## Abstract ## Background and Objectives A disintegrin and metalloprotease 12 (ADAM12) has multiple domains and functions, and it plays important roles in the development of cancer. We conducted a retrospective study to determine whether the expression of the membrane type of ADAM12 (ADAM12‐L) cou
ADAM (a disintegrin and metalloprotease) 12 is expressed in rat and human brain and localized to oligodendrocytes
✍ Scribed by Hans-Gert Bernstein; Gerburg Keilhoff; Alicja Bukowska; Anke Ziegeler; Sieglinde Funke; Henrik Dobrowolny; Dimitrios Kanakis; Bernhard Bogerts; Uwe Lendeckel
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 499 KB
- Volume
- 75
- Category
- Article
- ISSN
- 0360-4012
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✦ Synopsis
Abstract
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.
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