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The peanut‐agglutinin (PNA)‐binding surface components of malignant plasma cells
Author(s) -
Slupsky Joseph R.,
DugganKeen Margaret,
Booth Laurence A.,
Karpas Abraham,
Rhodes Elizabeth G. H.,
Cawley John C.,
Zuzel Mirko
Publication year - 1993
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1993.tb04692.x
Subject(s) - peanut agglutinin , agglutinin , chemistry , biochemistry , lectin
Summary. Plasma cells within bone marrow aspirates from multiple myeloma patients have been shown to be reactive with the lectin peanut agglutinin (PNA). This has been recently exploited by using PNA for purging bone marrow of malignant cells in autotransplantation therapy of the disease. The purpose of this investigation was to isolate and characterize the PNA‐binding proteins of myeloma cells. We used the malignant plasma cell‐derived line Karpas‐620 (K620) as a model, and showed by affinity chromatography, SDS‐PAGE, and immunoprecipitation that, among several PNA‐binding proteins, a major one is an incompletely sialylated form of CD44. CD44 is a well‐known homing receptor protein which is rich in carbohydrate and usually completely sialylated so that it does not react with PNA. We have then examined the PNA reactivity of myeloma cells from different patients and showed a clear difference in the profile of PNA‐binding proteins from case to case. Moreover, in contrast to K620 cells, some of the patient plasma cells tested did not have a PNA‐binding form of CD44. In conclusion, therefore, we have shown that a number of different proteins participate in PNA binding by malignant plasma cells. Moreover, we have demonstrated a novel, incompletely sialylated form of CD44 on a myeloma cell line. It is known that the level of glycosylation of CD44 and other proteins may affect their function, but how this relates to the malignant behaviour of plasma cells remains to be determined.