Carbohydrate induced modulation of cell membrane. VI. Binding of exogenous lectin induces susceptibility of erythrocytes to free radical damage: a spin label study

Hajela, Krishnan; Pande, Abhay H.; Sumati,

doi:10.1016/s0014-5793(97)00272-x

Cited by 5 publications

(10 citation statements)

References 22 publications

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“…This membrane destabilization could be due to the lectin-like behaviour of CRP [16,45]. Thus CRP when added exogenously will cross-link with the membrane surface receptors leading to lateral molecular reorganizations in the plane of the bilayer [63][64][65].…”

Section: Discussionmentioning

confidence: 99%

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Disease-associated glycosylated molecular variants of human C-reactive protein activate complement-mediated hemolysis of erythrocytes in tuberculosis and Indian visceral leishmaniasis

et al. 2009

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Human C-reactive protein (CRP), as a mediator of innate immunity, removed damaged cells by activating the classical complement pathway. Previous studies have successfully demonstrated that CRPs are differentially induced as glycosylated molecular variants in certain pathological conditions. Affinity-purified CRPs from two most prevalent diseases in India viz. tuberculosis (TB) and visceral leishmaniasis (VL) have differential glycosylation in their sugar composition and linkages. As anemia is a common manifestation in TB and VL, we assessed the contributory role of glycosylated CRPs to influence hemolysis via CRP-complement-pathway as compared to healthy control subjects. Accordingly, the specific binding of glycosylated CRPs with erythrocytes was established by flow-cytometry and ELISA. Significantly, deglycosylated CRPs showed a 7-8-fold reduced binding with erythrocytes confirming the role of glycosylated moieties. Scatchard analysis revealed striking differences in the apparent binding constants (10(4)-10(5) M(-1)) and number of binding sites (10(6)-10(7)sites/erythrocyte) for CRP on patients' erythrocytes as compared to normal. Western blotting along with immunoprecipitation analysis revealed the presence of distinct molecular determinants on TB and VL erythrocytes specific to disease-associated CRP. Increased fragility, hydrophobicity and decreased rigidity of diseased-erythrocytes upon binding with glycosylated CRP suggested membrane damage. Finally, the erythrocyte-CRP binding was shown to activate the CRP-complement-cascade causing hemolysis, even at physiological concentration of CRP (10 microg/ml). Thus, it may be postulated that CRP have a protective role towards the clearance of damaged-erythrocytes in these two diseases.

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Section: Discussionmentioning

confidence: 99%

“…However, physiological level of PC and Ca +2 were added to facilitate erythrocyte-CRP binding in vitro. This erythrocyte-CRP binding might thus activate the complement mediated-hemolysis in TB and VL and this could cause formation of membrane leaks [63][64][65][66][67].…”

Section: Discussionmentioning

confidence: 99%

Disease-associated glycosylated molecular variants of human C-reactive protein activate complement-mediated hemolysis of erythrocytes in tuberculosis and Indian visceral leishmaniasis

et al. 2009

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“…However, no release of oxyhemoglobin was observed in erythrocytes, which were neither treated with lectin nor exposed to oxidative damage (control), or lectin treated cells but not exposed to oxyradical shock. Lectin mediated crosslinking of erythrocyte surface glycoprotein has been reported to significantly enhance the susceptibility to free radical induced membrane damage (Hajela et al, 1997). The effect of lectin induced agglutination on the rate of oxidative damage to the cell membrane revealed that lectin induced perturbations in cell membrane make it more vulnerable to oxidative attack.…”

Section: Resultsmentioning

confidence: 99%

Studies on the role of goat heart galectin-1 as a tool for detecting post-malignant changes in glycosylation pattern

Ashraf¹,

Perveen²,

Tabrez³

et al. 2015

Saudi Journal of Biological Sciences

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Galectins are mammalian lectins established to play a crucial role in the progression of various cancer types by the virtue of their differential expression in normal and cancerous cells. In the present study, goat heart galectin-1 (GHG-1) was purified and investigated for its potential role in the detection of post-malignant changes in glycosylation pattern. When exposed to superoxide radicals generated from a pyrogallol auto-oxidation system, GHG-1 treated erythrocyte suspension released higher amount of oxyhemoglobin than the unagglutinated erythrocytes. The extent of erythrocyte hemolysis was found to be directly proportional to concentrations of hypochlorous acid. GHG-1 was used to detect the change in the β-galactoside expression pattern in erythrocyte membrane from human donors suffering from prostate and breast cancer. No significant change was observed in the hemolysis of lectin agglutinated erythrocytes collected from pre-operated breast cancer patients, whereas significant increase was observed in normal healthy control and post-operated samples. Findings of this study proclaim GHG-1 as an important tool for the detection of post-malignant changes in glycosylation pattern.

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“…Results are reported as percentage of lysis, the extent of lysis of identical volume of erythrocyte suspension in distilled water being set to 100%. Agglutinated cells were exposed to superoxide radical, generated from a pyrogallol autooxidation system by adding 10 μl of pyrogallol solution (0.02 M freshly made in H 2 O) and incubated for a period of 20 min at 30 °C [16]. The released oxyhemoglobin concentration in supernatants was measured by method of Winterbourne [18].…”

Section: Methodsmentioning

confidence: 99%

Carbohydrate‐induced modulation of cell membrane. VIII. Agglutination with mammalian lectin galectin‐1 increases osmofragility and membrane fluidity of trypsinized erythrocytes

et al. 2006

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Interaction of lectins with cell surface determinants may alter membrane properties. Using trypsinized rabbit erythrocytes as model we tested the capacity of an endogenous lectin in this respect. Galectin-1 is a member of an adhesion/growthregulatory family known to interact for example with ganglioside GM 1 and also the hydrophobic tail of oncogenic H-Ras. Assays on membrane fluidity and osmofragility detect galectin-1's capacity to increase the parameters. Moreover, it increases susceptibility of erythrocytes to radical damage. These observations indicate the potential of this endogenous lectin to affect membrane properties beyond the immediate interaction with cell surface epitopes.

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Carbohydrate induced modulation of cell membrane. VI. Binding of exogenous lectin induces susceptibility of erythrocytes to free radical damage: a spin label study

Cited by 5 publications

References 22 publications

Disease-associated glycosylated molecular variants of human C-reactive protein activate complement-mediated hemolysis of erythrocytes in tuberculosis and Indian visceral leishmaniasis

Disease-associated glycosylated molecular variants of human C-reactive protein activate complement-mediated hemolysis of erythrocytes in tuberculosis and Indian visceral leishmaniasis

Studies on the role of goat heart galectin-1 as a tool for detecting post-malignant changes in glycosylation pattern

Carbohydrate‐induced modulation of cell membrane. VIII. Agglutination with mammalian lectin galectin‐1 increases osmofragility and membrane fluidity of trypsinized erythrocytes

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