Short-term effects of palmitate and 2-bromopalmitate on the lipolytic activity of rat adipocytes

Szkudelski, Tomasz; Szkudelska, Katarzyna

doi:10.1016/j.lfs.2011.07.010

Cited by 7 publications

(5 citation statements)

References 37 publications

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“…The reductions in embryo cleavage and blastocyst hatching are quite similar to previous work (Figure 5) [25]. Likewise, PPARδ inhibition significantly reduced mitochondrial activity, and we found that PPARδ inhibition not only reduced the mitochondrial membrane potential, but also the implantation potential of bovine embryos (Figure 7) [30,31].…”

Section: Discussionsupporting

confidence: 89%

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The PPARδ Agonist GW501516 Improves Lipolytic/Lipogenic Balance through CPT1 and PEPCK during the Development of Pre-Implantation Bovine Embryos

Idrees

Sheikh

et al. 2019

IJMS

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The PPARs (peroxisome proliferator-activated receptors) play critical roles in the regulation of lipid and glucose metabolism. PPARδ, a member of the PPARs family, is associated with decreased susceptibility to ectopic lipid deposition and is implicated in the regulation of mitochondrial processes. The current study aimed to determine the role of PPARδ in fatty acid β-oxidation and its influence on PEPCK for the lipogenic/lipolytic balance during in vitro bovine oocyte maturation and embryo development. Activation of PPARδ by GW501516, but not 2-BP, was indicated by intact embryonic PEPCK (cytosolic) and CPT1 expression and the balance between free fatty acids and mitochondrial β-oxidation that reduced ROS and inhibited p-NF-κB nuclear localization. Genes involved in lipolysis, fatty acid oxidation, and apoptosis showed significant differences after the GW501516 treatment relative to the control- and 2-BP-treated embryos. GSK3787 reversed the PPARδ-induced effects by reducing PEPCK and CPT1 expression and the mitochondrial membrane potential, revealing the importance of PPARδ/PEPCK and PPARδ/CPT1 for controlling lipolysis during embryo development. In conclusion, GW501516-activated PPARδ maintained the correlation between lipolysis and lipogenesis by enhancing PEPCK and CPT1 to improve bovine embryo quality.

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Section: Discussionsupporting

confidence: 89%

“…Immunofluorescent expression of the mitochondrial β-oxidation surrogate marker CPT1 also showed downregulation in the 2-BP-treated group (Figure 3C). 2-BP significantly translocated PPARδ to the nucleus, but repressed PEPCK and CPT1 expression by inhibiting fatty acid conversion to triglycerides and mitochondrial β-oxidation [29,30].…”

Section: Resultsmentioning

confidence: 99%

The PPARδ Agonist GW501516 Improves Lipolytic/Lipogenic Balance through CPT1 and PEPCK during the Development of Pre-Implantation Bovine Embryos

Idrees

Sheikh

et al. 2019

IJMS

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“…Then, the lysis buffer was added to each tube, and the mixture was shaken and incubated for 10 min at room temperature (Szkudelska et al . ; Szkudelski & Szkudelska ). Cell lysate was transferred to the assay plate, and total cAMP was measured using non‐acetylation EIA procedure according to the manufacturer's instruction.…”

Section: Methodsmentioning

confidence: 99%

Adipocyte dysfunction in rats with streptozotocin–nicotinamide‐induced diabetes

Szkudelska

Nogowski

Szkudelski

2014

Int J Experimental Path

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Administration of streptozotocin (STZ) and nicotinamide (NA) to adult rats allows for the induction of mild diabetes. However, this experimental model has not been fully characterized. This study was undertaken to determine the metabolic and secretory activity of adipose tissue in rats with STZ-NA-induced diabetes. Experiments were performed using epididymal adipocytes isolated from control and mildly diabetic rats. Lipogenesis, glucose transport as well as glucose and alanine oxidation, lipolysis, anti-lipolysis, cAMP levels and adipokine secretion were compared in cells isolated from the control and diabetic rats. Lipogenesis, glucose transport and oxidation were diminished in the adipocytes of diabetic rats compared with the fat cells of control animals. However, alanine oxidation appeared to be similar in the cells of non-diabetic and diabetic animals. Lipolytic response to low epinephrine concentrations was slightly increased in the adipocytes of diabetic rats; however, at higher concentrations of the hormone, lipolysis was similar in both groups of cells. The epinephrine-induced rise in cAMP levels was higher in the adipocytes of STZ-NA-induced diabetic rats, even in the presence of insulin. Lipolysis stimulated by dibutyryl-cAMP did not significantly differ, whereas anti-lipolytic effects of insulin were mildly decreased in the cells of diabetic rats. Secretion of adiponectin and leptin was substantially diminished in the adipocytes of diabetic rats compared with the cells of control animals. Our studies demonstrated that the balance between lipogenesis and lipolysis in the adipose tissue of rats with mild diabetes induced by STZ and NA is slightly shifted towards reduced lipid accumulation. Simultaneously, adiponectin and leptin secretion is significantly impaired.

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“…6). To determine whether palmitoylation has a role in activating endogenous ENaCs in mCCD cl1 cells, we treated polarized cultures of mCCD cl1 cells mounted in an Ussing chamber with either 2-bromopalmitate (2-BP), a general irreversible inhibitor of protein palmitoylation, or DMSO (vehicle control) (42)(43)(44). We observed a significant decrease in short circuit current (I sc ) within 5 min after apical addition of 2-BP that reached a new steady state I sc after 30 min (Fig.…”

Section: Palmitoylation Inhibitor 2-bromopalmitate Blunts Transepithementioning

confidence: 99%

Specific Palmitoyltransferases Associate with and Activate the Epithelial Sodium Channel

Mukherjee¹,

Wang²,

Kinlough³

et al. 2017

Journal of Biological Chemistry

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Edited by Henrik G. DohlmanThe epithelial sodium channel (ENaC) has an important role in regulating extracellular fluid volume and blood pressure, as well as airway surface liquid volume and mucociliary clearance. ENaC is a trimer of three homologous subunits (␣, ␤, and ␥). We previously reported that cytoplasmic residues on the ␤ (␤Cys-43 and ␤Cys-557) and ␥ (␥Cys-33 and ␥Cys-41) subunits are palmitoylated. Mutation of Cys that blocked ENaC palmitoylation also reduced channel open probability. Furthermore, ␥ subunit palmitoylation had a dominant role over ␤ subunit palmitoylation in regulating ENaC. To determine which palmitoyltransferases (termed DHHCs) regulate the channel, mouse ENaCs were co-expressed in Xenopus oocytes with each of the 23 mouse DHHCs. ENaC activity was significantly increased by DHHCs 1, 2, 3, 7, and 14. ENaC activation by DHHCs was lost when ␥ subunit palmitoylation sites were mutated, whereas DHHCs 1, 2, and 14 still activated ENaC lacking ␤ subunit palmitoylation sites. ␤ subunit palmitoylation was increased by ENaC co-expression with DHHC 7. Both wild type ENaC and channels lacking ␤ and ␥ palmitoylation sites co-immunoprecipitated with the five activating DHHCs, suggesting that ENaC forms a complex with multiple DHHCs. RT-PCR revealed that transcripts for the five activating DHHCs were present in cultured mCCD cl1 cells, and DHHC 3 was expressed in aquaporin 2-positive principal cells of mouse aldosterone-sensitive distal nephron where ENaC is localized. Treatment of polarized mCCD cl1 cells with a general inhibitor of palmitoylation reduced ENaC-mediated Na ؉ currents within minutes. Our results indicate that specific DHHCs have a role in regulating ENaC.ENaCs 2 are amiloride-sensitive Na ϩ channels that are found in high resistance epithelia and other tissues. In the aldosterone-sensitive distal nephron (ASDN), ENaC-dependent Na ϩ transport has an important role in the maintenance of extracellular fluid volume and blood pressure, as well as extracellular K ϩ homeostasis. In the lung, ENaC has a role in regulating airway surface fluid volume, mucociliary clearance, and alveolar fluid volume (1-3). The channels are composed of three homologous subunits (termed ␣, ␤, and ␥), each with two transmembrane domains, a large extracellular loop and cytoplasmic N and C termini (3-5).ENaCs are regulated by signaling pathways that modulate its membrane trafficking, residency on the plasma membrane, and degradation (6 -8). ENaCs are also regulated by a variety of extracellular factors that affect its open probability (P o ). These include extracellular cations (H ϩ , Na ϩ , and other metals), anions (Cl Ϫ ), laminar shear stress, and proteases that cleave ENaC subunits at specific sites and release embedded inhibitory tracts (1, 2, 9 -14). Intracellular phosphorylation, inositol phospholipids, and cytoplasmic Cys palmitoylation also regulate ENaC P o (15-21).Cys palmitoylation of soluble and transmembrane proteins is a reversible post-translational modification that increases protein surface hydr...

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Short-term effects of palmitate and 2-bromopalmitate on the lipolytic activity of rat adipocytes

Cited by 7 publications

References 37 publications

The PPARδ Agonist GW501516 Improves Lipolytic/Lipogenic Balance through CPT1 and PEPCK during the Development of Pre-Implantation Bovine Embryos

The PPARδ Agonist GW501516 Improves Lipolytic/Lipogenic Balance through CPT1 and PEPCK during the Development of Pre-Implantation Bovine Embryos

Adipocyte dysfunction in rats with streptozotocin–nicotinamide‐induced diabetes

Specific Palmitoyltransferases Associate with and Activate the Epithelial Sodium Channel

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