Expression of nucleotide pyrophosphatase and alkaline phosphodiesterase I activities of PC-1, the murine plasma cell antigen

Neil F. Rebbe, Benton D. Tong, Scot Hickman

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

Nucleotide pyrophosphatase (EC 3.6.1.9) is a membrane enzyme purified from a number of mammalian sources that may have alkaline phosphodiesterase I (EC 3.1.4.1) activity as well. The mol. wt and subunit structure of this membrane glycoprotein are similar to that of the murine plasma cell alloantigen, PC-1. The PC-1 protein is a disulfide-bonded dimer of identical 115kDa polypeptides that is selectively expressed on B lineage cells that have reached the degree of maturation associated with immunoglobulin secretion. It also has restricted expression in certain non-lymphoid tissues. In this report, we show that alkaline phosphodiesterase I activity parallels PC-1 mRNA expression in a number of B lineage cell lines at different stages of differentiation. Furthermore, we demonstrate increases in both nucleotide pyrophosphatase and alkaline phosphodiesterase I enzymatic activities in transiently transfected COS-7 cells expressing a cloned PC-1 cDNA construction. These results extend our previous immunological and correlative studies and directly ascribe an enzymatic activity to this cell surface differentiation antigen. These experiments also demonstrate that a single protein is responsible for both alkaline phosphodiesterase I and nucleotide pyrophosphatase activities.

Original languageEnglish
Pages (from-to)87-93
Number of pages7
JournalMolecular Immunology
Volume30
Issue number1
DOIs
StatePublished - Jan 1993

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