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Type: Journal article
Title: Primitive human haemopoietic progenitors adhere to P-selectin (CD62P)
Author: Zannettino, A.
Berndt, M.
Nuitta, S.
Butcher, C.
Vadas, M.
Simmons, P.
Citation: Blood, 1995; 85(12):3466-3477
Publisher: Grune and Stratton
Issue Date: 1995
ISSN: 0006-4971
Statement of
AC Zannettino, MC Berndt, C Butcher, EC Butcher, MA Vadas, and PJ Simmons
Abstract: P-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.
Keywords: Bone Marrow Cells
Hematopoietic Stem Cells
Bone Marrow
Platelet Membrane Glycoproteins
Antigens, CD
Antigens, CD34
Polymerase Chain Reaction
Cell Adhesion
Base Sequence
Molecular Sequence Data
DOI: 10.1182/blood.v85.12.3466.bloodjournal85123466
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Appears in Collections:Aurora harvest 2
Microbiology and Immunology publications

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