Serum amyloid P component-induced cell death in primary cultures of rat cerebral cortex

Urbányi, Zoltán; Lakics, Viktor; Erdö, Sándor L.

doi:10.1016/0926-6917(94)90016-7

Cited by 18 publications

(19 citation statements)

References 8 publications

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“…155,156 SAP has been shown to induce cell death in primary cultures of rat cerebral cortex suggesting that SAP may play a role in the development of Alzheimer’s disease. 157 Binding of SAP to amyloid fibrils prevents proteolysis of the amyloid fibrils in vitro and thus enhances induction of amyloidosis in vivo as shown by delayed and reduced amyloid deposition in SAP-deficient mice. 158,159 The interference with binding of SAP to amyloid fibrils in vivo may promote regression of the deposits.…”

Section: Short Pentraxins: Crp and Sapmentioning

confidence: 99%

Pattern Recognition by Pentraxins

Agrawal

Singh

Bottazzi

et al. 2009

Advances in Experimental Medicine and Biology

139

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Pentraxins are a family of evolutionarily conserved pattern-recognition proteins that are made up of five identical subunits. Based on the primary structure of the subunit, the pentraxins are divided into two groups: short pentraxins and long pentraxins. C-reactive protein (CRP) and serum amyloid P-component (SAP) are the two short pentraxins. The prototype protein of the long pentraxin group is pentraxin 3 (PTX3). CRP and SAP are produced primarily in the liver while PTX3 is produced in a variety of tissues during inflammation. The main functions of short pentraxins are to recognize a variety of pathogenic agents and then to either eliminate them or neutralize their harmful effects by utilizing the complement pathways and macrophages in the host. CRP binds to modified low-density lipoproteins, bacterial polysaccharides, apoptotic cells, and nuclear materials. By virtue of these recognition functions, CRP participates in the resolution of cardiovascular, infectious, and autoimmune diseases. SAP recognizes carbohydrates, nuclear substances, and amyloid fibrils and thus participates in the resolution of infectious diseases, autoimmunity, and amyloidosis. PTX3 interacts with several ligands, including growth factors, extracellular matrix component and selected pathogens, playing a role in complement activation and facilitating pathogen recognition by phagocytes. In addition, data in gene-targeted mice show that PTX3 is essential in female fertility, participating in the assembly of the cumulus oophorus extra-cellular matrix. PTX3 is therefore a nonredundant component of the humoral arm of innate immunity as well as a tuner of inflammation. Thus, in conjunction with the other components of innate immunity, the pentraxins use their pattern-recognition property for the benefit of the host.

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Section: Short Pentraxins: Crp and Sapmentioning

confidence: 99%

Pattern Recognition by Pentraxins

Agrawal

Singh

Bottazzi

et al. 2009

Advances in Experimental Medicine and Biology

139

View full text Add to dashboard Cite

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“…SAP is highly resistant to proteolysis (10) and its binding stabilizes amyloid fibrils (11), enhances their formation in vitro (12), and contributes to their pathogenic deposition and/or persistence in vivo in systemic amyloidosis (13). Furthermore, human SAP has been reported to bind to and enter neurons in culture and in rat brain in vivo, to cause apoptotic cell death (14)(15)(16)(17)(18), and to activate human microglia synergistically with A␤ and C1q in vitro, provoking increased production of pro-inflammatory cytokines and A␤ itself (19). Current therapeutic developments for Alzheimer's disease, largely focused on A␤, have so far shown modest if any clinical benefit (20).…”

mentioning

confidence: 99%

Molecular dissection of Alzheimer's disease neuropathology by depletion of serum amyloid P component

Kolstoe

Ridha

Bellotti

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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“…SAP is reported to co-localise with Aβ plaques in human AD brain [23,24], exhibit up-regulated synthesis in AD affected brain regions [25], induce neuronal apoptosis in vitro [26,27] and protect senile plaques from proteolysis [28].…”

Section: Discussionmentioning

confidence: 99%

Longitudinal Protein Changes in Blood Plasma Associated with the Rate of Cognitive Decline in Alzheimer’s Disease

Sattlecker

Khondoker

Proitsi

et al. 2016

JAD

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Biomarkers of Alzheimer's disease (AD) progression are needed to support the development of urgently needed disease modifying drugs. We employed a SOMAscan assay for quantifying 1,001 proteins in blood samples from 90 AD subjects, 37 stable mild cognitive impaired (MCI) subjects, 39 MCI subjects converting to AD within a year and 69 controls at baseline and one year follow up. We used linear mixed effects models to identify proteins changing significantly over one year with the rate of cognitive decline, which was quantified as the reduction of Mini Mental State Examination (MMSE) scores. Additionally we investigated proteins changing differently across disease groups and during the conversion from MCI to AD. We found that levels of proteins belonging to the complement cascade increase significantly in fast declining AD patients. Longitudinal changes in the complement cascade might be a surrogate biomarker for disease progression. Additionally we found that members of the cytokine-cytokine receptor interaction pathway change during AD when compared to healthy aging subjects.

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Serum amyloid P component-induced cell death in primary cultures of rat cerebral cortex

Cited by 18 publications

References 8 publications

Pattern Recognition by Pentraxins

Pattern Recognition by Pentraxins

Molecular dissection of Alzheimer's disease neuropathology by depletion of serum amyloid P component

Longitudinal Protein Changes in Blood Plasma Associated with the Rate of Cognitive Decline in Alzheimer’s Disease

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