Complement Factor H: Using Atomic Resolution Structure to Illuminate Disease Mechanisms

Paul N. Barlow; Gregory S. Hageman; Susan M. Lea

doi:10.1007/978-0-387-78952-1_10

Complement Factor H: Using Atomic Resolution Structure to Illuminate Disease Mechanisms

Paul N. Barlow, Gregory S. Hageman, Susan M. Lea

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

Abstract

Complement Factor H has recently come to the fore with variant forms implicated in a range of serious disease states. This review aims to bring together recent data concerning the structure and biological activity of this molecule to highlight the way in which a molecular understanding of function may open novel therapeutic possibilities. In particular we examine the evidence for and against the hypothesis that sequence variations in factor H may predispose to disease if they perturb its ability to recognise and respond appropriately to polyanionic carbohydrates on host surfaces that require protection From complement-mediated damage.

Original language	English
Title of host publication	CURRENT TOPICS IN COMPLEMENT II
Editors	JD Lambris
Place of Publication	BERLIN
Publisher	Springer
Pages	117-142
Number of pages	26
ISBN (Print)	978-0-387-78951-4
DOIs	https://doi.org/10.1007/978-0-387-78952-1_10
Publication status	Published - 2008
Event	4th Aegean Workshop on Complement Associated Diseases, Animal Models and Therapeutics - Porto Heli Duration: 10 Jun 2007 → 17 Jun 2007

Conference

Conference	4th Aegean Workshop on Complement Associated Diseases, Animal Models and Therapeutics
City	Porto Heli
Period	10/06/07 → 17/06/07

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10.1007/978-0-387-78952-1_10

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title = "Complement Factor H: Using Atomic Resolution Structure to Illuminate Disease Mechanisms",

abstract = "Complement Factor H has recently come to the fore with variant forms implicated in a range of serious disease states. This review aims to bring together recent data concerning the structure and biological activity of this molecule to highlight the way in which a molecular understanding of function may open novel therapeutic possibilities. In particular we examine the evidence for and against the hypothesis that sequence variations in factor H may predispose to disease if they perturb its ability to recognise and respond appropriately to polyanionic carbohydrates on host surfaces that require protection From complement-mediated damage.",

author = "Barlow, {Paul N.} and Hageman, {Gregory S.} and Lea, {Susan M.}",

year = "2008",

doi = "10.1007/978-0-387-78952-1_10",

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pages = "117--142",

editor = "JD Lambris",

booktitle = "CURRENT TOPICS IN COMPLEMENT II",

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note = "4th Aegean Workshop on Complement Associated Diseases, Animal Models and Therapeutics ; Conference date: 10-06-2007 Through 17-06-2007",

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AU - Barlow, Paul N.

AU - Hageman, Gregory S.

AU - Lea, Susan M.

PY - 2008

Y1 - 2008

N2 - Complement Factor H has recently come to the fore with variant forms implicated in a range of serious disease states. This review aims to bring together recent data concerning the structure and biological activity of this molecule to highlight the way in which a molecular understanding of function may open novel therapeutic possibilities. In particular we examine the evidence for and against the hypothesis that sequence variations in factor H may predispose to disease if they perturb its ability to recognise and respond appropriately to polyanionic carbohydrates on host surfaces that require protection From complement-mediated damage.

AB - Complement Factor H has recently come to the fore with variant forms implicated in a range of serious disease states. This review aims to bring together recent data concerning the structure and biological activity of this molecule to highlight the way in which a molecular understanding of function may open novel therapeutic possibilities. In particular we examine the evidence for and against the hypothesis that sequence variations in factor H may predispose to disease if they perturb its ability to recognise and respond appropriately to polyanionic carbohydrates on host surfaces that require protection From complement-mediated damage.

U2 - 10.1007/978-0-387-78952-1_10

DO - 10.1007/978-0-387-78952-1_10

M3 - Conference contribution

SN - 978-0-387-78951-4

SP - 117

EP - 142

BT - CURRENT TOPICS IN COMPLEMENT II

A2 - Lambris, JD

PB - Springer

CY - BERLIN

T2 - 4th Aegean Workshop on Complement Associated Diseases, Animal Models and Therapeutics

Y2 - 10 June 2007 through 17 June 2007

ER -

Complement Factor H: Using Atomic Resolution Structure to Illuminate Disease Mechanisms

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