| First Author | Rebbe NF | Year | 1993 |
| Journal | Mol Immunol | Volume | 30 |
| Issue | 1 | Pages | 87-93 |
| PubMed ID | 7678057 | Mgi Jnum | J:3344 |
| Mgi Id | MGI:51857 | Doi | 10.1016/0161-5890(93)90429-f |
| Citation | Rebbe NF, et al. (1993) Expression of nucleotide pyrophosphatase and alkaline phosphodiesterase I activities of PC-1, the murine plasma cell antigen. Mol Immunol 30(1):87-93 |
| abstractText | 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 115 kDa 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. |
