Catalytic activity of ADAM28
- 30 May 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 498 (1), 82-86
- https://doi.org/10.1016/s0014-5793(01)02506-6
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.Keywords
This publication has 33 references indexed in Scilit:
- Expression and Enzymatic Activity of Human Disintegrin and Metalloproteinase ADAM19/Meltrin BetaBiochemical and Biophysical Research Communications, 2001
- ADAM 12-S Cleaves IGFBP-3 and IGFBP-5 and Is Inhibited by TIMP-3Biochemical and Biophysical Research Communications, 2000
- Biochemical Characterization of the Catalytic Domain of Human Matrix Metalloproteinase 19Journal of Biological Chemistry, 2000
- Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymisMolecular Human Reproduction, 1999
- An Essential Role for Ectodomain Shedding in Mammalian DevelopmentScience, 1998
- Evidence That Tumor Necrosis Factor α Converting Enzyme Is Involved in Regulated α-Secretase Cleavage of the Alzheimer Amyloid Protein PrecursorJournal of Biological Chemistry, 1998
- TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3FEBS Letters, 1998
- Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-αNature, 1997
- A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cellsNature, 1997
- Mutation of the Active Site Glutamic Acid of Human Gelatinase A: Effects on Latency, Catalysis, and the Binding of Tissue Inhibitor of Metalloproteinases-1Biochemistry, 1994