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Complex Pattern of Membrane Type 1 Matrix Metalloproteinase Shedding

Toth, Marta, Hernandez-Barrantes, Sonia, Osenkowski, Pamela, Bernardo, M. Margarida, Gervasi, David C., Shimura, Yoichiro, Meroueh, Oussama, Kotra, Lakshmi P., Gálvez, Beatriz G., Arroyo, Alicia G., Mobashery, Shahriar, Fridman, Rafael·2002·Journal of Biological Chemistry
DOI 10.1074/jbc.m200655200
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Abstract

Membrane type 1 matrix metalloproteinase (MT1-MMP) is a type I transmembrane MMP shown to play a critical role in normal development and in malignant processes. Emerging evidence indicates that MT1-MMP is regulated by a process of ectodomain shedding. Active MT1-MMP undergoes autocatalytic processing on the cell surface, leading to the formation of an inactive 44-kDa fragment and release of the entire catalytic domain. Analysis of the released MT1-MMP forms in various cell types revealed a complex pattern of shedding involving two major fragments of 50 and 18 kDa and two minor species of 56 and 31-35 kDa. Protease inhibitor studies and a catalytically inactive MT1-MMP mutant revealed both autocatalytic (18 kDa) and non-autocatalytic (56, 50, and 31-35 kDa) shedding mechanisms. Purification and sequencing of the 18-kDa fragment indicated that it extends from Tyr(112) to Ala(255). Structural and sequencing data indicate that shedding of the 18-kDa fragment is initiated at the Gly(284)-Gly(285) site, followed by cleavage between the conserved Ala(255) and Ile(256) residues near the conserved methionine turn, a structural feature of the catalytic domain of all MMPs. Consistently, a recombinant 18-kDa fragment had no catalytic activity and did not bind TIMP-2. Thus, autocatalytic shedding evolved as a specific mechanism to terminate MT1-MMP activity on the cell surface by disrupting enzyme integrity at a vital structural site. In contrast, functional data suggest that the non-auto…

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  • MT1-MMP is constitutively shed via proteolytic cleavage by ADAM family metalloproteinases, resulting in detectable quantities of soluble MT1-MMP (sMT1-MMP) in the plasma.

    “MT1-MMP is constitutively shed via proteolytic cleavage by A Disintegrin and Metalloproteinase (ADAM) family metalloproteinases, resulting in detectable quantities of soluble MT1-MMP (sMT1-MMP) in the plasma20–22.”

    From MT1-MMP inhibition rejuvenates ageing brain and rescues cognitive deficits in obesity (2025) · cites this paper as [20]

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Metadata

Authors
Toth, M., Hernandez-Barrantes, S., Osenkowski, P., Bernardo, M. M., Gervasi, D. C., Shimura, Y., Meroueh, O., Kotra, L. P., Gálvez, B. G., Arroyo, A. G., Mobashery, S., & Fridman, R.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2002-07
Volume
277
Issue
29
Pages
26340-26350
ISSN
0021-9258
DOI
10.1074/jbc.m200655200
Cited by
119
References
0
Language
en
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