Rehli, M. and Krause, S. W. and Kreutz, M. and Andreesen, Reinhard (1995) Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation. The Journal of biological chemistry 270 (26), pp. 15644-9.
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The two monoclonal antibodies MAX.1 and MAX.11 recognize cell surface antigens that are almost undetectable on monocytes but highly expressed on differentiated macrophages. Biochemical characterization revealed that both antibodies detect the same 58-64-kDa glycoprotein anchored to the plasma membrane by glycosyl-phosphatidylinositol linkage. We purified the MAX.1/11 antigen by immunoaffinity chromatography using monoclonal antibody MAX.11. The NH2-terminal amino acid sequence was determined and turned out to be identical to the NH2-terminal sequence of the membrane-bound carboxypeptidase M. By precipitation with antibodies MAX.1 and MAX.11, membrane preparations of macrophages and placental microvilli were almost completely depleted of enzyme activity, indicating that the two antibodies indeed recognize carboxypeptidase M. Immunoreactivity of both antibodies correlates with the reported tissue distribution of enzyme activity. Expression of carboxypeptidase M on mRNA level and enzymatic activity markedly increase during in vitro differentiation of monocytes, according to the described increase in MAX.1 and MAX.11 antigen expression. Moreover, in vitro differentiated macrophages show the highest specific activity yet described in any tissue. In addition, carboxypeptidase M expression could be detected in HL-60, U937, and THP-1 myeloid cell lines. Vitamin D3-induced monocytic differentiation resulted in an increased carboxypeptidase M expression in all three cell lines. Further studies are needed to elucidate the functional role of carboxypeptidase M during monocytic differentiation and activation.
|Institutions:||Medicine > Abteilung für Hämatologie und Internistische Onkologie|
|Subjects:||600 Technology > 610 Medical sciences Medicine|
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||Yes|
|Deposited On:||14 Apr 2010 05:04|
|Last Modified:||14 Apr 2010 05:04|