Histamine induces the production of matrix metalloproteinase-9 in human astrocytic cultures via H1-receptor subtype
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- 作者：Aarti Patel ; Vishnu Vasanthan ; Wen Fu ; Richard P. Fahlman…
- 关键词：Histamine ; Matrix metalloproteinase ; 9 ; Astrocytes ; Soluble oligomeric amyloid beta peptide
- 刊名：Brain Structure and Function
- 出版年：2016
- 出版时间：May 2016
- 年：2016
- 卷：221
- 期：4
- 页码：1845-1860
- 全文大小：1,427 KB
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Vishnu Vasanthan (1)
Wen Fu (1)
Richard P. Fahlman (2)
David MacTavish (1)
Jack H. Jhamandas (1)
1. Division of Neurology, Department of Medicine, Institute of Neuroscience and Mental Health, 530 Heritage Medical Research Centre, University of Alberta, Edmonton, AB, T6G 2S2, Canada
2. Department of Biochemistry, University of Alberta, Edmonton, AB, T6G 2S2, Canada - 刊物主题：Neurosciences; Cell Biology; Neurology;
- 出版者：Springer Berlin Heidelberg
- ISSN：1863-2661
- 卷排序：221
文摘
Accumulation of β-amyloid (Aβ) protein within the brain is a neuropathological hallmark of Alzheimer’s disease (AD). One strategy to facilitate Aβ clearance from the brain is to promote Aβ catabolism. Matrix metalloproteinase-9 (MMP-9), a member of the family of Zn+2-containing endoproteases, known to be expressed and secreted by astrocytes, is capable of degrading Aβ. Histamine, a major aminergic brain neurotransmitter, stimulates the production of MMP-9 in keratinocytes through the histamine H1 receptor (H1R). In the present study, we show that histamine evokes a concentration- and calcium-dependent release of MMP-9 from human astrocytic U373 cells and primary cultures of human and rat astrocytes through the H1R subtype. Activation of H1R on astrocytes elevated intracellular levels of Ca2+ that was accompanied by time-dependent increases in MAP kinase p44/p42 and PKC. In-cell western blots revealed dose-dependent increases in both enzymes, confirming involvement of these signal transduction pathways. We next investigated the extent of recombinant human MMP-9 (rhMMP-9) proteolytic activity on soluble oligomeric Aβ (soAβ). Mass spectrometry demonstrated time-dependent cleavage of soAβ (20 μM), but not another amyloidogenic protein amylin, upon incubation with rhMMP-9 (100 nM) at 1, 4 and 17 h. Furthermore, Western blots showed a shift in soAβ equilibrium toward lower order, less toxic monomeric species. In conclusion, both MAPK p44/p42 and PKC pathways appear to be involved in histamine-upregulated MMP-9 release via H1Rs in astrocytes. Furthermore, MMP-9 appears to cleave soAβ into less toxic monomeric species. Given the key role of histamine in MMP-9 release, this neurotransmitter may serve as a potential therapeutic target for AD. Keywords Histamine Matrix metalloproteinase-9 Astrocytes Soluble oligomeric amyloid beta peptide