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Research Article Free access | 10.1172/JCI113936

Common acute lymphoblastic leukemia antigen expressed on leukemia and melanoma cell lines has neutral endopeptidase activity.

C V Jongeneel, E J Quackenbush, P Ronco, P Verroust, S Carrel, and M Letarte

Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland.

Find articles by Jongeneel, C. in: PubMed | Google Scholar

Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland.

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Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland.

Find articles by Ronco, P. in: PubMed | Google Scholar

Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland.

Find articles by Verroust, P. in: PubMed | Google Scholar

Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland.

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Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland.

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Published February 1, 1989 - More info

Published in Volume 83, Issue 2 on February 1, 1989
J Clin Invest. 1989;83(2):713–717. https://doi.org/10.1172/JCI113936.
© 1989 The American Society for Clinical Investigation
Published February 1, 1989 - Version history
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Abstract

We have previously reported that the amino acid sequence of the common acute lymphoblastic leukemia antigen (CALLA, CD10) translated from a normal human kidney cDNA clone is identical to that of neutral endopeptidase (NEP, EC 3.4.24.11). In this study, we show that by flow cytometry, a monoclonal antibody (135A3) produced against rabbit NEP reacted selectively with leukemia and melanoma cell lines expressing CALLA on their surface. A glycoprotein of apparent Mr 100,000 was immunoprecipitated from surface labeled NALM-1 leukemia or Mel-1477 melanoma cells with monoclonal antibodies to NEP (135A3) or CALLA (44C10). mRNAs hybridizing to a NEP-specific probe were present in CALLA+ leukemia and melanoma cell lines, but absent from CALLA- lines. NEP enzymatic activity was detected on intact cells from CALLA+ lines, but not CALLA- lines. The activity was blocked by two selective inhibitors of NEP, thiorphan and phosphoramidon. CALLA antigen purified from the NALM-6 leukemic cell line by affinity to 44C10-IgG Sepharose retained a peptidase activity that was completely blocked by thiorphan and phosphoramidon. Thus the CALLA antigen present at the surface of leukemia and melanoma cell lines is an enzymatically active neutral endopeptidase.

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