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ADAM (a disintegrin and metalloprotease) 12 is expressed in rat and human brain and localized to oligodendrocytes
Author(s) -
Bernstein HansGert,
Keilhoff Gerburg,
Bukowska Alicja,
Ziegeler Anke,
Funke Sieglinde,
Dobrowolny Henrik,
Kanakis Dimitrios,
Bogerts Bernhard,
Lendeckel Uwe
Publication year - 2003
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.10858
Subject(s) - disintegrin , metalloproteinase , reverse transcriptase , immunohistochemistry , biology , mesenchymal stem cell , microbiology and biotechnology , protease , pathology , cell type , cell , matrix metalloproteinase , polymerase chain reaction , immunology , medicine , enzyme , gene , biochemistry
ADAM12 is a member of the large family of multidomain metalloprotease‐disintegrins which possess cell‐binding and metalloprotease properties. Typically, ADAM12 is expressed in mesenchymal cells, developing and regenerating heart and skeletal muscle, bone as well as in certain tumours. This report shows by means of reverse transcriptase‐polymerase chain reaction (RT‐PCR) and immunohistochemistry that the protease ADAM12 is detectable in human and rat brain tissue as well as in cultured cells derived from rat brain. With the exception of a very few immunopositive pyramidal neurons in the developing rat brain, the cellular localization of ADAM12 was exclusively confined to oligodendroglial cells. Thus, ADAM12 may be regarded a new suitable marker for this cell type. © 2003 Wiley‐Liss, Inc.