Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain

Amanda J. Fosang; Karena Last; Yutaka Fujii; Motoharu Seiki; Yasunori Okada

doi:10.1016/S0014-5793(98)00667-X

Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain

Amanda J. Fosang, Karena Last, Yutaka Fujii, Motoharu Seiki, Yasunori Okada

Research output: Contribution to journal › Article › peer-review

54 Citations (Scopus)

Abstract

An aggrecan G1-G2 substrate was used to determine sites within the interglobular domain that were susceptible to cleavage by MT1-MMP. Degradation products were identified by Western blotting with neo-epitope antibodies specific for MMP-derived N- and C-terminal sequences. The results showed that MT1-MMP cleaved at the N₃₄₁-F₃₄₂ and D₄₄₁-L₄₄₂ bonds, as shown for other MMPs, and also at a site 13 amino acids C-terminal to the N₃₄₁-F₃₄₂ site. The G2 product of this additional cleavage was identified by sequence analysis and revealed an N-terminus commencing T₃₅₅ VxxPDVELPLP. The data are consistent with MT1-MMP cleavage at three sites in the aggrecan interglobular domain; one at N₃₄₂-F₃₄₂, a second at D₄₄₁-L₄₄₂ and a third at Q₃₅₄-T₃₅₅.

Original language	English
Pages (from-to)	186-190
Number of pages	5
Journal	FEBS Letters
Volume	430
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(98)00667-X
Publication status	Published - 1998 Jul 3
Externally published	Yes

Keywords

Aggrecan
Arthritis
Matrix metalloproteinase
Membrane-type matrix metalloproteinase
Neo-epitope

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(98)00667-X

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title = "Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain",

abstract = "An aggrecan G1-G2 substrate was used to determine sites within the interglobular domain that were susceptible to cleavage by MT1-MMP. Degradation products were identified by Western blotting with neo-epitope antibodies specific for MMP-derived N- and C-terminal sequences. The results showed that MT1-MMP cleaved at the N341-F342 and D441-L442 bonds, as shown for other MMPs, and also at a site 13 amino acids C-terminal to the N341-F342 site. The G2 product of this additional cleavage was identified by sequence analysis and revealed an N-terminus commencing T355 VxxPDVELPLP. The data are consistent with MT1-MMP cleavage at three sites in the aggrecan interglobular domain; one at N342-F342, a second at D441-L442 and a third at Q354-T355.",

keywords = "Aggrecan, Arthritis, Matrix metalloproteinase, Membrane-type matrix metalloproteinase, Neo-epitope",

author = "Fosang, {Amanda J.} and Karena Last and Yutaka Fujii and Motoharu Seiki and Yasunori Okada",

note = "Funding Information: The authors are grateful to Prof. G. Murphy (Norwich) for providing proMMP2 and to Dr. C. Hughes and Prof. B. Caterson (Cardiff) for providing BC-3 monoclonal antibody. We acknowledge the National Health and Medical Research Council (Australia) and the Arthritis Foundation of Australia for financial support, and Grants-in-Aid (1047005 and 10877231) from the Ministry of Education, Science and Culture of Japan to Y.O.",

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AU - Fosang, Amanda J.

AU - Last, Karena

AU - Fujii, Yutaka

AU - Seiki, Motoharu

AU - Okada, Yasunori

N1 - Funding Information: The authors are grateful to Prof. G. Murphy (Norwich) for providing proMMP2 and to Dr. C. Hughes and Prof. B. Caterson (Cardiff) for providing BC-3 monoclonal antibody. We acknowledge the National Health and Medical Research Council (Australia) and the Arthritis Foundation of Australia for financial support, and Grants-in-Aid (1047005 and 10877231) from the Ministry of Education, Science and Culture of Japan to Y.O.

PY - 1998/7/3

Y1 - 1998/7/3

N2 - An aggrecan G1-G2 substrate was used to determine sites within the interglobular domain that were susceptible to cleavage by MT1-MMP. Degradation products were identified by Western blotting with neo-epitope antibodies specific for MMP-derived N- and C-terminal sequences. The results showed that MT1-MMP cleaved at the N341-F342 and D441-L442 bonds, as shown for other MMPs, and also at a site 13 amino acids C-terminal to the N341-F342 site. The G2 product of this additional cleavage was identified by sequence analysis and revealed an N-terminus commencing T355 VxxPDVELPLP. The data are consistent with MT1-MMP cleavage at three sites in the aggrecan interglobular domain; one at N342-F342, a second at D441-L442 and a third at Q354-T355.

AB - An aggrecan G1-G2 substrate was used to determine sites within the interglobular domain that were susceptible to cleavage by MT1-MMP. Degradation products were identified by Western blotting with neo-epitope antibodies specific for MMP-derived N- and C-terminal sequences. The results showed that MT1-MMP cleaved at the N341-F342 and D441-L442 bonds, as shown for other MMPs, and also at a site 13 amino acids C-terminal to the N341-F342 site. The G2 product of this additional cleavage was identified by sequence analysis and revealed an N-terminus commencing T355 VxxPDVELPLP. The data are consistent with MT1-MMP cleavage at three sites in the aggrecan interglobular domain; one at N342-F342, a second at D441-L442 and a third at Q354-T355.

KW - Aggrecan

KW - Arthritis

KW - Matrix metalloproteinase

KW - Membrane-type matrix metalloproteinase

KW - Neo-epitope

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Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain

Abstract

Keywords

ASJC Scopus subject areas

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