EGFR signaling, macrophage recruitment, enhanced blood and lymphatic vascular surface areas, and increased lymphatic metastasis. Collectively, these data show that activation of TGFalpha-EGFR signaling in colon cancer cells creates a microenvironment that is conducive for metastasis, providing a rationale for efforts to inhibit EGFR signaling in TGFalpha-positive colon cancers.
    Document Type:
    Reference
    Product Catalog Number:
    AB13458

  • Certificate of Analysis BI0832 47173

    Document Type:
    Certificate of Analysis
    Lot Number:
    47173
    Product Catalog Number:
    BI0832
    Product Catalog Name:
    Deblocking Reagent 3% Dichloroacetic Acid in Toluene

  • Hepatic steatosis and plasma dyslipidemia induced by a high-sucrose diet are corrected by an acute leptin infusion. 17363621

    High sucrose (HS) feeding in rats induces hepatic steatosis and plasma dyslipidemia. In previous reports (Huang W, Dedousis N, Bhatt BA, O'Doherty RM. J Biol Chem 279: 21695-21700, 2004; and Huang W, Dedousis N, Bandi A, Lopaschuk GD, O'Doherty RM. Endocrinology 147: 1480-1487, 2006), our laboratory demonstrated a rapid ( approximately 100 min) leptin-induced decrease in liver and plasma VLDL triglycerides (TG) in lean rats, effects that were abolished in obese rats fed a high-fat diet, a model that also presents with hepatic steatosis and plasma dyslipidemia. To further examine the capacity of acute leptin treatment to improve metabolic abnormalities induced by nutrient excess, hepatic leptin action was studied in rats after 5 wk of HS feeding. HS feeding induced hepatic steatosis (TG+80+/-8%; P=0.001), plasma hyperlipidemia (VLDL-TG+102+/-14%; P=0.001), hyperinsulinemia (plasma insulin +67+/-12%; P=0.04), and insulin resistance as measured by homeostasis model assessment (+125+/-20%; P=0.02), without increases in adiposity or plasma leptin concentration compared with standard chow-fed controls. A 120-min infusion of leptin (plasma leptin 13.6+/-0.7 ng/ml) corrected hepatic steatosis (liver TG-29+/-3%; P=0.003) and plasma hyperlipidemia in HS (VLDL-TG-42+/-4%; P=0.001) and increased plasma ketones (+45+/-3%; P=0.006), without altering plasma glucose, insulin, or homeostasis model assessment compared with saline-infused HS controls. In addition, leptin activated liver phosphatidylinositol 3-kinase (+70+/-18%; P=0.01) and protein kinase B (Akt; +90+/-29%; P=0.02), and inhibited acetyl-CoA carboxylase (40+/-7%; P=0.04) in HS, further demonstrating that hepatic leptin action was intact in these animals. We conclude that 1) leptin action on hepatic lipid metabolism remains intact in HS-fed rats, 2) leptin rapidly reverses hepatic steatosis and plasma dyslipidemia induced by sucrose, and 3) the preservation of hepatic leptin action after a HS diet is associated with the maintenance of low adiposity and plasma leptin concentrations.
    Document Type:
    Reference
    Product Catalog Number:
    07-303
    Product Catalog Name:
    Anti-phospho-Acetyl CoA Carboxylase (Ser79) Antibody

  • Beta-adrenoceptor stimulation potentiates insulin-stimulated PKB phosphorylation in rat cardiomyocytes via cAMP and PKA. 20412069

    BACKGROUND AND PURPOSE: Genetic approaches have documented protein kinase B (PKB) as a pivotal regulator of heart function. Insulin strongly activates PKB, whereas adrenaline is not considered a major physiological regulator of PKB in heart. In skeletal muscles, however, adrenaline potentiates insulin-stimulated PKB activation without having effect in the absence of insulin. The purpose of the present study was to investigate the interaction between insulin and beta-adrenergic stimulation in regulation of PKB phosphorylation. EXPERIMENTAL APPROACH: Cardiomyocytes were isolated from adult rats by collagenase, and incubated with insulin, isoprenaline, and other compounds. Protein phosphorylation was evaluated by Western blot and phospho-specific antibodies. KEY RESULTS: Isoprenaline increased insulin-stimulated PKB Ser(473) and Thr(308) phosphorylation more than threefold in cardiomyocytes. Isoprenaline alone did not increase PKB phosphorylation. Isoprenaline also increased insulin-stimulated GSK-3beta Ser(9) phosphorylation approximately twofold, supporting that PKB phosphorylation increased kinase activity. Dobutamine (beta(1)-agonist) increased insulin-stimulated PKB phosphorylation as effectively as isoprenaline (more than threefold), whereas salbutamol (beta(2)-agonist) only potentiated insulin-stimulated PKB phosphorylation by approximately 80%. Dobutamine, but not salbutamol, increased phospholamban Ser(16) phosphorylation and glycogen phosphorylase activation (PKA-mediated effects). Furthermore, the cAMP analogue that activates PKA (dibutyryl-cAMP and N(6)-benzoyl-cAMP) increased insulin-stimulated PKB phosphorylation by more than threefold without effect alone. The Epac-specific activator 8-(4-chlorophenylthio)-2'-O-methyl-cAMP (007) increased insulin-stimulated PKB phosphorylation by approximately 50%. Db-cAMP and N(6)-benzoyl-cAMP, but not 007, increased phospholamban Ser(16) phosphorylation. CONCLUSIONS AND IMPLICATIONS: beta-adrenoceptors are strong regulators of PKB phosphorylation via cAMP and PKA when insulin is present. We hypothesize that PKB mediates important signalling in the heart during beta-adrenergic receptors stimulation.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • Short-term in vivo inhibition of insulin receptor substrate-1 expression leads to insulin resistance, hyperinsulinemia, and increased adiposity. 15550510

    Insulin receptor substrate-1 (IRS-1) has an important role as an early intermediary between the insulin and IGF receptors and downstream molecules that participate in insulin and IGF-I signal transduction. Here we employed an antisense oligonucleotide (IRS-1AS) to inhibit whole-body expression of IRS-1 in vivo and evaluate the consequences of short-term inhibition of IRS-1 in Wistar rats. Four days of treatment with IRS-1AS reduced the expression of IRS-1 by 80, 75, and 65% (P less than 0.05) in liver, skeletal muscle, and adipose tissue, respectively. This was accompanied by a 40% (P less than 0.05) reduction in the constant of glucose decay during an insulin tolerance test, a 78% (P less than 0.05) reduction in glucose consumption during a hyperinsulinemic-euglycemic clamp, and a 90% (P less than 0.05) increase in basal plasma insulin level. The metabolic effects produced by IRS-1AS were accompanied by a significant reduction in insulin-induced [Ser (473)] Akt phosphorylation in liver (85%, P less than 0.05), skeletal muscle (40%, P less than 0.05), and adipose tissue (85%, P less than 0.05) and a significant reduction in insulin-induced tyrosine phosphorylation of ERK in liver (20%, P less than 0.05) and skeletal muscle (30%, P less than 0.05). However, insulin-induced tyrosine phosphorylation of ERK was significantly increased (60%, P less than 0.05) in adipose tissue of IRS-1AS-treated rats. In rats treated with IRS-1AS for 8 d, a 100% increase (P less than 0.05) in relative epididymal fat weight and a 120% (P less than 0.05) increase in nuclear expression of peroxisome proliferator-activated receptor-gamma were observed. Thus, acute inhibition of IRS-1 expression in rats leads to insulin resistance accompanied by activation of a growth-related pathway exclusively in white adipose tissue.
    Document Type:
    Reference
    Product Catalog Number:
    AB1603
    Product Catalog Name:
    Anti-Phosphoserine Antibody

  • Persistent diet-induced obesity in male C57BL/6 mice resulting from temporary obesigenic diets. 19401758

    BACKGROUND: Does diet-induced obesity persist after an obesigenic diet is removed? We investigated this question by providing male C57BL/6 mice with free access to two different obesigenic diets followed by a switch to chow to determine if obesity was reversible. METHODOLOGY/PRINCIPAL FINDINGS: Male C57BL/6 mice were randomly assigned to five weight-matched groups: 1) C group that continuously received a chow diet; 2) HF group on a 60% high fat diet; 3) EN group on the high fat diet plus liquid Ensure; 4) HF-C group switched from high fat to chow after 7 weeks; 5) EN-C group switched from high fat plus Ensure to chow after 7 weeks. All food intake was ad libitum. Body weight was increased after 7 weeks on both obesigenic diets (44.6+/-0.65, 39.8+/-0.63, and 28.6+/-0.63 g for EN, HF, and C groups, respectively) and resulted in elevated concentrations of serum insulin, glucose, and leptin and lower serum triglycerides. Development of obesity in HF and EN mice was caused by increased energy intake and a relative decrease of average energy output along with decreased ambulatory activity. After the switch to chow, the HF-C and EN-C groups lost weight but subsequently maintained a state of persistent obesity in comparison to the C group (34.8+/-1.2, 34.1+/-1.2 vs. 30.8+/-0.8 g respectively; P0.05) with a 40-50% increase of body fat. All serum hormones and metabolites returned to control levels with the exception of a trend for increased leptin. The HF-C and EN-C groups had an average energy output in line with the C group and the persistent obesity was maintained despite a non-significant increase of energy intake of less than 1 kcal/d at the end of the study. CONCLUSION: Our results illustrate the importance of considering the history of energy imbalance in determining body weight and that a persistent elevation of body weight after removal of obesigenic diets can result from very small increases of energy intake.
    Document Type:
    Reference
    Product Catalog Number:
    SRI-13K
    Product Catalog Name:
    Sensitive Rat Insulin RIA

  • Cereal and nonfat milk support muscle recovery following exercise. 19442266

    ABSTRACT: BACKGROUND: This study compared the effects of ingesting cereal and nonfat milk (Cereal) and a carbohydrate-electrolyte sports drink (Drink) immediately following endurance exercise on muscle glycogen synthesis and the phosphorylation state of proteins controlling protein synthesis: Akt, mTOR, rpS6 and eIF4E. METHODS: Trained cyclists or triathletes (8 male: 28.0 +/- 1.6 yrs, 1.8 +/- 0.0 m, 75.4 +/- 3.2 kg, 61.0 +/- 1.6 ml O2*kg-1*min-1; 4 female: 25.3 +/- 1.7 yrs, 1.7 +/- 0.0 m, 66.9 +/- 4.6 kg, 46.4 +/- 1.2 mlO2*kg-1*min-1) completed two randomly-ordered trials serving as their own controls. After 2 hours of cycling at 60-65% VO2MAX, a biopsy from the vastus lateralis was obtained (Post0), then subjects consumed either Drink (78.5 g carbohydrate) or Cereal (77 g carbohydrate, 19.5 g protein and 2.7 g fat). Blood was drawn before and at the end of exercise, and at 15, 30 and 60 minutes after treatment. A second biopsy was taken 60 minutes after supplementation (Post60). Differences within and between treatments were tested using repeated measures ANOVA. RESULTS: At Post60, blood glucose was similar between treatments (Drink 6.1 +/- 0.3, Cereal 5.6 +/- 0.2 mmol/L, p .05), but after Cereal, plasma insulin was significantly higher (Drink 123.1 +/- 11.8, Cereal 191.0 +/- 12.3 pmol/L, p .05), and plasma lactate significantly lower (Drink 1.4 +/- 0.1, Cereal 1.00 +/- 0.1 mmol/L, p .05). Except for higher phosphorylation of mTOR after Cereal, glycogen and muscle proteins were not statistically different between treatments. Significant Post0 to Post60 changes occurred in glycogen (Drink 52.4 +/- 7.0 to 58.6 +/- 6.9, Cereal 58.7 +/- 9.6 to 66.0 +/- 10.0 mumol/g, p .05) and rpS6 (Drink 17.9 +/- 2.5 to 35.2 +/- 4.9, Cereal 18.6 +/- 2.2 to 35.4 +/- 4.4 %Std, p .05) for each treatment, but only Cereal significantly affected glycogen synthase (Drink 66.6 +/- 6.9 to 64.9 +/- 6.9, Cereal 61.1 +/- 8.0 to 54.2 +/- 7.2%Std, p .05), Akt (Drink 57.9 +/- 3.2 to 55.7 +/- 3.1, Cereal 53.2 +/- 4.1 to 60.5 +/- 3.7 %Std, p .05) and mTOR (Drink 28.7 +/- 4.4 to 35.4 +/- 4.5, Cereal 23.0 +/- 3.1 to 42.2 +/- 2.5 %Std, p .05). eIF4E was unchanged after both treatments. CONCLUSION: These results suggest that Cereal is as good as a commercially-available sports drink in initiating post-exercise muscle recovery.
    Document Type:
    Reference
    Product Catalog Number:
    05-736
    Product Catalog Name:
    Anti-phospho-Akt1/PKBα (Ser473) Antibody, clone SK703, rabbit monoclonal