C1q ablation exacerbates amyloid deposition: A study in a transgenic mouse model of ATTRV30M amyloid neuropathy
PLoS ONE, ISSN: 1932-6203, Vol: 12, Issue: 4, Page: e0175767
2017
- 11Citations
- 30Captures
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Metrics Details
- Citations11
- Citation Indexes11
- CrossRef11
- 11
- Captures30
- Readers30
- 30
Article Description
ATTRV30M amyloid neuropathy is a lethal autosomal dominant sensorimotor and autonomic neuropathy, caused by deposition of amyloid fibrils composed of aberrant transthyretin (TTR). Ages of onset and penetrance exhibit great variability and genetic factors have been implicated. Complement activation co-localizes with amyloid deposits in amyloidotic neuropathy and is possibly involved in the kinetics of amyloidogenesis. A candidate gene approach has recently identified C1q polymorphisms to correlate with disease onset in a Cypriot cohort of patients with ATTRV30M amyloid neuropathy. In the current study we use a double transgenic mouse model of ATTRV30M amyloid neuropathy in which C1q is ablated to elucidate further a possible modifier role for C1q. Amyloid deposition is found to be increased by 60% in the absence of C1q. Significant up regulation is also recorded in apoptotic and cellular stress markers reflecting extracellular toxicity of pre-fibrillar and fibrillar TTR. Our data further indicate that in the absence of C1q there is marked reduction of macrophages in association with amyloid deposits and thus less effective phagocytosis of TTR.
Bibliographic Details
10.1371/journal.pone.0175767; 10.1371/journal.pone.0175767.g001; 10.1371/journal.pone.0175767.g008; 10.1371/journal.pone.0175767.g003; 10.1371/journal.pone.0175767.g002; 10.1371/journal.pone.0175767.g007; 10.1371/journal.pone.0175767.g004; 10.1371/journal.pone.0175767.g005; 10.1371/journal.pone.0175767.g006
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