Role of galectin-3 as a receptor for advanced glycosylation end products

Role of galectin-3 as a receptor for advanced glycosylation end products. The advanced glycosylation end product (AGE)-binding proteins identified so far include the components of the AGE-receptor complex p60, p90 and galectin-3, receptor for advanced glycosylation end products (RAGE), and the macrophage scavenger receptor types I and II. Galectin-3 interacts with β-galactoside residues of several cell surface and matrix glycoproteins through the carbohydrate recognition domain and is also capable of peptide–peptide associations mediated by its N-terminus domain. These structural properties enable galectin-3 to exert multiple functions, including the modulation of cell adhesion, the control of cell cycle, and the mRNA splicing activity. Moreover, in macrophages, astrocytes, and endothelial cells, galectin-3 has been shown to exhibit a high-affinity binding for AGEs; the lack of a transmembrane anchor sequence or signal peptide suggests that it associates with other AGE-receptor components rather than playing an independent role as AGE-receptor. In tissues that are targets of diabetic vascular complications, such as the mesangium and the endothelium, galectin-3 is not expressed or only weakly expressed under basal conditions, at variance with p90 and p60 but becomes detectable with aging and is induced or up-regulated by the diabetic milieu, which only slightly affects the expression of p90 or p60. This (over)expression of galectin-3 may in turn modulate AGE-receptor-mediated events by modifying the function of the AGE-receptor complex, which could play a role in the pathogenesis of target tissue injury. Up-regulated galectin-3 expression may also exert direct effects on tissue remodeling, independently of AGE ligands, by virtue of its adhesive and growth regulating properties

Age and growth of the Amazonian migratory catfish Brachyplatystoma rousseauxii in the Madeira River basin before the construction of dams

The goliath catfish Brachyplatystoma rousseauxii has crucial economical and ecological functions in the Amazon basin. Although its life history characteristics have been studied in the Amazon, there is little information in the Madeira River basin, which holds genetically distinct populations and where dams were recently built. Using fish collected in Bolivia, Brazil and Peru, this study provides a validation of growth rings deposition and details the growth patterns of B. rousseauxii in the Madeira before the dams' construction. Age structure and growth parameters were determined from 497 otolith readings. The species exhibits two growth rings per year and sampled fish were between 0 and 16 years old. In the Brazilian portion of the basin, mainly young individuals below 5 years old were found, whereas older fish (> 5 years) were caught only in the Bolivian and Peruvian stretches, indicating that after migrating upstream to reproduce, adults remain in the headwaters of the Madeira River. Comparing with previous publications, B. rousseauxii had a slower growth and 20 cm lower maximum standard length in the Madeira River than in the Amazon River. This study provides a baseline for future evaluation of changes in population dynamics of the species following dams closure.Santo Antonio Energia (SAE)Universidade Federal de Rondonia (UNIR)Instituto de Estudos e Pesquisas Agroambientais e Organizacoes Sustentaveis (IEPAGRO)CAPES [1402376, 047/2012, 6632/14-9]CNPq [204344/2015-8]Foundation of Support to Research of the Amazon [PAREV/FAPEAM 019/2010]FAPESP (Sao Paulo Research Foundation) [2016/07910-0]Univ Fed Rondonia UNIR, Dept Biol, Lab Ictiol & Pesca, BR 364,Km 9,5, BR-76801059 Porto Velho, RO, BrazilPrograma Posgrad Rede Biodiversidade & Biotechnol, BR 364,Km 9,5, BR-76801059 Porto Velho, RO, BrazilUAGRM, IRD, IIAP, LMI,EDIA, Montpellier, FranceINPA, Av Andre Araujo 2936, BR-69067375 Manaus, AM, BrazilUniv Fed Alagoas UFAL, Av Lourival Melo Mota,S-N Tabuleiro Martins, BR-57072900 Maceio, AL, BrazilUniv Fed Sao Paulo, Rua Doutor Carvalho Mendonca 144, BR-11070100 Santos, SP, BrazilUniv Fed Amazonas, Av Gen Rodrigo Octavio Jordao Ramos 3000, BR-69077000 Manaus, AM, BrazilIIAP, Vv Jose Quinones Km 2-5,Apartado Postal 784, Iquitos, PeruIRD, UMR BOREA, MNHN, CNRS 7208,SU,UCN,UA,IRD 207, Ave Agropolis 911, F-34394 Montpellier, FranceUMSS, ULRA, FAUNAGUA, ECOSINTEGRALES SRL, Ave Max Fernandez Final S-N, Cochabamba, BoliviaECOSINTEGRALES SRL, Res Act, Carlos Muller St 211, Cochabamba, Cercado, BoliviaInst Amazon Invest Cient SINCHI, Ave Vasquez Cobo Entre Calles 15 & 16, Bogota, ColombiaUniv Fed Sao Paulo, Rua Doutor Carvalho Mendonca 144, BR-11070100 Santos, SP, BrazilCAPES [1402376, 047/2012, 6632/14-9]CNPq [204344/2015-8][PAREV/FAPEAM 019/2010]FAPESP [2016/07910-0]Web of Scienc

Purinergic modulation of mesangial extracellular matrix production: Role in diabetic and other glomerular diseases

Background. Extracellular adenosine triphosphate (ATP) (eATP) mediates several biologic activities via purinergic P2 receptors (P2Rs). This study aimed at (1) evaluating the role of the purinergic system in modulating mesangial extracellular matrix (ECM) and transforming growth factor-beta (TGF-beta) production and (2 1 its contribution to diabetes-induced mesangial ECM accumulation. Methods. Rat mesangial cells were grown in normal glucose (5.5 mmol/L) or high glucose (30 mmol/L) containing media and probed with purinergic agonists and antagonists for the assessment of the expression pattern and function of P2Rs; release of ATP and activity of ectoATPases; and changes in ECM and TGF-beta expression. Results. Cells cultured in normal glucose and high glucose expressed similar amounts of functional P2Rs of the P2X(2), P2X(3), P2X(4), P2X(5), P2X(7), P2Y(1), P2Y(2), P2Y(4), and P2Y(6) subtypes. Levels of eATP were higher in high glucose vs. normal glucose, with unchanged ectc ATPase activity. The ATP-hydrolyzing enzymes hexokinase or apyrase reduced ECM and TGF-beta production from cells grow-a in high glucose, but not normal glucose. Under both normal glucose and high glucose conditions, ATP and the P2X7 agonist benzoylbenzoylATP increased dose-dependently ECM and TGF-beta production, whereas the P2Y agonist uridine triphosphate produced the opposite effect. The P2X7 inhibitor oxidized ATP attenuated the ECM and TGF-beta up-regulation induced by ATP and, to a lesser extent, that caused by high glucose. A TGF-beta neutralizing antibody also prevented ATP-induced ECM up-regulation. Conclusion. These data indicate a role for eATP in regulating ECM production via TGF-beta and suggest that P2XRs and P2YRs differentially modulate this process. An increased ATP release induced by hyperglycemia might contribute to mesangial matrix expansion occurring in diabetes

Increased retinal endothelial cell monolayer permeability induced by the diabetic milieu: role of advanced non-enzymatic glycation and polyol pathway activation

Background Increased vascular permeability could be involved in the pathogenesis of diabetic retinopathy. The present study was aimed at assessing whether high glucose concentrations can impair retinal endothelial cell barrier function directly, irrespective of changes in other determinants of permeability, and the role of non-enzymatic glycation and polyol pathway activation in these alterations. Methods Bovine retinal endothelial cells (BREC) were exposed for various periods to high glucose vs iso-osmolar mannitol and normal glucose containing media agents mimicking or inhibiting advanced glycation end product (AGE) formation and polyol pathway activation. Monolayer permeability was assessed by measuring the transendothelial passage of I-125-labeled proteins. Results Permeability increased significantly (up to +70%) in BREC exposed to high glucose, but not to mannitol, for 1-30 days, vs normal glucose control cells. Exposure to AGE-modified bovine serum albumin (BSA) (greater than or equal to 90%) and, to a lesser extent, sorbitol (+28%) mimicked the high glucose effect. The AGE formation and nitric oxide synthase (NOS) inhibitor aminoguanidine significantly reduced (by 60%) changes induced by 30-day exposure to high glucose, whereas methylguanidine, which inhibits only NOS activity, did not affect permeability. Aldose reductase or sorbitol dehydrogenase inhibitors decreased (by similar to 40%) the enhanced leakage produced by 1-day, but not 30-day, incubation in high glucose. Conclusions The present results indicate that high glucose is capable of impairing retinal endothelial cell barrier function directly and that nonenzymatic glycation and polyol pathway activation may mediate these changes, with AGES participating in the long-term alterations and increased flux through the sorbitol pathway in the short-term effect. Copyright (C) 2001 John Wiley & Sons Ltd