Identification of factor H-like protein 1 as the predominant complement regulator in Bruch’s membrane: Implications for age-related macular degeneration
Open accessAbstract
The tight regulation of innate immunity on extracellular matrix (ECM) is a vital part of immune homeostasis throughout the human body, and disruption to this regulation in the eye is thought to contribute directly to the progression of age-related macular degeneration (AMD). The plasma complement regulator factor H (FH) is thought to be the main regulator that protects ECM against damaging complement activation. However, in the present study we demonstrate that a truncated form of FH, called FH-like protein 1 (FHL-1), is the main regulatory protein in the layer of ECM under human retina, called Bruch’s membrane. Bruch’s membrane is a major site of AMD disease pathogenesis and where drusen, the hallmark lesions of AMD, form. We show that FHL-1 can passively diffuse through Bruch’s membrane, whereas the full sized, glycosylated, FH cannot. FHL-1 is largely bound to Bruch’s membrane through interactions with heparan sulfate, and we show that the common Y402H polymorphism in the CFH gene, associated with an increased risk of AMD, reduces the binding of FHL-1 to this heparan sulfate. We also show that FHL-1 is retained in drusen whereas FH coats the periphery of the lesions, perhaps inhibiting their clearance. Our results identify a novel mechanism of complement regulation in the human eye, which highlights potential new avenues for therapeutic strategies.
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Some complement proteins such as FHL-1, FD, and C5a have been found to pass through BrM, while C3a is not able to do so despite its small molecular weight.
“While some complement proteins such as Factor H-like protein 1 (FHL-1), Factor D (FD), and C5a have been found to pass through BrM [35,36], it has been reported that C3a, despite its small molecular weight, is not able to do so.”
From Bruch’s Membrane: A Key Consideration with Complement-Based Therapies for Age-Related Macular Degeneration (2023) · cites this paper as [36]
FHL-1 (49 kDa), a splice variant of CFH, has better tissue penetration than full-length glycosylated FH (155 kDa).
“The fact that FHL-1 (49 kDa), a splice variant of the CFH gene, has better tissue penetration than the full-length, glycosylated FH protein (155 kDa)”
From Bruch’s Membrane: A Key Consideration with Complement-Based Therapies for Age-Related Macular Degeneration (2023) · cites this paper as [36]
FHL-1 may play a specialised role in controlling complement activation locally.
“suggests that it may play a specialised role in controlling complement activation locally [35,36].”
From Bruch’s Membrane: A Key Consideration with Complement-Based Therapies for Age-Related Macular Degeneration (2023) · cites this paper as [36]
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Self-citation
- Authors
- Clark, S. J., Schmidt, C. Q., White, A. M., Hakobyan, S., Morgan, B. P., & Bishop, P. N.
- Affiliations
- Manchester Academic Health Science Centre (GB)
- Universität Ulm (DE)
- Centre for Hearing and Vision Research, Institute of Human Development, University of Manchester , Manchester M13 9PT ,
- Cardiff University (GB)
- Corresponding author
- Clark, Simon J
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2014-11
- Volume
- 193
- Issue
- 10
- Pages
- 4962-4970
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- PMC
- PMC4225158
- OpenAlex
- W1871202872
- Cited by
- 122
- References
- 59
- Citations by year
- 2026: 13 · 2025: 6 · 2024: 8 · 2023: 8 · 2022: 10 · 2021: 13 · 2020: 13 · 2019: 5 · 2018: 12 · 2017: 10 · 2016: 10 · 2015: 13 · 2014: 1
- FWCI
- 5.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Immunology (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- ORCA Online Research @Cardiff (Cardiff University) (submittedVersion)
- Funders
- Wellcome Trust
- University of Manchester
- Directorate for Biological Sciences
- Medical Research Council (MR/K004441/1, K004441, MR/K024418/1)
- Biotechnology and Biological Sciences Research Council
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Complement system in diseases
- Health Sciences › Medicine › Ophthalmology › Retinal Diseases and Treatments
- Health Sciences › Medicine › Ophthalmology › Ocular Diseases and Behçet’s Syndrome
- Keywords
- factor H-like protein 1, complement factor H, complement regulation, Bruch's membrane, age-related macular degeneration, drusen, heparan sulfate, CFH Y402H polymorphism, extracellular matrix, complement activation
- MeSH terms
- Complement Activation, Complement C3b Inactivator Proteins, Extracellular Matrix, Gene Expression Regulation, Glycosylation, Heparan Sulfate, Homeostasis, Humans, Immunity, Innate, Macular Degeneration, Protein Binding, Retina, Signal Transduction, Retinal Drusen, Bruch Membrane, Complement Factor H, Protein Transport
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