Institut for Biomedicin

Thomas Vorup-Jensen

Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin αXβ 2

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

Standard

Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin αXβ 2. / Vorup-Jensen, Thomas; Carman, Christopher V.; Shimaoka, Motomu; Schuck, Peter; Svitel, Juraj; Springer, Timothy A.

I: Proceedings of the National Academy of Sciences of the United States of America, Bind 102, Nr. 5, 01.02.2005, s. 1614-1619.

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

Harvard

Vorup-Jensen, T, Carman, CV, Shimaoka, M, Schuck, P, Svitel, J & Springer, TA 2005, 'Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin αXβ 2', Proceedings of the National Academy of Sciences of the United States of America, bind 102, nr. 5, s. 1614-1619. https://doi.org/10.1073/pnas.0409057102

APA

Vorup-Jensen, T., Carman, C. V., Shimaoka, M., Schuck, P., Svitel, J., & Springer, T. A. (2005). Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin αXβ 2. Proceedings of the National Academy of Sciences of the United States of America, 102(5), 1614-1619. https://doi.org/10.1073/pnas.0409057102

CBE

Vorup-Jensen T, Carman CV, Shimaoka M, Schuck P, Svitel J, Springer TA. 2005. Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin αXβ 2. Proceedings of the National Academy of Sciences of the United States of America. 102(5):1614-1619. https://doi.org/10.1073/pnas.0409057102

MLA

Vancouver

Vorup-Jensen T, Carman CV, Shimaoka M, Schuck P, Svitel J, Springer TA. Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin αXβ 2. Proceedings of the National Academy of Sciences of the United States of America. 2005 feb 1;102(5):1614-1619. https://doi.org/10.1073/pnas.0409057102

Author

Vorup-Jensen, Thomas ; Carman, Christopher V. ; Shimaoka, Motomu ; Schuck, Peter ; Svitel, Juraj ; Springer, Timothy A. / Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin αXβ 2. I: Proceedings of the National Academy of Sciences of the United States of America. 2005 ; Bind 102, Nr. 5. s. 1614-1619.

Bibtex

@article{2a1b5bf298764be88b8dc95308282eb6,
title = "Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin αXβ 2",
abstract = "The structural integrity of tissue proteins is damaged in processes ranging from remodeling of the extracellular matrix to destruction by microbial pathogens. Leukocytes play a prominent role in tissue surveillance and repair. However, it remains enigmatic what features of structurally decayed proteins prompt recognition by leukocyte cell-surface receptors. Here, we report that adhesion of human neutrophil granulocytes to fibrinogen is greatly increased by plasmin digestion in a mode where αXβ2 dominates the integrin-dependent binding. The bacterial protease subtilisin also enhances binding by αXβ2. The αX ligand binding domain has an unusually high affinity for carboxyl groups, with KD at ≈ 100 μM. Our findings implicate enhanced accessibility of negatively charged residues in structurally decayed proteins as a pattern recognition motif for αXβ 2 integrin. Comparisons among integrins show relevance of these findings to the large number of ligands recognized by αMβ 2 and αXβ2 but not αLβ2. The observations suggest that the pericellular proteolysis at the leading edge of neutrophils not only facilitates passage through the extracellular matrix but also manufactures binding sites for αXβ2.",
keywords = "Plasmin, Scavenger receptor",
author = "Thomas Vorup-Jensen and Carman, {Christopher V.} and Motomu Shimaoka and Peter Schuck and Juraj Svitel and Springer, {Timothy A.}",
year = "2005",
month = "2",
day = "1",
doi = "10.1073/pnas.0409057102",
language = "English",
volume = "102",
pages = "1614--1619",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "5",

}

RIS

TY - JOUR

T1 - Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin αXβ 2

AU - Vorup-Jensen, Thomas

AU - Carman, Christopher V.

AU - Shimaoka, Motomu

AU - Schuck, Peter

AU - Svitel, Juraj

AU - Springer, Timothy A.

PY - 2005/2/1

Y1 - 2005/2/1

N2 - The structural integrity of tissue proteins is damaged in processes ranging from remodeling of the extracellular matrix to destruction by microbial pathogens. Leukocytes play a prominent role in tissue surveillance and repair. However, it remains enigmatic what features of structurally decayed proteins prompt recognition by leukocyte cell-surface receptors. Here, we report that adhesion of human neutrophil granulocytes to fibrinogen is greatly increased by plasmin digestion in a mode where αXβ2 dominates the integrin-dependent binding. The bacterial protease subtilisin also enhances binding by αXβ2. The αX ligand binding domain has an unusually high affinity for carboxyl groups, with KD at ≈ 100 μM. Our findings implicate enhanced accessibility of negatively charged residues in structurally decayed proteins as a pattern recognition motif for αXβ 2 integrin. Comparisons among integrins show relevance of these findings to the large number of ligands recognized by αMβ 2 and αXβ2 but not αLβ2. The observations suggest that the pericellular proteolysis at the leading edge of neutrophils not only facilitates passage through the extracellular matrix but also manufactures binding sites for αXβ2.

AB - The structural integrity of tissue proteins is damaged in processes ranging from remodeling of the extracellular matrix to destruction by microbial pathogens. Leukocytes play a prominent role in tissue surveillance and repair. However, it remains enigmatic what features of structurally decayed proteins prompt recognition by leukocyte cell-surface receptors. Here, we report that adhesion of human neutrophil granulocytes to fibrinogen is greatly increased by plasmin digestion in a mode where αXβ2 dominates the integrin-dependent binding. The bacterial protease subtilisin also enhances binding by αXβ2. The αX ligand binding domain has an unusually high affinity for carboxyl groups, with KD at ≈ 100 μM. Our findings implicate enhanced accessibility of negatively charged residues in structurally decayed proteins as a pattern recognition motif for αXβ 2 integrin. Comparisons among integrins show relevance of these findings to the large number of ligands recognized by αMβ 2 and αXβ2 but not αLβ2. The observations suggest that the pericellular proteolysis at the leading edge of neutrophils not only facilitates passage through the extracellular matrix but also manufactures binding sites for αXβ2.

KW - Plasmin

KW - Scavenger receptor

UR - http://www.scopus.com/inward/record.url?scp=13444294243&partnerID=8YFLogxK

U2 - 10.1073/pnas.0409057102

DO - 10.1073/pnas.0409057102

M3 - Journal article

C2 - 15665082

AN - SCOPUS:13444294243

VL - 102

SP - 1614

EP - 1619

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 5

ER -