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B-CAM/LU expression and the role of B-CAM/LU activation in binding of low- and high-density red cells to laminin in sickle cell disease.
Am J Hematol. 2004 Feb; 75(2):63-72.AJ

Abstract

Red blood cells from patients with sickle cell disease (SS RBC) adhere to laminin and over-express the high-affinity laminin receptor basal cell adhesion molecule/Lutheran protein (B-CAM/LU). This receptor has recently been shown to undergo activation in vitro through a protein kinase A-dependent mechanism. Low-density SS RBC express two-thirds more B-CAM/LU than high-density SS RBC. However, high-density SS RBC have been identified as most adherent to laminin under flow conditions. We investigated the ability of low- and high-density SS RBC to interact with laminin under various conditions and explored factors that might be responsible for the differences in B-CAM/LU-laminin interaction between high- and low-density SS RBC. We confirmed that high-density SS RBC adhere to laminin more strongly than low-density SS RBC under flow conditions. However, low-density SS RBC bind soluble laminin most strongly and are the most adherent to laminin under static conditions. Soluble recombinant Lutheran extracellular domain protein completely blocked SS RBC adhesion to laminin under both static and flow conditions. The protein kinase A inhibitor 14-22 amide inhibited adhesion to laminin during flow by high-density SS RBC from patients with strongly adherent cells but had no effect on adhesion observed after a static phase. Deletion of the cytoplasmic domain of B-CAM as well as mutation of the juxtamembranous tyrosine residue failed to reduce B-CAM-mediated adhesion to laminin by transfected MEL cells. These studies confirm that B-CAM/LU is the most critical receptor mediating adhesion to laminin under both static and flow conditions. Dense SS RBC are most adherent to laminin despite bearing fewer laminin receptors, apparently due to a reversible protein kinase A-dependent process that is unlikely to involve direct phosphorylation of B-CAM/LU. Our results also suggest that the nature of the interaction of B-CAM/LU with laminin may be different under static and flow conditions.

Authors+Show Affiliations

Division of Hematology, Department of Medicine, Duke University Medical Center and Duke Comprehensive Sickle Cell Center, Durham, North Carolina 27710, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

14755370

Citation

Zen, Qin, et al. "B-CAM/LU Expression and the Role of B-CAM/LU Activation in Binding of Low- and High-density Red Cells to Laminin in Sickle Cell Disease." American Journal of Hematology, vol. 75, no. 2, 2004, pp. 63-72.
Zen Q, Batchvarova M, Twyman CA, et al. B-CAM/LU expression and the role of B-CAM/LU activation in binding of low- and high-density red cells to laminin in sickle cell disease. Am J Hematol. 2004;75(2):63-72.
Zen, Q., Batchvarova, M., Twyman, C. A., Eyler, C. E., Qiu, H., De Castro, L. M., & Telen, M. J. (2004). B-CAM/LU expression and the role of B-CAM/LU activation in binding of low- and high-density red cells to laminin in sickle cell disease. American Journal of Hematology, 75(2), 63-72.
Zen Q, et al. B-CAM/LU Expression and the Role of B-CAM/LU Activation in Binding of Low- and High-density Red Cells to Laminin in Sickle Cell Disease. Am J Hematol. 2004;75(2):63-72. PubMed PMID: 14755370.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - B-CAM/LU expression and the role of B-CAM/LU activation in binding of low- and high-density red cells to laminin in sickle cell disease. AU - Zen,Qin, AU - Batchvarova,Milena, AU - Twyman,Christina A, AU - Eyler,Christine E, AU - Qiu,Huiling, AU - De Castro,Laura M, AU - Telen,Marilyn J, PY - 2004/2/3/pubmed PY - 2004/3/6/medline PY - 2004/2/3/entrez SP - 63 EP - 72 JF - American journal of hematology JO - Am J Hematol VL - 75 IS - 2 N2 - Red blood cells from patients with sickle cell disease (SS RBC) adhere to laminin and over-express the high-affinity laminin receptor basal cell adhesion molecule/Lutheran protein (B-CAM/LU). This receptor has recently been shown to undergo activation in vitro through a protein kinase A-dependent mechanism. Low-density SS RBC express two-thirds more B-CAM/LU than high-density SS RBC. However, high-density SS RBC have been identified as most adherent to laminin under flow conditions. We investigated the ability of low- and high-density SS RBC to interact with laminin under various conditions and explored factors that might be responsible for the differences in B-CAM/LU-laminin interaction between high- and low-density SS RBC. We confirmed that high-density SS RBC adhere to laminin more strongly than low-density SS RBC under flow conditions. However, low-density SS RBC bind soluble laminin most strongly and are the most adherent to laminin under static conditions. Soluble recombinant Lutheran extracellular domain protein completely blocked SS RBC adhesion to laminin under both static and flow conditions. The protein kinase A inhibitor 14-22 amide inhibited adhesion to laminin during flow by high-density SS RBC from patients with strongly adherent cells but had no effect on adhesion observed after a static phase. Deletion of the cytoplasmic domain of B-CAM as well as mutation of the juxtamembranous tyrosine residue failed to reduce B-CAM-mediated adhesion to laminin by transfected MEL cells. These studies confirm that B-CAM/LU is the most critical receptor mediating adhesion to laminin under both static and flow conditions. Dense SS RBC are most adherent to laminin despite bearing fewer laminin receptors, apparently due to a reversible protein kinase A-dependent process that is unlikely to involve direct phosphorylation of B-CAM/LU. Our results also suggest that the nature of the interaction of B-CAM/LU with laminin may be different under static and flow conditions. SN - 0361-8609 UR - https://www.unboundmedicine.com/medline/citation/14755370/B_CAM/LU_expression_and_the_role_of_B_CAM/LU_activation_in_binding_of_low__and_high_density_red_cells_to_laminin_in_sickle_cell_disease_ L2 - https://doi.org/10.1002/ajh.10442 DB - PRIME DP - Unbound Medicine ER -