Linked Life Data

7797563

Source:http://linkedlifedata.com/resource/pubmed/id/7797563

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
1995-8-1
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15644-9
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation.
pubmed:affiliation
Department of Hematology and Oncology, University of Regensburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't