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An antibody that facilitates hematopoietic engraftment recognizes CD44
BM Sandmaier, R Storb, FR Appelbaum and WM Gallatin
Division of Clinical Research, Fred Hutchinson Cancer Research Center,
Seattle, WA 98104.
Pretreatment of recipients with the monoclonal antibody (MoAb) S5
facilitates engraftment of bone marrow from mismatched, unrelated donors in
the canine transplantation model. In the direct comparisons reported here,
the S5 glycoprotein (gp) was found to have structural homology to CD44 that
in humans has been implicated in adhesive interactions of one type of
effector cell, the lymphocyte. The S5 antigen and gp90Hermes-1 exhibited
codistribution on canine peripheral blood cells. Both S5 and Hermes-1
(anti-CD44) MoAbs recognized 90-Kd species in radioimmune precipitations of
125I surface-labeled canine peripheral blood lymphocytes and bone marrow
cells. Competitive antibody binding experiments showed that the epitope
detected by S5 was distinct from that bound by Hermes-1 but overlapped with
those defined by two other known anti-CD44 reagents, IM7 and Hutch-1.
Sequential immunoprecipitation with S5 and Hermes-1 indicated that the two
antibodies recognize the same or overlapping subsets of membrane gps.
Tryptic digestion of S5 and anti-CD44 immunoprecipitates generated two
major iodinated peptides of 27 and 35 Kd in both cases, a further
indication of structural homology. Similarly, after N-glycanase digestion,
S5 and CD44 immunoprecipitates were resolved to a single 68- Kd species.
These findings suggest that CD44-mediated adhesive events may affect the
fate of transplanted hematopoietic cells. The previous implications of this
gp in T-lymphocyte activation and lymphocyte adhesion to endothelium thus
provide useful paradigms to analyze its function in the bone marrow
transplant setting.
Volume 76,
Issue 3,
pp. 630-635,
08/01/1990
Copyright © 1990 by The American Society of Hematology

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