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The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition.

Rapti, Magdalini, Atkinson, Susan J., Lee, Meng-Huee, Trim, Andrew, Moss, Marcia, Murphy, Gillian·2008·Biochemical Journal
DOI 10.1042/bj20071430
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Abstract

ADAM (a disintegrin and metalloproteinase) 10 is a key member of the ADAM family of disintegrin and metalloproteinases which process membrane-associated proteins to soluble forms in a process known as ‘shedding’. Among the major targets of ADAM10 are Notch, EphrinA2 and CD44. In many cell-based studies of shedding, the activity of ADAM10 appears to overlap with that of ADAM17, which has a similar active-site topology relative to the other proteolytically active ADAMs. The tissue inhibitors of metalloproteinases, TIMPs, have proved useful in the study of ADAM function, since TIMP-1 inhibits ADAM10, but not ADAM17; however, both enzymes are inhibited by TIMP-3. In the present study, we show that, in comparison with ADAM17 and the MMPs (matrix metalloproteinases), the N-terminal domains of TIMPs alone are insufficient for the inhibition of ADAM10. This knowledge could form the basis for the design of directed inhibitors against different metalloproteinases.

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Research works printed but not linked: 32

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Metadata

Authors
Rapti, M., Atkinson, S. J., Lee, M.-H., Trim, A., Moss, M., & Murphy, G.
Affiliations
  • Department of Oncology, Cambridge University, Cancer Research UK Cambridge Research Institute, Li Ka Shing Centre, Cambridge CB2 0RE, U.K.
  • Department of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, U.K.
  • Biozyme Inc., Apex, NC 7523, U.S.A.
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
2008-03-27
Volume
411
Issue
2
Pages
433-439
ISSN
  • 0264-6021
  • 1470-8728
DOI
10.1042/bj20071430
Cited by
43
References
0
Language
en

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