Differential actions of proteinases and neuraminidase on mammalian erythrocyte surface and its impact on erythrocyte agglutination by concanavalin A

Sharma, Savita; Gokhale, Sadashiv M.

doi:10.4149/gpb_2012_051

Cited by 2 publications

(1 citation statement)

References 25 publications

(39 reference statements)

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“…The integral protein glycophorin A represents 75% of all sialoglycoproteins in the membrane of RBCs [25]. Trypsin has a proteolytic effect only on glycophorin A [26][27][28].…”

Section: Discussionmentioning

confidence: 99%

Effects of trypsin on aggregation, disaggregation and aggregate morphology of red blood cells in autologous plasma and serum

2021

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We study the influence of trypsin on aggregation, disaggregation, and aggregate morphology of RBCs in autologous plasma and serum. The effect of trypsin on the surface charge of red blood cells and the aggregation of glutaraldehyde fixed cells after treatment with the enzyme was also studied. RBC aggregation was studied by means of an aggregometer and microscopic observations. The results obtained in this study indicate that trypsin treatment increases RBCs aggregation in autologous plasma and serum. The disaggregation of erythrocytes after trypsin treatment considerably decreased in autologous plasma and serum. Increase in the strength of red blood cell aggregates was observed in autologous plasma and serum. The microscopic images of RBCs aggregates indicate the formation of globular (pathologic) structures of aggregates in autologous plasma and serum. Trypsin decrease the surface charge of RBCs. In autologous plasma and serum, the cup shapes of RBCs appear. The control RBCs fixed with glutaraldehyde were not aggregated after their placement in autologous plasma. At the same time, red blood cells pretreated with trypsin and fixed with glutaraldehyde interact with each other in autologous plasma. The physiological significance of glycoproteins of erythrocyte surface for RBCs aggregation was discussed.

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“…The integral protein glycophorin A represents 75% of all sialoglycoproteins in the membrane of RBCs [25]. Trypsin has a proteolytic effect only on glycophorin A [26][27][28].…”

Section: Discussionmentioning

confidence: 99%

Effects of trypsin on aggregation, disaggregation and aggregate morphology of red blood cells in autologous plasma and serum

2021

Preprint

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A Comparative Protein Profile of Mammalian Erythrocyte Membranes Identified by Mass Spectrometry

et al. 2014

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A comparative analysis of erythrocyte membrane proteins of economically important animals, goat (Capra aegagrus hircus), buffalo (Bubalus bubalis), pig (Sus scrofa), cow (Bos tauras), and human (Homo sapiens) was performed. Solubilized erythrocyte membrane proteins were separated by sodium dodecyl sulfate-polyacryamide gel electrophoresis (SDS-PAGE), visualized by staining the gels with Commassie Brilliant Blue (CBB), and identified by matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/MS). Emerging results show that all major erythrocyte membrane proteins present in human are also seen in all the animals except for band 4.5 which could not be identified. Band 3 is seen as more intense and compact, band 4.1 appears as a doublet in all the animal erythrocyte membranes, band 4.2 exhibits a slightly higher molecular weight (Mr) in buffalo, and cow and band 4.9 has a higher Mr in all the animals relative to the human protein. In addition, there are two new bands in the goat membrane, band G1, identified as HSP 90α, and band G2 identified as HSP 70. A new band C2 identified as HSP 70 is also seen in cow membranes. Peroxiredoxin II is of lower intensity and/or higher Mr in the animals. The difference in size of the proteins possibly indicates the variations in the composition of the amino acids. The difference in intensity of the proteins among these mammalians highlights the presence of less or more number of copies of that protein per cell. This data complement the earlier observations of differences in the sialoglycoprotein profile and effect of proteases and neuraminidase on agglutination among the mammalian erythrocytes. This study provides a platform to understand the molecular architecture of the individual erythrocytes, and in turn the dependent disorders, their phylogenetic relationship and also generates a database of erythrocyte membrane proteins of mammals. The animals selected for this study are of economic importance as they provide milk for the dairy industry and raw material for leather industry and are routinely sacrificed to obtain non vegetarian food worldwide.

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Differential actions of proteinases and neuraminidase on mammalian erythrocyte surface and its impact on erythrocyte agglutination by concanavalin A

Cited by 2 publications

References 25 publications

Effects of trypsin on aggregation, disaggregation and aggregate morphology of red blood cells in autologous plasma and serum

Effects of trypsin on aggregation, disaggregation and aggregate morphology of red blood cells in autologous plasma and serum

A Comparative Protein Profile of Mammalian Erythrocyte Membranes Identified by Mass Spectrometry

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Differential actions of proteinases and neuraminidase on mammalian erythrocyte surface and its impact on erythrocyte agglutination by concanavalin A

Cited by 2 publications

References 25 publications

Effects of trypsin on aggregation, disaggregation and aggregate morphology of red blood cells in autologous plasma and serum

Effects of trypsin on aggregation, disaggregation and aggregate morphology of red blood cells in autologous plasma and serum

A Comparative Protein Profile of Mammalian Erythrocyte Membranes Identified by Mass Spectrometry

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Differential actions of proteinases and neuraminidase on mammalian erythrocyte surface and its impact on erythrocyte agglutination by concanavalin A