Inhibition of leukocyte-endothelial cell interactions and inflammation by peptides from a bacterial adhesin which mimic coagulation factor X

Eva Rozdzinski; Jens Sandros; Michiel Van Der Flier; Alison Young; Barbara Spellerberg; Chandrabali Bhattacharyya; Julie Straub; Gary Musso; Scott Putney; Ruth Starzyk; Elaine Tuomanen

doi:10.1172/JCI117754

Inhibition of leukocyte-endothelial cell interactions and inflammation by peptides from a bacterial adhesin which mimic coagulation factor X

Eva Rozdzinski, Jens Sandros, Michiel Van Der Flier, Alison Young, Barbara Spellerberg, Chandrabali Bhattacharyya, Julie Straub, Gary Musso, Scott Putney, Ruth Starzyk, Elaine Tuomanen^*

^*Corresponding author for this work

Infectious Diseases patient care

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

36 Citations (Scopus)

Abstract

Factor X (factor ten) of the coagulation cascade binds to the integrin CD11b/CD18 during inflammation, initiating procoagulant activity on the surface of leukocytes (Altieri, D.C., O. R. Etingin, D. S. Fair, T. K. Brunk, J. E. Geltosky, D. P. Hajjar, and T. S. Edgington. 1991. Science [Wash. DC]. 254:1200-1202). Filamentous hemagglutinin (FHA), an adhesin of Bordetella pertussis also binds to the CD11b/CD18 integrin (Relman D., E. Tuomanen, S. Falkow, D. T. Golenbock, K. Saukkonen, and S. D. Wright. 1990. Cell. 61:1375- 1382). FHA and the CD11b/CD18 binding loops of Factor X share amino acid sequence similarity. FHA peptides similar to Factor X binding loops inhibited ¹²⁵I-Factor X binding to human neutrophils and prolonged clotting time. In addition, ETKEVDG and its Factor X analogue prevented transendothelial migration of leukocytes in vitro and reduced leukocytosis and blood brain barrier disruption in vivo. Interference with leukocyte migration by a coagulation-based peptide suggests a novel strategy for antiinflammatory therapy.

Original language	English
Pages (from-to)	1078-1085
Number of pages	8
Journal	Journal of Clinical Investigation
Volume	95
Issue number	3
DOIs	https://doi.org/10.1172/JCI117754
Publication status	Published - 1 Jan 1995

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Rozdzinski, E., Sandros, J., Van Der Flier, M., Young, A., Spellerberg, B., Bhattacharyya, C., Straub, J., Musso, G., Putney, S., Starzyk, R., & Tuomanen, E. (1995). Inhibition of leukocyte-endothelial cell interactions and inflammation by peptides from a bacterial adhesin which mimic coagulation factor X. Journal of Clinical Investigation, 95(3), 1078-1085. https://doi.org/10.1172/JCI117754

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title = "Inhibition of leukocyte-endothelial cell interactions and inflammation by peptides from a bacterial adhesin which mimic coagulation factor X",

abstract = "Factor X (factor ten) of the coagulation cascade binds to the integrin CD11b/CD18 during inflammation, initiating procoagulant activity on the surface of leukocytes (Altieri, D.C., O. R. Etingin, D. S. Fair, T. K. Brunk, J. E. Geltosky, D. P. Hajjar, and T. S. Edgington. 1991. Science [Wash. DC]. 254:1200-1202). Filamentous hemagglutinin (FHA), an adhesin of Bordetella pertussis also binds to the CD11b/CD18 integrin (Relman D., E. Tuomanen, S. Falkow, D. T. Golenbock, K. Saukkonen, and S. D. Wright. 1990. Cell. 61:1375- 1382). FHA and the CD11b/CD18 binding loops of Factor X share amino acid sequence similarity. FHA peptides similar to Factor X binding loops inhibited 125I-Factor X binding to human neutrophils and prolonged clotting time. In addition, ETKEVDG and its Factor X analogue prevented transendothelial migration of leukocytes in vitro and reduced leukocytosis and blood brain barrier disruption in vivo. Interference with leukocyte migration by a coagulation-based peptide suggests a novel strategy for antiinflammatory therapy.",

author = "Eva Rozdzinski and Jens Sandros and {Van Der Flier}, Michiel and Alison Young and Barbara Spellerberg and Chandrabali Bhattacharyya and Julie Straub and Gary Musso and Scott Putney and Ruth Starzyk and Elaine Tuomanen",

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Rozdzinski, E, Sandros, J, Van Der Flier, M, Young, A, Spellerberg, B, Bhattacharyya, C, Straub, J, Musso, G, Putney, S, Starzyk, R & Tuomanen, E 1995, 'Inhibition of leukocyte-endothelial cell interactions and inflammation by peptides from a bacterial adhesin which mimic coagulation factor X', Journal of Clinical Investigation, vol. 95, no. 3, pp. 1078-1085. https://doi.org/10.1172/JCI117754

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T1 - Inhibition of leukocyte-endothelial cell interactions and inflammation by peptides from a bacterial adhesin which mimic coagulation factor X

AU - Rozdzinski, Eva

AU - Sandros, Jens

AU - Van Der Flier, Michiel

AU - Young, Alison

AU - Spellerberg, Barbara

AU - Bhattacharyya, Chandrabali

AU - Straub, Julie

AU - Musso, Gary

AU - Putney, Scott

AU - Starzyk, Ruth

AU - Tuomanen, Elaine

PY - 1995/1/1

Y1 - 1995/1/1

N2 - Factor X (factor ten) of the coagulation cascade binds to the integrin CD11b/CD18 during inflammation, initiating procoagulant activity on the surface of leukocytes (Altieri, D.C., O. R. Etingin, D. S. Fair, T. K. Brunk, J. E. Geltosky, D. P. Hajjar, and T. S. Edgington. 1991. Science [Wash. DC]. 254:1200-1202). Filamentous hemagglutinin (FHA), an adhesin of Bordetella pertussis also binds to the CD11b/CD18 integrin (Relman D., E. Tuomanen, S. Falkow, D. T. Golenbock, K. Saukkonen, and S. D. Wright. 1990. Cell. 61:1375- 1382). FHA and the CD11b/CD18 binding loops of Factor X share amino acid sequence similarity. FHA peptides similar to Factor X binding loops inhibited 125I-Factor X binding to human neutrophils and prolonged clotting time. In addition, ETKEVDG and its Factor X analogue prevented transendothelial migration of leukocytes in vitro and reduced leukocytosis and blood brain barrier disruption in vivo. Interference with leukocyte migration by a coagulation-based peptide suggests a novel strategy for antiinflammatory therapy.

AB - Factor X (factor ten) of the coagulation cascade binds to the integrin CD11b/CD18 during inflammation, initiating procoagulant activity on the surface of leukocytes (Altieri, D.C., O. R. Etingin, D. S. Fair, T. K. Brunk, J. E. Geltosky, D. P. Hajjar, and T. S. Edgington. 1991. Science [Wash. DC]. 254:1200-1202). Filamentous hemagglutinin (FHA), an adhesin of Bordetella pertussis also binds to the CD11b/CD18 integrin (Relman D., E. Tuomanen, S. Falkow, D. T. Golenbock, K. Saukkonen, and S. D. Wright. 1990. Cell. 61:1375- 1382). FHA and the CD11b/CD18 binding loops of Factor X share amino acid sequence similarity. FHA peptides similar to Factor X binding loops inhibited 125I-Factor X binding to human neutrophils and prolonged clotting time. In addition, ETKEVDG and its Factor X analogue prevented transendothelial migration of leukocytes in vitro and reduced leukocytosis and blood brain barrier disruption in vivo. Interference with leukocyte migration by a coagulation-based peptide suggests a novel strategy for antiinflammatory therapy.

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JO - Journal of Clinical Investigation

JF - Journal of Clinical Investigation

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ER -

Inhibition of leukocyte-endothelial cell interactions and inflammation by peptides from a bacterial adhesin which mimic coagulation factor X

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