ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity

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Standard

ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity. / Lund, Jacob; Olsen, Ole H; Sørensen, Esben Skipper; Stennicke, Henning R; Petersen, Helle H; Overgaard, Michael Toft.

I: Journal of Biological Chemistry, Bind 288, Nr. 29, 19.07.2013, s. 21367-21375.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Lund, J, Olsen, OH, Sørensen, ES, Stennicke, HR, Petersen, HH & Overgaard, MT 2013, 'ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity', Journal of Biological Chemistry, bind 288, nr. 29, s. 21367-21375. https://doi.org/10.1074/jbc.M113.474536

APA

Lund, J., Olsen, O. H., Sørensen, E. S., Stennicke, H. R., Petersen, H. H., & Overgaard, M. T. (2013). ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity. Journal of Biological Chemistry, 288(29), 21367-21375. https://doi.org/10.1074/jbc.M113.474536

CBE

Lund J, Olsen OH, Sørensen ES, Stennicke HR, Petersen HH, Overgaard MT. 2013. ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity. Journal of Biological Chemistry. 288(29):21367-21375. https://doi.org/10.1074/jbc.M113.474536

MLA

Lund, Jacob o.a.. "ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity". Journal of Biological Chemistry. 2013, 288(29). 21367-21375. https://doi.org/10.1074/jbc.M113.474536

Vancouver

Lund J, Olsen OH, Sørensen ES, Stennicke HR, Petersen HH, Overgaard MT. ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity. Journal of Biological Chemistry. 2013 jul 19;288(29):21367-21375. https://doi.org/10.1074/jbc.M113.474536

Author

Lund, Jacob ; Olsen, Ole H ; Sørensen, Esben Skipper ; Stennicke, Henning R ; Petersen, Helle H ; Overgaard, Michael Toft. / ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity. I: Journal of Biological Chemistry. 2013 ; Bind 288, Nr. 29. s. 21367-21375.

Bibtex

@article{8f27430a4f984ab29cbbc56f2b508bc8,
title = "ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity",
abstract = "ADAMDEC1 (Decysin-1) is a putative ADAM (a disintegrin and metalloprotease)-like metalloprotease with an unknown physiological role, selectively expressed in mature dendritic cells and macrophages. When compared with other members of the ADAM family, ADAMDEC1 displays some unusual features. It lacks the auxiliary cysteine-rich, EGF, and transmembrane domains, as well as the cytoplasmic tail. The active site of ADAMDEC1 is unique by being the only mammalian ADAM protease with a non-histidine zinc ligand, having an aspartic acid residue instead. Here we demonstrate that ADAMDEC1, despite these unique features, functions as an active metalloprotease. Thus, ADAMDEC1 is secreted as a mature, glycosylated, and proteolytically active metalloprotease, capable of cleaving macromolecular substrates. In the recombinant form, three of the four potential N-linked glycosylation sites are modified by carbohydrate attachment. Substitution of basic residues at the predicted proprotein convertase cleavage site blocks proprotein processing, revealing both specific ADAMDEC1-dependent and specific ADAMDEC1-independent cleavage of the prodomain. The pro-form of ADAMDEC1 does not have proteolytic activity, demonstrating that the prodomain of ADAMDEC1, like in other members of the ADAM family, confers catalytic latency. Interestingly, the proteolytic activity of mature ADAMDEC1 can be significantly enhanced when a canonical ADAM active site with three zinc-coordinating histidine residues is introduced.",
author = "Jacob Lund and Olsen, {Ole H} and S{\o}rensen, {Esben Skipper} and Stennicke, {Henning R} and Petersen, {Helle H} and Overgaard, {Michael Toft}",
year = "2013",
month = jul,
day = "19",
doi = "10.1074/jbc.M113.474536",
language = "English",
volume = "288",
pages = "21367--21375",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "29",

}

RIS

TY - JOUR

T1 - ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity

AU - Lund, Jacob

AU - Olsen, Ole H

AU - Sørensen, Esben Skipper

AU - Stennicke, Henning R

AU - Petersen, Helle H

AU - Overgaard, Michael Toft

PY - 2013/7/19

Y1 - 2013/7/19

N2 - ADAMDEC1 (Decysin-1) is a putative ADAM (a disintegrin and metalloprotease)-like metalloprotease with an unknown physiological role, selectively expressed in mature dendritic cells and macrophages. When compared with other members of the ADAM family, ADAMDEC1 displays some unusual features. It lacks the auxiliary cysteine-rich, EGF, and transmembrane domains, as well as the cytoplasmic tail. The active site of ADAMDEC1 is unique by being the only mammalian ADAM protease with a non-histidine zinc ligand, having an aspartic acid residue instead. Here we demonstrate that ADAMDEC1, despite these unique features, functions as an active metalloprotease. Thus, ADAMDEC1 is secreted as a mature, glycosylated, and proteolytically active metalloprotease, capable of cleaving macromolecular substrates. In the recombinant form, three of the four potential N-linked glycosylation sites are modified by carbohydrate attachment. Substitution of basic residues at the predicted proprotein convertase cleavage site blocks proprotein processing, revealing both specific ADAMDEC1-dependent and specific ADAMDEC1-independent cleavage of the prodomain. The pro-form of ADAMDEC1 does not have proteolytic activity, demonstrating that the prodomain of ADAMDEC1, like in other members of the ADAM family, confers catalytic latency. Interestingly, the proteolytic activity of mature ADAMDEC1 can be significantly enhanced when a canonical ADAM active site with three zinc-coordinating histidine residues is introduced.

AB - ADAMDEC1 (Decysin-1) is a putative ADAM (a disintegrin and metalloprotease)-like metalloprotease with an unknown physiological role, selectively expressed in mature dendritic cells and macrophages. When compared with other members of the ADAM family, ADAMDEC1 displays some unusual features. It lacks the auxiliary cysteine-rich, EGF, and transmembrane domains, as well as the cytoplasmic tail. The active site of ADAMDEC1 is unique by being the only mammalian ADAM protease with a non-histidine zinc ligand, having an aspartic acid residue instead. Here we demonstrate that ADAMDEC1, despite these unique features, functions as an active metalloprotease. Thus, ADAMDEC1 is secreted as a mature, glycosylated, and proteolytically active metalloprotease, capable of cleaving macromolecular substrates. In the recombinant form, three of the four potential N-linked glycosylation sites are modified by carbohydrate attachment. Substitution of basic residues at the predicted proprotein convertase cleavage site blocks proprotein processing, revealing both specific ADAMDEC1-dependent and specific ADAMDEC1-independent cleavage of the prodomain. The pro-form of ADAMDEC1 does not have proteolytic activity, demonstrating that the prodomain of ADAMDEC1, like in other members of the ADAM family, confers catalytic latency. Interestingly, the proteolytic activity of mature ADAMDEC1 can be significantly enhanced when a canonical ADAM active site with three zinc-coordinating histidine residues is introduced.

U2 - 10.1074/jbc.M113.474536

DO - 10.1074/jbc.M113.474536

M3 - Journal article

C2 - 23754285

VL - 288

SP - 21367

EP - 21375

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 29

ER -