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Catalytic activity of ADAM28
Author(s) -
Howard Linda,
Zheng Yufang,
Horrocks Maureen,
Maciewicz Rose A.,
Blobel Carl
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02506-6
Subject(s) - disintegrin , metalloproteinase , glycoprotein , recombinant dna , chemistry , glycosylation , biology , biochemistry , microbiology and biotechnology , enzyme , gene
ADAMs are membrane‐anchored glycoproteins containing a disintegrin and metalloprotease domain that have important roles in fertilization, development, and diseases such as Alzheimer's dementia. Here we present the first evidence for catalytic activity of ADAM28, a protein that is highly expressed in the epididymis and lymphocytes. Recombinant ADAM28 cleaves myelin basic protein at two sites. The catalytic activity of ADAM28 is not sensitive to tissue inhibitors of metalloproteases 1 and 2, but can be abolished by a mutation in the catalytic site. Catalytically active ADAM28 will be valuable for further studies of its role in sperm maturation and lymphocyte function.