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Role of the interaction between Lu/BCAM and the spectrin-based membrane skeleton in the increased adhesion of hereditary spherocytosis red cells to laminin.
Br J Haematol. 2010 Feb; 148(3):456-65.BJ

Abstract

Lu/BCAM, the unique erythroid receptor for laminin 511/521, interacts with the erythrocyte membrane skeleton through spectrin binding. It has been reported that Hereditary Spherocytosis red blood cells (HS RBC) exhibit increased adhesion to laminin. We investigated the role of Lu/BCAM-spectrin interaction in the RBC adhesion properties of 2 splenectomised HS patients characterized by 40% spectrin deficiency. Under physiological flow conditions, HS RBC exhibited an exaggerated adhesion to laminin that was completely abolished by soluble Lu/BCAM. Triton extraction experiments revealed that a greater fraction of Lu/BCAM was unlinked to the membrane skeleton of HS RBC, as compared to normal RBC. Disruption of the spectrin interaction site in Lu/BCAM expressed in the transfected K562 cell line resulted in a weakened interaction to the skeleton and an enhanced interaction to laminin. These results demonstrated that the adhesion of HS RBC to laminin was mediated by Lu/BCAM and that its interaction with the spectrin-based skeleton negatively regulated cell adhesion to laminin. Finally, the results of this study strongly suggest that the reinforced adhesiveness of spectrin-deficient HS RBC to laminin is partly brought about by an impaired interaction between Lu/BCAM and the membrane skeleton.

Authors+Show Affiliations

Inserm, UMR-S 665, Paris.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Case Reports
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20092464

Citation

Gauthier, Emilie, et al. "Role of the Interaction Between Lu/BCAM and the Spectrin-based Membrane Skeleton in the Increased Adhesion of Hereditary Spherocytosis Red Cells to Laminin." British Journal of Haematology, vol. 148, no. 3, 2010, pp. 456-65.
Gauthier E, El Nemer W, Wautier MP, et al. Role of the interaction between Lu/BCAM and the spectrin-based membrane skeleton in the increased adhesion of hereditary spherocytosis red cells to laminin. Br J Haematol. 2010;148(3):456-65.
Gauthier, E., El Nemer, W., Wautier, M. P., Renaud, O., Tchernia, G., Delaunay, J., Le Van Kim, C., & Colin, Y. (2010). Role of the interaction between Lu/BCAM and the spectrin-based membrane skeleton in the increased adhesion of hereditary spherocytosis red cells to laminin. British Journal of Haematology, 148(3), 456-65. https://doi.org/10.1111/j.1365-2141.2009.07973.x
Gauthier E, et al. Role of the Interaction Between Lu/BCAM and the Spectrin-based Membrane Skeleton in the Increased Adhesion of Hereditary Spherocytosis Red Cells to Laminin. Br J Haematol. 2010;148(3):456-65. PubMed PMID: 20092464.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Role of the interaction between Lu/BCAM and the spectrin-based membrane skeleton in the increased adhesion of hereditary spherocytosis red cells to laminin. AU - Gauthier,Emilie, AU - El Nemer,Wassim, AU - Wautier,Marie P, AU - Renaud,Olivier, AU - Tchernia,Gil, AU - Delaunay,Jean, AU - Le Van Kim,Caroline, AU - Colin,Yves, PY - 2010/1/23/entrez PY - 2010/1/23/pubmed PY - 2010/8/11/medline SP - 456 EP - 65 JF - British journal of haematology JO - Br J Haematol VL - 148 IS - 3 N2 - Lu/BCAM, the unique erythroid receptor for laminin 511/521, interacts with the erythrocyte membrane skeleton through spectrin binding. It has been reported that Hereditary Spherocytosis red blood cells (HS RBC) exhibit increased adhesion to laminin. We investigated the role of Lu/BCAM-spectrin interaction in the RBC adhesion properties of 2 splenectomised HS patients characterized by 40% spectrin deficiency. Under physiological flow conditions, HS RBC exhibited an exaggerated adhesion to laminin that was completely abolished by soluble Lu/BCAM. Triton extraction experiments revealed that a greater fraction of Lu/BCAM was unlinked to the membrane skeleton of HS RBC, as compared to normal RBC. Disruption of the spectrin interaction site in Lu/BCAM expressed in the transfected K562 cell line resulted in a weakened interaction to the skeleton and an enhanced interaction to laminin. These results demonstrated that the adhesion of HS RBC to laminin was mediated by Lu/BCAM and that its interaction with the spectrin-based skeleton negatively regulated cell adhesion to laminin. Finally, the results of this study strongly suggest that the reinforced adhesiveness of spectrin-deficient HS RBC to laminin is partly brought about by an impaired interaction between Lu/BCAM and the membrane skeleton. SN - 1365-2141 UR - https://www.unboundmedicine.com/medline/citation/20092464/Role_of_the_interaction_between_Lu/BCAM_and_the_spectrin_based_membrane_skeleton_in_the_increased_adhesion_of_hereditary_spherocytosis_red_cells_to_laminin_ L2 - https://doi.org/10.1111/j.1365-2141.2009.07973.x DB - PRIME DP - Unbound Medicine ER -