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dc.contributor.authorZannettino, A.-
dc.contributor.authorBerndt, M.-
dc.contributor.authorNuitta, S.-
dc.contributor.authorButcher, C.-
dc.contributor.authorVadas, M.-
dc.contributor.authorSimmons, P.-
dc.identifier.citationBlood, 1995; 85(12):3466-3477-
dc.description.abstractP-selectin was shown to bind committed human hematopoietic progenitors (colony-forming unit-granulocyte-macrophage [CFU-GM] and burst-forming unit-erythroid [BFU-E]) as identified by their expression of the CD34 antigen and by in vitro clonogenic assays. In addition, P-selectin bound all precursors (pre-CFU) of committed myeloid progenitors assayed by their ability to sustain hematopoiesis in both conventional stroma-containing and stroma-free, cytokine-dependent systems. Binding of CD34+ cells to P-selectin was temperature-independent and shear-resistant, occurred only in the presence of divalent cations, was protease sensitive, and was completely blocked by anti-P-selectin antibody. Neuraminidase treatment of CD34+ cells completely abrogated their binding to P-selectin, implying a prominent role for sialic acid in the structure and function of the P-selectin ligand on hematopoietic progenitors. Monoclonal antibodies (MoAbs) CSLEX-1 and HECA-452, which identify carbohydrate epitopes involving sialic acid, bound to 33% and 35% of CD34+ cells, respectively, and included the majority of CFU-GM and pre-CFU. Three-color flow cytometric analysis showed a precise codistribution of CSLEX-1 and HECA-452 antigens on CD34+ cells, implying recognition of the same glycoprotein antigen by the two MoAbs. Treatment of CD34+ cells with neuraminidase completely abolished binding of both MoAbs. In addition, HECA-452 partially blocked the adhesion of CD34+ cells to P-selectin. P-selectin glycoprotein ligand (PSGL-1), recently molecularly cloned from the promyelocytic leukemia cell line HL60, was expressed by CD34+ cells as determined by reverse transcription polymerase chain reaction. Combined with the functional and biochemical characteristics, these data suggest that PSGL-1 may comprise an important P-selectin ligand expressed by primitive hematopoietic cells, but do not preclude the existence of additional P-selectin ligands on these cells.-
dc.description.statementofresponsibilityAC Zannettino, MC Berndt, C Butcher, EC Butcher, MA Vadas, and PJ Simmons-
dc.publisherGrune and Stratton-
dc.subjectBone Marrow Cells-
dc.subjectHematopoietic Stem Cells-
dc.subjectBone Marrow-
dc.subjectPlatelet Membrane Glycoproteins-
dc.subjectAntigens, CD-
dc.subjectAntigens, CD34-
dc.subjectPolymerase Chain Reaction-
dc.subjectCell Adhesion-
dc.subjectBase Sequence-
dc.subjectMolecular Sequence Data-
dc.titlePrimitive human haemopoietic progenitors adhere to P-selectin (CD62P)-
dc.typeJournal article-
dc.identifier.orcidZannettino, A. [0000-0002-6646-6167]-
Appears in Collections:Aurora harvest 2
Microbiology and Immunology publications

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