|
|
||||||||
The Journal of Immunology, Vol 136, Issue 7 2709-2714, Copyright © 1986 by American Association of Immunologists
ARTICLES |
JM Pesando, P Hoffman and T Conrad
Monoclonal antibodies (MoAb) to a leukemia-associated p24 cell surface antigen are currently being used to purge bone marrow of malignant cells before autologous transplantation for acute lymphoblastic leukemia (ALL). Their use as potential diagnostic reagents for hematologic disorders is also under investigation. It has been assumed throughout these investigations that the p24-specific MoAb produced by different laboratories all identify the same antigen. Our present studies indicate that at least two populations of p24 antigens, having different chemical properties and cellular distributions, exist on malignant B cells. For example, eight MoAb raised to ALL cells (ALL- MoAb) identify a p24 antigen on these cells but do not react with the Burkitt's lymphoma cell line Ramos. In contrast, six MoAb raised to Ramos (Ramos-MoAb) identify a p24 antigen on both Ramos and ALL cells. Quantitative binding of both sets of MoAb to ALL cells is comparable. The ALL-MoAb react with platelets, granulocytes, and activated but not resting T lymphocytes, whereas the Ramos-MoAb react with both resting and activated T lymphocytes but not with platelets or granulocytes. The ALL-MoAb react with 11 of 34 human hematopoietic cell lines tested; the Ramos-MoAb react with all 34. Both sets of MoAb react with most of the nonhematopoietic human cell lines tested. Reciprocal exhaustive radioimmune precipitation experiments performed with an ALL cell line indicate that the antigenic determinants recognized by these two sets of MoAb are present on different molecules. Similarly, proteolytic digests of iodinated antigens identified by these two sets of MoAb on ALL cells confirm the unique chemical identities of these molecules and suggest that they reflect the products of different genetic loci. The presence of the antigen identified by the Ramos-MoAb on every cell population tested except granulocytes suggests that it may serve an important cellular function. The existence of two populations of p24 antigens on at least some hematopoietic cells indicates the need for caution when comparing the results of studies of these antigens by groups employing different MoAb.
This article has been cited by other articles:
![]() |
K. D. Little, M. E. Hemler, and C. S. Stipp Dynamic Regulation of a GPCR-Tetraspanin-G Protein Complex on Intact Cells: Central Role of CD81 in Facilitating GPR56-G{alpha}q/11 Association Mol. Biol. Cell, May 1, 2004; 15(5): 2375 - 2387. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. V. Kolesnikova, C. S. Stipp, R. M. Rao, W. S. Lane, F. W. Luscinskas, and M. E. Hemler EWI-2 modulates lymphocyte integrin {alpha}4{beta}1 functions Blood, April 15, 2004; 103(8): 3013 - 3019. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. R. Kazarov, X. Yang, C. S. Stipp, B. Sehgal, and M. E. Hemler An extracellular site on tetraspanin CD151 determines {alpha}3 and {alpha}6 integrin-dependent cellular morphology J. Cell Biol., September 29, 2002; 158(7): 1299 - 1309. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. S. Stipp, D. Orlicky, and M. E. Hemler FPRP, a Major, Highly Stoichiometric, Highly Specific CD81- and CD9-associated Protein J. Biol. Chem., February 9, 2001; 276(7): 4853 - 4862. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. S. Stipp, T. V. Kolesnikova, and M. E. Hemler EWI-2 Is a Major CD9 and CD81 Partner and Member of a Novel Ig Protein Subfamily J. Biol. Chem., October 26, 2001; 276(44): 40545 - 40554. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |