Properdin: New roles in pattern recognition and target clearance

Claudia Kemper; Dennis E. Hourcade

doi:10.1016/j.molimm.2008.06.034

Properdin: New roles in pattern recognition and target clearance

Claudia Kemper, Dennis E. Hourcade^*

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Systemische Entzündungsforschung

Washington University in St. Louis

87 Zitate (Scopus)

Abstract

Properdinwas first described over 50 years ago by Louis Pillemer and his collaborators as a vitalcomponent of an antibody-independent complement activation pathway. In the 1970s properdin was shown to be a stabilizing component of the alternative pathway convertases, the central enzymes of the complement cascade. Recently we have reported that properdin can also bind to target cells and microbes, provide a platform for convertase assembly and function, and promote target phagocytosis. Evidence is emerging that suggests that properdin interacts with a network of target ligands, phagocyte receptors, and serum regulators. Here we review the new findings and their possible implications.

Originalsprache	Englisch
Zeitschrift	Molecular Immunology
Jahrgang	45
Ausgabenummer	16
Seiten (von - bis)	4048-4056
Seitenumfang	9
ISSN	0161-5890
DOIs	https://doi.org/10.1016/j.molimm.2008.06.034
Publikationsstatus	Veröffentlicht - 10.2008

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We gratefully acknowledge our properdin collaborators Dirk Spitzer, Lynne Mitchell, LiJuan Zhang, and John Atkinson and the helpful suggestions of Anja Fuchs, Christine Pham, Peter Densen, Michael Apicella, Tony Zalewski and Panisadee Avirutnan. We thank Madonna Bogacki for help with the manuscript. DEH was supported by NIH grant R01 AI05143. The content of this article is solely the responsibility of the authors and does not necessarily represent the official views of the National Institute of Allergy and infectious Diseases or the National Institutes of Health.

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Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

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10.1016/j.molimm.2008.06.034

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title = "Properdin: New roles in pattern recognition and target clearance",

abstract = "Properdinwas first described over 50 years ago by Louis Pillemer and his collaborators as a vitalcomponent of an antibody-independent complement activation pathway. In the 1970s properdin was shown to be a stabilizing component of the alternative pathway convertases, the central enzymes of the complement cascade. Recently we have reported that properdin can also bind to target cells and microbes, provide a platform for convertase assembly and function, and promote target phagocytosis. Evidence is emerging that suggests that properdin interacts with a network of target ligands, phagocyte receptors, and serum regulators. Here we review the new findings and their possible implications.",

author = "Claudia Kemper and Hourcade, \{Dennis E.\}",

note = "Funding Information: We gratefully acknowledge our properdin collaborators Dirk Spitzer, Lynne Mitchell, LiJuan Zhang, and John Atkinson and the helpful suggestions of Anja Fuchs, Christine Pham, Peter Densen, Michael Apicella, Tony Zalewski and Panisadee Avirutnan. We thank Madonna Bogacki for help with the manuscript. DEH was supported by NIH grant R01 AI05143. The content of this article is solely the responsibility of the authors and does not necessarily represent the official views of the National Institute of Allergy and infectious Diseases or the National Institutes of Health.",

year = "2008",

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doi = "10.1016/j.molimm.2008.06.034",

language = "English",

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N2 - Properdinwas first described over 50 years ago by Louis Pillemer and his collaborators as a vitalcomponent of an antibody-independent complement activation pathway. In the 1970s properdin was shown to be a stabilizing component of the alternative pathway convertases, the central enzymes of the complement cascade. Recently we have reported that properdin can also bind to target cells and microbes, provide a platform for convertase assembly and function, and promote target phagocytosis. Evidence is emerging that suggests that properdin interacts with a network of target ligands, phagocyte receptors, and serum regulators. Here we review the new findings and their possible implications.

AB - Properdinwas first described over 50 years ago by Louis Pillemer and his collaborators as a vitalcomponent of an antibody-independent complement activation pathway. In the 1970s properdin was shown to be a stabilizing component of the alternative pathway convertases, the central enzymes of the complement cascade. Recently we have reported that properdin can also bind to target cells and microbes, provide a platform for convertase assembly and function, and promote target phagocytosis. Evidence is emerging that suggests that properdin interacts with a network of target ligands, phagocyte receptors, and serum regulators. Here we review the new findings and their possible implications.

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U2 - 10.1016/j.molimm.2008.06.034

DO - 10.1016/j.molimm.2008.06.034

M3 - Scientific review articles

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AN - SCOPUS:55949096010

SN - 0161-5890

VL - 45

SP - 4048

EP - 4056

JO - Molecular Immunology

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IS - 16

ER -

Properdin: New roles in pattern recognition and target clearance

Abstract

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