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PMID: 2521388 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Common acute lymphoblastic leukemia antigen (CALLA) is active neutral endopeptidase 24.11 ("enkephalinase"): direct evidence by cDNA transfection analysis.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 86 ·No. 1 ·1989-01-00 ·Pages 297-301

Shipp MA, Vijayaraghavan J, Schmidt EV, Masteller EL, D'Adamio L, Hersh LB, Reinherz EL

Abstract

The common acute lymphoblastic leukemia antigen (CALLA) is a 749-amino acid type II integral membrane protein expressed by most acute lymphoblastic leukemias, certain other lymphoid malignancies with an immature phenotype, and normal lymphoid progenitors. A computer search against the most recent GenBank release (no. 56) indicates that human CALLA cDNA encodes a protein nearly identical to the rat and rabbit neutral endopeptidase 24.11 ("enkephalinase;" EC 3.4.24.11). This zinc metalloendopeptidase, which has been shown to inactivate a variety of peptide hormones including enkephalin, chemotactic peptide, substance P, neurotensin, oxytocin, bradykinin, and angiotensins I and II, had not been identified in lymphoid cells. To determine whether CALLA cDNA derived from human acute lymphoblastic leukemia cells (Nalm-6 cell line) encodes functional neutral endopeptidase activity, we generated CALLA+ stable transfectants in the CALLA- murine myeloma cell line J558 and analyzed them for enzymatic activity in a fluorometric assay based upon cleavage of the substrate glutaryl-Ala-Ala-Phe 4-methoxy-2-naphthylamide at the Ala-Phe bond. Total lysates as well as whole-cell suspensions of the Nalm-6 line and of the CALLA+ transfectants, but not of the CALLA- J558 cells, possessed neutral endopeptidase activity. This enzymatic activity was associated with the cellular membrane fraction and was abrogated by the specific neutral endopeptidase inhibitor phosphoramidon. The unequivocal identification of CALLA as a functional neutral endopeptidase provides insight into its potential role in both normal and malignant lymphoid function.

MeSH Terms
Animals Antigens, Differentiation/genetics Antigens, Neoplasm/genetics Cell Line DNA, Neoplasm/genetics Glycopeptides/pharmacology Humans Mice Neprilysin/antagonists & inhibitors,genetics,metabolism Precursor Cell Lymphoblastic Leukemia-Lymphoma/enzymology,immunology Restriction Mapping Transfection
Chemicals
Antigens, Differentiation Antigens, Neoplasm DNA, Neoplasm Glycopeptides Neprilysin phosphoramidon
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Shipp M A
Dana-Farber Cancer Institute, Department of Medicine, Boston, MA.
Vijayaraghavan J
Schmidt E V
Masteller E L
D'Adamio L
Hersh L B
Reinherz E L
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.86.1.297
Published
1989-01-00
Pages
297-301
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC286451
Subset
IM
Grants
NIDA NIH HHS · DA02243 · United States
NCI NIH HHS · KO8 CA01057 · United States
NCI NIH HHS · R01 CA49232 · United States
External Links
PubMed source DOI: 10.1073/pnas.86.1.297 PMC Full Text View journal details
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