Significance of cytoplasmic fatty acid-binding protein for the ischemic heart

Glatz, Jan F. C.; Vork, M; Vusse, Ger J.

doi:10.1007/978-1-4615-3096-1_22

Cited by 5 publications

(5 citation statements)

References 37 publications

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“…Thus, accumulation of fatty acids surrounding the mitochondria subjects the fatty acids to lipid peroxidation, which in turn leads to mitochondrial damage. 25 Physiologically, these adverse events are prevented by the binding of intracellular fatty acids to fatty acid-binding protein (FABP) 26,27 or their transformation to acyl-CoA by acylCoA synthase. Acyl-CoA is metabolized through fatty acid ␤-oxidation; alternatively, the acyl group is removed and incorporated into nontoxic triglycerides.…”

Section: Discussionmentioning

confidence: 99%

PPARα Protects Proximal Tubular Cells from Acute Fatty Acid Toxicity

Kamijo

Hora²,

Kono

et al. 2007

Journal of the American Society of Nephrology

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Fatty acids bound to albumin are filtered through glomeruli, reabsorbed by proximal tubular epithelial cells, and metabolized. Because albumin serves as a carrier, an increase in delivery of fatty acids to the proximal tubule may occur in proteinuric states, possibly leading to toxic effects. At present, the contribution of fatty acids to tubulointerstitial damage and the mechanisms underlying this toxicity remain unclear. We recently found that the transcription factor peroxisome proliferator-activated receptor ␣ (PPAR␣) regulates fatty acid metabolism in proximal tubules, so we tested its role in tubular damage under proteinuric conditions. We induced protein-overload nephropathy in Ppara-null or wildtype (WT) mice by injecting fatty acids bound to BSA. Ppara-null mice exhibited greater renal dysfunction from severe proximal tubular injury than WT mice. Kidneys from Ppara-null mice injected with albumin alone showed little injury. Acute tubular injury was associated with deranged fatty acid homeostasis, increased oxidative stress, increased apoptosis, and activation of NFB signaling. These results suggest a role for fatty acids in proteinuria-associated tubular toxicity, as well as a protective role for PPAR␣. Modulation of PPAR␣ may be a future therapeutic option for tubular toxicity from fatty acids.

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Section: Discussionmentioning

confidence: 99%

PPARα Protects Proximal Tubular Cells from Acute Fatty Acid Toxicity

Kamijo

Hora²,

Kono

et al. 2007

Journal of the American Society of Nephrology

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“…Multiple species of FABPs had been identified and named according to the tissues of their first isolation sites such as heart (H-), epidermal (E-), brain (B-) and adipocyte (A-) types, however, they showed much wider tissue distribution than first thought (Gordon et al 1983;Alpers et al 1984;Hunt et al 1986;Siegenthaler et al 1993;Feng et al 1994;Kurtz et al 1994). Several roles have been assigned to these FABPs such as control of cellular uptake of fatty acids and their subsequent utilization and intracellular compartmentation, modulation of activity of enzymes involved in fatty acid metabolism, protection of cellular membranes and enzymes from detergent effects of fatty acids, and carriers of signaling fatty acids (Glatz et al 1993;Coe and Bernlohr 1998).…”

Section: Differential Localization Of Brain-type and Epidermal-type Fmentioning

confidence: 99%

Differential Localization of Brain-Type and Epidermal-Type Fatty Acid Binding Proteins in the Adrenal Gland of Mice

Xia

Nourani

Abdelwahab

et al. 2004

Tohoku J. Exp. Med.

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In immuno-light and -electron microscopy, brain-type fatty acid binding protein (B-FABP) is localized in the sustentacular cells enclosing the chromaffin cells in the adrenal medulla. This represents another new feature commonly shared by the sustentacular cells and ganglionic satellite cells, the latter of which has already been reported to localize this molecule, and suggests a common feature in lipid metabolism shared by the two cells enclosing peripheral neurons and paraneurons. On the other hand, epidermal-type fatty acid binding protein (E-FABP) is localized in two discrete cells in the adrenal gland: the one is a subpopulation of intra-adrenal macrophages which are intensely immunoreactive for F4/80, a marker of macrophages, and are rich in pleomorphic lysosomes. Because of their direct apposition to adjacent cortical endocrine cells and medullary chromaffin cells, the macrophages may be involved not only in phagocytosis of degenerating adrenal cells but also in exertion of some yet unknown effects on the endocrine function of the cortical and medullary cells via humoral factors such as cytokines which have recently been known to be secreted by macrophages. The other is a population of cells having scanty perikaryal cytoplasm poor in organneles and several thinny extended processes in the cortex and exhibiting weak immunoreactivity for E-FABP. The possible natures of these cells immunoreactive for E-FABP are discussed in view of a subpopulation of endothelial cells or the dendritic cells of antigen-presenting property.B-FABP; E-FABP; sustentacular cells; adrenal gland; immunohistochemistry

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“…The primary role of all FABP is the regulation of fatty acid uptake and intracellular transport. A-FABP impacts glucose and lipid metabolism, 5 plays a role in signal transduction, [6][7][8] and could contribute to cell proliferation and apoptotic processes. 9 In addition, FABP function as cytoplasmic shuttle proteins for ligand activation of PPAR (Peroxisome Proliferator-Activated Receptor).…”

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confidence: 99%

A‐FABP, a candidate progression marker of human transitional cell carcinoma of the bladder, is differentially regulated by PPAR in urothelial cancer cells

Boiteux

Lascombe

Roche

et al. 2009

Intl Journal of Cancer

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Superficial pT1 bladder tumors are characterized by a high risk of recurrence and progression in grade and stage. Few studies provided evidence that loss of adipocyte-fatty acid binding protein (A-FABP) expression was associated with bladder cancer progression. A-FABP is a lipid binding protein playing a role in intracellular lipid transport and metabolism, as well as in signal transduction. We reported from bladder tumors that decrease of A-FABP transcript level significantly correlated to tumor stage and to histologic grade (p < 0.05). Namely, in poor prognosis high grade pT1 tumors there was a loss of A-FABP expression compared to good prognosis tumors suggesting that re-expression of A-FABP could be a therapeutic approach in early stage bladder cancer to prevent disease progression. We demonstrated for the first time that this marker is upregulated by Peroxisome Proliferator-Activated Receptor (PPAR) a, b and c in T24 cells (derived from an undifferentiated grade III carcinoma) and only by PPARb in RT4 cells (derived from a well differentiated grade I papillary tumor). This effect occurred through a PPAR-dependent transcriptional mechanism without modifying mRNA stability and interestingly required de novo protein synthesis. Data as a whole suggest a prognostic significance of A-FABP in bladder cancer outcome and the potential utility of overexpression of this protein by PPAR agonists open up new perspectives in the treatment of bladder cancer.

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Significance of cytoplasmic fatty acid-binding protein for the ischemic heart

Cited by 5 publications

References 37 publications

PPARα Protects Proximal Tubular Cells from Acute Fatty Acid Toxicity

PPARα Protects Proximal Tubular Cells from Acute Fatty Acid Toxicity

Differential Localization of Brain-Type and Epidermal-Type Fatty Acid Binding Proteins in the Adrenal Gland of Mice

A‐FABP, a candidate progression marker of human transitional cell carcinoma of the bladder, is differentially regulated by PPAR in urothelial cancer cells

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