Catalytic activity of ADAM28 Journal Article
| Authors: | Howard, L.; Zheng, Y.; Horrocks, M.; Maciewicz, R. A.; Blobel, C. |
| Article Title: | Catalytic activity of ADAM28 |
| Abstract: | 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. © 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Societies. |
| Keywords: | controlled study; protein expression; unclassified drug; mutation; nonhuman; myelin basic protein; animal cell; animals; mice; protein degradation; protein; enzyme activity; recombinant enzyme; amino acid sequence; molecular sequence data; recombinant fusion proteins; nucleotide sequence; proteinase; catalysis; epididymis; lymphocytes; lymphocyte function; metalloproteinase; adam proteins; tissue inhibitor of metalloproteinase 1; tissue inhibitor of metalloproteinase 2; enzyme active site; cho cells; cricetinae; myelin basic proteins; spermatozoon maturation; adam; metalloendopeptidases; female; priority journal; article; metalloprotease disintegrin; adam 28 proteinase; sperm maturation |
| Journal Title: | FEBS Letters |
| Volume: | 498 |
| Issue: | 1 |
| ISSN: | 0014-5793 |
| Publisher: | Wiley Blackwell |
| Date Published: | 2001-06-01 |
| Start Page: | 82 |
| End Page: | 86 |
| Language: | English |
| DOI: | 10.1016/s0014-5793(01)02506-6 |
| PUBMED: | 11389903 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 21 May 2015 -- Source: Scopus |
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