Novel potential inhibitors of complement system and their roles in complement regulation and beyond
(2018) In Molecular Immunology 102. p.73-83- Abstract
The complement system resembles a double-edged sword since its activation can either benefit or harm the host. Thus, regulation of this system is of utmost importance and performed by several circulating and membrane-bound complement inhibitors. The pool of well-established regulators has recently been enriched with proteins that either share structural homology to known complement inhibitors such as Sushi domain-containing (SUSD) protein family and Human CUB and Sushi multiple domains (CSMD) families or extracellular matrix (ECM) macromolecules that interact with and modulate complement activity. In this review, we summarize the current knowledge about newly discovered complement inhibitors and discuss their implications in complement... (More)
The complement system resembles a double-edged sword since its activation can either benefit or harm the host. Thus, regulation of this system is of utmost importance and performed by several circulating and membrane-bound complement inhibitors. The pool of well-established regulators has recently been enriched with proteins that either share structural homology to known complement inhibitors such as Sushi domain-containing (SUSD) protein family and Human CUB and Sushi multiple domains (CSMD) families or extracellular matrix (ECM) macromolecules that interact with and modulate complement activity. In this review, we summarize the current knowledge about newly discovered complement inhibitors and discuss their implications in complement regulation, as well as in processes beyond complement regulation such cancer development. Understanding the behavior of these proteins will introduce new mechanisms of complement regulation and may provide new avenues in the development of novel therapies.
(Less)
- author
- Gialeli, Chrysostomi
LU
; Gungor, Bilgi
LU
and Blom, Anna M.
LU
- organization
- publishing date
- 2018
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Complement regulation, CSMD1, Extracellular matrix proteins, SUSD4
- in
- Molecular Immunology
- volume
- 102
- pages
- 11 pages
- publisher
- Pergamon Press Ltd.
- external identifiers
-
- pmid:30217334
- scopus:85053083427
- ISSN
- 0161-5890
- DOI
- 10.1016/j.molimm.2018.05.023
- language
- English
- LU publication?
- yes
- id
- 6e2a2e9b-f9b0-483f-8e55-a7deedc62e5a
- date added to LUP
- 2018-10-09 12:05:09
- date last changed
- 2025-07-10 21:06:27
@article{6e2a2e9b-f9b0-483f-8e55-a7deedc62e5a, abstract = {{<p>The complement system resembles a double-edged sword since its activation can either benefit or harm the host. Thus, regulation of this system is of utmost importance and performed by several circulating and membrane-bound complement inhibitors. The pool of well-established regulators has recently been enriched with proteins that either share structural homology to known complement inhibitors such as Sushi domain-containing (SUSD) protein family and Human CUB and Sushi multiple domains (CSMD) families or extracellular matrix (ECM) macromolecules that interact with and modulate complement activity. In this review, we summarize the current knowledge about newly discovered complement inhibitors and discuss their implications in complement regulation, as well as in processes beyond complement regulation such cancer development. Understanding the behavior of these proteins will introduce new mechanisms of complement regulation and may provide new avenues in the development of novel therapies.</p>}}, author = {{Gialeli, Chrysostomi and Gungor, Bilgi and Blom, Anna M.}}, issn = {{0161-5890}}, keywords = {{Complement regulation; CSMD1; Extracellular matrix proteins; SUSD4}}, language = {{eng}}, pages = {{73--83}}, publisher = {{Pergamon Press Ltd.}}, series = {{Molecular Immunology}}, title = {{Novel potential inhibitors of complement system and their roles in complement regulation and beyond}}, url = {{http://dx.doi.org/10.1016/j.molimm.2018.05.023}}, doi = {{10.1016/j.molimm.2018.05.023}}, volume = {{102}}, year = {{2018}}, }