Fluidity gradient of erythrocyte membranes in diabetics: the effect of resorcylidene aminoguanidine

Waczulı́ková, Iveta; Šikurová, L; Čársky, J

doi:10.1016/s1567-5394(01)00134-7

Cited by 25 publications

(20 citation statements)

References 7 publications

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“…3B). The change in fluorescence polarization (0.034) was higher than several physiologically significant changes reported in the literature (41)(42)(43). On the contrary to our results with geldanamycin, another N-terminal inhibitor of Hsp90, radicicol (22) did not induce a significant change in DPH fluorescence polarization (data not shown).…”

Section: Geldanamycin Induces An Accelerated Lysis Of Jurkatcontrasting

confidence: 96%

Hsp90 Inhibition Accelerates Cell Lysis

Sreedhar¹,

Kálmán²,

Pato³

et al. 2003

Journal of Biological Chemistry

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The 90 kDa heat shock protein, Hsp90, is an abundant molecular chaperone participating in the cytoprotection of eukaryotic cells. Here we analyzed the involvement of Hsp90 in the maintenance of cellular integrity using partial cell lysis as a measure. Inhibition of Hsp90 by geldanamycin, radicicol, cisplatin, and novobiocin induced a significant acceleration of detergent-and hypotonic shock-induced cell lysis. The concentration and time dependence of cell lysis acceleration was in agreement with the Hsp90 inhibition characteristics of the N-terminal inhibitors, geldanamycin and radicicol. Glutathione and other reducing agents partially blocked geldanamycin-induced acceleration of cell lysis but were largely ineffective with other inhibitors. Indeed, geldanamycin treatment led to superoxide production and a change in membrane fluidity. When Hsp90 content was diminished using anti-Hsp90 hammerhead ribozymes, an accelerated cell lysis was also observed. Hsp90 inhibition-induced cell lysis was more pronounced in eukaryotic (yeast, mouse red blood, and human T-lymphoma) cells than in bacteria. Our results indicate that besides the geldanamycin-induced superoxide production, and a consequent increase in cell lysis, inhibition or lack of Hsp90 alone can also compromise cellular integrity. Moreover, cell lysis after hypoxia and complement attack was also enhanced by any type of Hsp90 inhibition used, which shows that the maintenance of cellular integrity by Hsp90 is important in physiologically relevant lytic conditions of tumor cells.The 90 kDa heat shock protein (Hsp90) 1 is a central part of a chaperone meshwork chaperoning a large number of substrate proteins (1-5). Besides being a partner of a large number of co-chaperones and substrates, Hsp90 binds to filamentous actin and tubulin (6 -8) and the involvement of the cytoskeleton in the traffic of Hsp90 substrates has also been demonstrated (5, 9). Together with other chaperones, like Hsp27 and Hsp70, Hsp90 is involved in cytoprotection (10 -12).Cell lysis is one of the most commonly used methods to test cellular integrity. Moreover, lysis rate anomalies (13,14) together with diffusional anomalies (15, 16) were used as important arguments for the organization of the cytoplasm. Since cellular integrity is preserved after a partial cell lysis to a large extent (13,14), partial lysis provides a highly sensitized, but still somewhat organized cellular system, where the contribution of various components to both the cytoplasmic organization and cellular stability can be studied.The original aim of the present study was to examine whether Hsp90 inhibition induces any change in the rate of cell lysis induced by mild detergent treatment or hypotonic shock. The rationale behind these experiments was to test, whether Hsp90, a cytoprotective chaperone, binding to "thousand-andone" substrates and other proteins is involved in the maintenance of cellular integrity (17), and whether its inhibition renders cells more "lysis-prone." The first experiments were very promising: geldan...

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Section: Geldanamycin Induces An Accelerated Lysis Of Jurkatcontrasting

confidence: 96%

Hsp90 Inhibition Accelerates Cell Lysis

Sreedhar¹,

Kálmán²,

Pato³

et al. 2003

Journal of Biological Chemistry

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“…In the presence of glycated albumin, antioxidant status of erythrocytes was strongly impaired with noted increase in hemolysis, LPO, and decrease in GSH levels indicating its pleiotropic action. Major pathological consequence of glycation is free radical induced erythrocytes membrane peroxidation resulting in increased membrane rigidity, decreased cellular deformability, reduced erythrocyte survival, higher rate of rouleaux formation, and lipid fluidity (Candiloros et al, 1996;Waczulikova et al, 2000). The presence of plant extracts during glycation significantly reduced the toxicity of glycated albumin and prevented erythrocyte oxidative damage.…”

Section: Discussionmentioning

confidence: 99%

Nutraceutical properties of dietary plants extracts: Prevention of diabetic nephropathy through inhibition of glycation and toxicity to erythrocytes and HEK293 cells

Tupe

Sankhe

Shaikh

et al. 2014

Pharmaceutical Biology

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Context: Glycated albumin is reported to elicit pathobiologic effects in diabetic nephropathy and abrogating its biologic effects has novel therapeutic potential. Objective: This study examines the effects of dietary plants extracts (Laurus nobilis, Carum carvi, Coccinia grandis, Mentha arvensis, Phaseolus vulgaris) against albumin glycation and its toxicity to erythrocytes and HEK293 cells. Materials and methods: Albumin (10 mg/ml) was incubated with fructose (250 mM) in PBS along with aqueous plant extracts (1% w/v) for 4 d. After incubation, the antiglycation potential of extracts was estimated by measuring AGEs, fructosamine, amyloids, carbonyls, free amino groups, and antioxidant potential of albumin. The glycation extent of the treated samples was determined by boronate affinity chromatography. Effect of extracts against glycation induced cytotoxicity in erythrocytes and HEK 293 cells was assessed by estimating viability, glutathione, and antioxidant capacity. Plant extracts were tested for their phenolic content and antioxidant potential (reducing potential, DPPH, ABTS, NO, and H 2 O 2 radical scavenging activities). Results: Plant extracts significantly decreased the AGEs formation and amyloid aggregation in glycated BSA (p50.001). Further, fructosamine and carbonyls were reduced to 55-72% and 83-89%, respectively. Free amino group and antioxidant activity of albumin were also preserved by 1.25-1.40-fold and 1.75-1.8-fold, respectively. Further, co-incubation of extracts with glycated albumin, protected erythrocytes, and HEK293 cells as they inhibited cellular hemolysis/toxicity (p50.001) by upregulating cellular antioxidants. Discussion and conclusion: Plant co-incubation reversed many modifications in albumin glycation, cellular dysfunction indicating that dietary sources with antiglycating and antioxidant potential could be considered for the effective management of diabetic nephropathy.

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“…Erythrocytes are more frequently exposed to albumin than other body tissue and thus, are more susceptible to oxidative damage induced by glycated albumin toxicity. Major pathological consequence of glycation is free radical induced erythrocytes membrane peroxidation which includes increased membrane rigidity, decreased cellular deformability, reduced erythrocyte survival and lipid fluidity (Waczulíkova et al 2000). Therefore the effect of glycation in presence and absence of plant extracts was evaluated in the present study.…”

Section: Discussionmentioning

confidence: 99%

Aqueous extract of some indigenous medicinal plants inhibits glycation at multiple stages and protects erythrocytes from oxidative damage–an in vitro study

et al. 2013

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Azadirachta indica, Emblica officinalis , Syzygium cumini and Terminalia bellirica are common in Indian system of traditional medicine for the prevention of diabetes and its complications. The aim of the present study was to comprehensively and comparatively investigate the antiglycation potential of these plant extracts at multiple stages and their possible protective effect against glycated albumin mediated toxicity to erythrocytes. Antiglycation activities of these plant extracts was measured by co-incubation of plant extract with bovine serum albumin-fructose glycation model. The multistage glycation markers-fructosamines (early stage), protein carbonyls (intermediate stage) and AGEs (late stage) are investigated along with measurement of thiols and β aggregation of albumin using amyloid-specific dyes-Congo red and Th T. Protection of erythrocytes from glycated albumin induced toxicity by these plant extracts was assessed by measuring erythrocytes hemolysis, lipid peroxidation, reduced glutathione and intracellular antioxidant capacity. Total phenolics, reducing power and antioxidant activities of the plant extracts were also measured. In vitro glycation assays showed that plant extracts exerted site specific inhibitory effects at multiple stages, with T. bellirica showing maximum attenuation. In erythrocytes, along with the retardation of glycated albumin induced hemolysis and lipid-peroxidation, T. bellirica considerably maintained cellular antioxidant potential. Significant positive correlations were observed between erythrocyte protection parameters with total phenolics. These plant extracts especially T. bellirica prevents glycation induced albumin modifications and subsequent toxicity to erythrocytes which might offer additional protection against diabetic vascular complications.

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Fluidity gradient of erythrocyte membranes in diabetics: the effect of resorcylidene aminoguanidine

Cited by 25 publications

References 7 publications

Hsp90 Inhibition Accelerates Cell Lysis

Hsp90 Inhibition Accelerates Cell Lysis

Nutraceutical properties of dietary plants extracts: Prevention of diabetic nephropathy through inhibition of glycation and toxicity to erythrocytes and HEK293 cells

Aqueous extract of some indigenous medicinal plants inhibits glycation at multiple stages and protects erythrocytes from oxidative damage–an in vitro study

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