Skip to main content

Advertisement

Springer Nature Link
Log in

Serum amyloid A1 is involved in amyloid plaque aggregation and memory decline in amyloid beta abundant condition

  • Original Paper
  • Published:
Transgenic Research Aims and scope Submit manuscript

Abstract

Alzheimer's disease (AD) is a neurodegenerative disorder, characterized by cognitive impairment, progressive neurodegeneration, and amyloid-β (Aβ) lesion. In the neuronal death and disease progression, inflammation is known to play an important role. Our previous study on acute-phase protein serum amyloid A1 (SAA1) overexpressed mice showed that the liver-derived SAA1 accumulated in the brain by crossing the brain blood barrier (BBB) and trigger the depressive-like behavior on mouse. Since SAA1 involved in immune responses in other diseases, we focused on the possibility that SAA1 may exacerbate the neuronal inflammation related to Alzheimer’s disease. A APP/SAA overexpressed double transgenic mouse was generated using amyloid precursor protein overexpressed (APP)-c105 mice and SAA1 overexpressed mice to examine the function of SAA1 in Aβ abundant condition. Comparisons between APP and APP/SAA1 transgenic mice showed that SAA1 exacerbated amyloid aggregation and glial activation; which lead to the memory decline. Behavior tests also supported this result. Overall, overexpression of SAA1 intensified the neuronal inflammation in amyloid abundant condition and causes the greater memory decline compared to APP mice, which only expresses Aβ 1–42.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Subscribe and save

Springer+ Basic
$34.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or eBook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

Explore related subjects

Discover the latest articles and news from researchers in related subjects, suggested using machine learning.

References

  • Bach JH et al (2001) C-terminal fragment of amyloid precursor protein induces astrocytosis. J Neurochem 78(1):109–120

    Article  CAS  Google Scholar 

  • Badolato R et al (1994) Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes. J Exp Med 180(1):203–209

    Article  CAS  Google Scholar 

  • Bhak G, Choe YJ, Paik SR (2009) Mechanism of amyloidogenesis: nucleation-dependent fibrillation versus double-concerted fibrillation. BMB Rep 42(9):541–551

    Article  CAS  Google Scholar 

  • Chung JK et al (2016) Cortical amyloid beta deposition and current depressive symptoms in alzheimer disease and mild cognitive impairment. J Geriatr Psychiatry Neurol 29(3):149–159

    Article  Google Scholar 

  • Chung TF et al (2000) Serum amyloid A in Alzheimer's disease brain is predominantly localized to myelin sheaths and axonal membrane. Amyloid 7(2):105–110

    Article  CAS  Google Scholar 

  • Collins JM et al (2015) The effect of focal brain injury on beta-amyloid plaque deposition, inflammation and synapses in the APP/PS1 mouse model of Alzheimer's disease. Exp Neurol 267:219–229

    Article  CAS  Google Scholar 

  • De Simone V et al (2015) Th17-type cytokines, IL-6 and TNF-alpha synergistically activate STAT3 and NF-kB to promote colorectal cancer cell growth. Oncogene 34(27):3493–3503

    Article  Google Scholar 

  • Duyckaerts C, Potier MC, Delatour B (2008) Alzheimer disease models and human neuropathology: similarities and differences. Acta Neuropathol 115(1):5–38

    Article  Google Scholar 

  • Fritschi SK et al (2014) Highly potent soluble amyloid-beta seeds in human Alzheimer brain but not cerebrospinal fluid. Brain 137(Pt 11):2909–2915

    Article  Google Scholar 

  • Gou JT et al (2002) Inflammation-dependent cerebral deposition of serum amyloid a protein in a mouse model of amyloidosis. J Neurosci 22(14):5900–5909

    Article  Google Scholar 

  • Han MS et al (2013) JNK expression by macrophages promotes obesity-induced insulin resistance and inflammation. Science 339(6116):218–222

    Article  CAS  Google Scholar 

  • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297(5580):353–356

    Article  CAS  Google Scholar 

  • Jang WY et al (2016) Overexpression of serum amyloid a 1 induces depressive-like behavior in mice. Brain Res

  • Jang WY et al (2017) Overexpression of serum amyloid a 1 induces depressive-like behavior in mice. Brain Res 1654(Pt A):55–65

    Article  CAS  Google Scholar 

  • Ji YR et al (2015) Hepatic serum amyloid A1 aggravates T cell-mediated hepatitis by inducing chemokines via Toll-like receptor 2 in mice. J Biol Chem 290(20):12804–12811

    Article  CAS  Google Scholar 

  • Kindy MS et al (1999) Apolipoprotein serum amyloid a in alzheimer's disease. J Alzheimers Dis 1(3):155–167

    Article  CAS  Google Scholar 

  • Kindy MS et al (1999) Apolipoprotein serum amyloid a in Alzheimer's disease. Neuropathol Appl J Alzheimers Dis 1(3):155–167

    Article  CAS  Google Scholar 

  • Lesne SE et al (2013) Brain amyloid-beta oligomers in ageing and Alzheimer's disease. Brain 136(Pt 5):1383–1398

    Article  Google Scholar 

  • Lim HJ et al (2005) NSE-controlled carboxyl-terminus of APP gene over-expressing in transgenic mice induces altered expressions in behavior, Abeta-42, and GSK3beta binding proteins. Cell Mol Neurobiol 25(5):833–850

    Article  CAS  Google Scholar 

  • Parra MA et al (2015) Memory binding and white matter integrity in familial Alzheimer's disease. Brain 138(Pt 5):1355–1369

    Article  Google Scholar 

  • Pujadas L et al (2014) Reelin delays amyloid-beta fibril formation and rescues cognitive deficits in a model of Alzheimer's disease. Nat Commun 5:3443

    Article  Google Scholar 

  • Rodrigues R, Petersen RB, Perry G (2014) Parallels between major depressive disorder and Alzheimer's disease: role of oxidative stress and genetic vulnerability. Cell Mol Neurobiol 34(7):925–949

    Article  CAS  Google Scholar 

  • Song C et al (2009) Serum amyloid A induction of cytokines in monocytes/macrophages and lymphocytes. Atherosclerosis 207(2):374–383

    Article  CAS  Google Scholar 

  • Storey E, Cappai R (1999) The amyloid precursor protein of Alzheimer's disease and the Abeta peptide. Neuropathol Appl Neurobiol 25(2):81–97

    Article  CAS  Google Scholar 

  • Suh YH, Checler F (2002) Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease. Pharmacol Rev 54(3):469–525

    Article  CAS  Google Scholar 

  • Wragg RE, Jeste DV (1989) Overview of depression and psychosis in Alzheimer's disease. Am J Psychiatry 146(5):577–587

    Article  CAS  Google Scholar 

  • Zhang C et al (2013) Interleukin-6/signal transducer and activator of transcription 3 (STAT3) pathway is essential for macrophage infiltration and myoblast proliferation during muscle regeneration. J Biol Chem 288(3):1489–1499

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This work was supported by the National Research Foundation of Korea (NRF) Grant funded by the Korea Government (MSIP) (No. 2016R1A2B4014686) and (No. 2017R1A2B4007888)

Author information

Author notes

  1. Soyoung Jang and WooYoung Jang equally contributed to this work.

Authors and Affiliations

  1. School of Life Science and Biotechnology, KNU Creative BioResearch Group (BK21 Plus Project), Kyungpook National University, 1370 Sankyuk-dong, Buk-ku, Daegu, 702-701, Republic of Korea

    Soyoung Jang, Minjee Choi, Jinhee Lee, Wookbong Kwon, Si Jun Park, Sanggyu Lee & Zae Young Ryoo

  2. School of Animal Biotechnology (BT) Science, Kyungpook National University, Daegu, 37224, Republic of Korea

    Myoung Ok Kim

  3. Gyeongsangbukdo Livestock Institute Research, 186, Daeryongsan-ro, Anjung-myon, Yeongju-city, Gyeongsangbuk-do, Republic of Korea

    Junkoo Yi

  4. Laboratory Animal Resources Division, Toxicological Evaluation and Research Department, National Institute of Food and Drug Safety Evaluation, Cheongju-si, Republic of Korea

    Woo Young Jang

  5. Osong Health Technology Administration Complex, 187, Osongsaengmyeng 2-ro, Osong-eup, Heungdeok-gu, Chungcheongbuk-do, Cheongju-si, 28159, Republic of Korea

    Woo Young Jang

  6. Department of Animal Science, Kyungpook National University, Daegu, 37224, Republic of Korea

    Duhak Yoon

  7. Core Protein Resources Center, DGIST, Daegu, Republic of Korea

    Minjee Choi

Authors
  1. Soyoung Jang
    View author publications

    Search author on:PubMed Google Scholar

  2. Woo Young Jang
    View author publications

    Search author on:PubMed Google Scholar

  3. Minjee Choi
    View author publications

    Search author on:PubMed Google Scholar

  4. Jinhee Lee
    View author publications

    Search author on:PubMed Google Scholar

  5. Wookbong Kwon
    View author publications

    Search author on:PubMed Google Scholar

  6. Junkoo Yi
    View author publications

    Search author on:PubMed Google Scholar

  7. Si Jun Park
    View author publications

    Search author on:PubMed Google Scholar

  8. Duhak Yoon
    View author publications

    Search author on:PubMed Google Scholar

  9. Sanggyu Lee
    View author publications

    Search author on:PubMed Google Scholar

  10. Myoung Ok Kim
    View author publications

    Search author on:PubMed Google Scholar

  11. Zae Young Ryoo
    View author publications

    Search author on:PubMed Google Scholar

Corresponding author

Correspondence to Zae Young Ryoo.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Electronic supplementary material

Below is the link to the electronic supplementary material.

Supplementary material 1 (JPEG 62 kb)

Supplementary material 2 (DOCX 10 kb)

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Jang, S., Jang, W.Y., Choi, M. et al. Serum amyloid A1 is involved in amyloid plaque aggregation and memory decline in amyloid beta abundant condition. Transgenic Res 28, 499–508 (2019). https://doi.org/10.1007/s11248-019-00166-x

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11248-019-00166-x

Keywords