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

Research output: Contribution to journal › Review article › peer-review

81 Scopus citations

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.

Original language	English
Pages (from-to)	4048-4056
Number of pages	9
Journal	Molecular Immunology
Volume	45
Issue number	16
DOIs	https://doi.org/10.1016/j.molimm.2008.06.034
State	Published - Oct 2008

Keywords

Apoptosis
Complement
Complement alternative pathway
Glycosaminoglycans
Neutrophils
Pattern recognition
Phagocytosis
Properdin

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10.1016/j.molimm.2008.06.034

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@article{2a926913abe444f69fed7eb456cd3a8a,

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.",

keywords = "Apoptosis, Complement, Complement alternative pathway, Glycosaminoglycans, Neutrophils, Pattern recognition, Phagocytosis, Properdin",

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",

month = oct,

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

language = "English",

volume = "45",

pages = "4048--4056",

journal = "Molecular Immunology",

issn = "0161-5890",

number = "16",

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TY - JOUR

T1 - Properdin

T2 - New roles in pattern recognition and target clearance

AU - Kemper, Claudia

AU - Hourcade, Dennis E.

N1 - 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.

PY - 2008/10

Y1 - 2008/10

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.

KW - Apoptosis

KW - Complement

KW - Complement alternative pathway

KW - Glycosaminoglycans

KW - Neutrophils

KW - Pattern recognition

KW - Phagocytosis

KW - Properdin

UR - http://www.scopus.com/inward/record.url?scp=55949096010&partnerID=8YFLogxK

U2 - 10.1016/j.molimm.2008.06.034

DO - 10.1016/j.molimm.2008.06.034

M3 - Review article

C2 - 18692243

AN - SCOPUS:55949096010

SN - 0161-5890

VL - 45

SP - 4048

EP - 4056

JO - Molecular Immunology

JF - Molecular Immunology

IS - 16

ER -

Properdin: New roles in pattern recognition and target clearance

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Keywords

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