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.

• Authors: L Howard, Y Zheng, M Horrocks, R A Maciewicz, C Blobel
• Journal: FEBS letters (FEBS Lett) Vol. 498 Issue 1 Pg. 82-6 (Jun 01 2001) ISSN: 0014-5793 [Print] England
• PMID: 11389903 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Myelin Basic Protein
• Recombinant Fusion Proteins
• ADAM Proteins
• ADAM28 protein, human
• Adam32 protein, mouse
• Metalloendopeptidases

Topics

• ADAM Proteins
• Amino Acid Sequence
• Animals
• CHO Cells
• Catalysis
• Cricetinae
• Lymphocytes (enzymology)
• Metalloendopeptidases (metabolism)
• Mice
• Molecular Sequence Data
• Myelin Basic Protein (metabolism)
• Recombinant Fusion Proteins (metabolism)
• Sperm Maturation (physiology)