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β-Amyloid induces the production of active, matrix-degrading proteases in cultured rat astrocytes
Abstract
The senile and neuritic plaque neuropathology of Alzheimer's disease (AD) is accompanied by an inflammatory response that includes activated astrocytes and microglia. Activated mononuclear phagocytes and reactive astrocytes, in response to inflammatory cytokines, secrete a set of extracellular matrix (ECM)-degrading enzymes that include the matrix metalloproteinases (MMPs). The major peptide component of senile plaques of AD, beta-amyloid (Abeta), stimulates the production of several MMPs from cultured rat astrocytes and microglia. The purpose of this study was two-fold: (1) to compare the pattern of MMP induction in rat astrocytes on treatment with 'soluble' and 'fibrillar' Abeta(1-40) and Abeta(1-42), and (2) to examine whether treatment of astrocytes with Abeta results in degraded fragments of ECM. Abeta aggregation differentially affected the production of MMP-2 and MMP-9 in astrocyte cultures. Activation experiments with amino phenyl mercuric acetate suggested that the 52-54 kDa gelatin-degrading activity was an activated form of MMP-2. In addition, Abeta peptide induced both MMP-3 and plasminogen activator-like activity from astrocytes. When medium from Abeta-treated, astrocyte cultures was immunoblotted for fibronectin, several immunopositive, lower molecular weight bands were observed as compared to untreated conditioned medium, suggestive of the presence of an active fibronectin-degrading protease. Thus, Abeta induces the secretion of several matrix-degrading proteas…
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Some MMPs may play an important role in degrading soluble Ab, such as secreted MMP-2 and MMP-9 that generate C-terminally truncated Ab fragments and membrane-type MMP-14 that degrades both soluble and fibrillary Ab.
“Increasing in vitro evidence indicates that some MMPs may play an important role in degrading soluble Ab (sAb), such as secreted MMP-2 and MMP-9 that generate C-terminally truncated Ab fragments and membrane-type MMP-14 that degrades both soluble and fibrillary Ab (29)(30)(31)(32).”
From Differential protective effects of connective tissue growth factor against Aβ neurotoxicity on neurons and glia (2017) · cites this paper as [30]
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Cites
Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y. (1994) · Neuron · doi:10.1016/0896-6273(94)90458-8 · Cited by 1,774
Backstrom, J. R., Lim, G. P., Cullen, M. J., & Tökés, Z. A. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-24-07910.1996 · Cited by 331
Selective distribution of matrix metalloproteinase-3 (MMP-3) in Alzheimer’s disease brain
Yoshiyama, Y., Asahina, M., & Hattori, T. (2000) · Acta Neuropathologica · doi:10.1007/pl00007428 · Cited by 128
Brain matrix metalloproteinase 1 levels are elevated in Alzheimer's disease
Leake, A., Morris, C. M., & Whateley, J. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01418-x · Cited by 95
Flagged first, then by citations
Research works printed but not linked: 38
- Abraham, 1988, Immunohistochemical identification of the serine protease inhibitor alpha1-antichymotrypsin in the brain amyloid deposits of Alzheimer’s disease, Cell, 52, 487, 10.1016/0092-8674(88)90462-X · DOI
- Backstrom, 1992, Characterization of neutral proteinases from Alzheimer-affected and control brain specimens: identification of calcium-dependent metalloproteinases from the hippocampus, J. Neurochem., 58, 983, 10.1111/j.1471-4159.1992.tb09352.x · DOI
- Chen, 1997, Neuronal death in the hippocampus is promoted by plasmin-catalyzed degradation of laminin, Cell, 91, 917, 10.1016/S0092-8674(00)80483-3 · DOI · Paper page
- Cotman, 1992, beta-Amyloid neurotoxicity—a discussion of in vitro findings, Neurobiol. Aging, 13, 587, 10.1016/0197-4580(92)90060-B · DOI
- Deb, 1996, Increased production of matrix metalloproteinases in enriched astrocyte and mixed hippocampal cultures treated with β-amyloid peptides, J. Neurochem., 66, 1641, 10.1046/j.1471-4159.1996.66041641.x · DOI
- Fukai, 1995, Release of biological activities from quiescent fibronectin by conformational change and limited proteolysis by matrix metalloproteinases, Biochemistry, 34, 11453, 10.1021/bi00036a018 · DOI
- Gottschall, 1995, Cytokines regulate gelatinase A and B (matrix metalloproteinase 2 and 9) activity in cultured rat astrocytes, J. Neurochem., 64, 1513, 10.1046/j.1471-4159.1995.64041513.x · DOI
- Homandberg, 1992, Fibronectin fragments cause chondrolysis of bovine articular cartilage slices in culture, J. Biol. Chem., 267, 3597, 10.1016/S0021-9258(19)50566-X · DOI
- Hu, 1998, Amyloid-beta peptide activates cultured astrocytes: morphological alterations, cytokine induction and nitric oxide release, Brain Res., 785, 195, 10.1016/S0006-8993(97)01318-8 · DOI · Paper page
- Jarrett, 1993, Seeding ‘one-dimensional crystalization’ of amyloid: a pathogenic mechanism in Alzheimer’s disease, Cell, 73, 1055, 10.1016/0092-8674(93)90635-4 · DOI · Paper page
- Johnstone, 1999, A central role for astrocytes in the inflammatory response to beta-amyloid; chemokines, cytokines and reactive oxygen species are produced, J. Neuroimmunol., 93, 182, 10.1016/S0165-5728(98)00226-4 · DOI
- Klein, 2001, Targeting small Abeta oligomers: the solution to an Alzheimer’s disease conundrum?, Trends Neurosci., 24, 219, 10.1016/S0166-2236(00)01749-5 · DOI · Paper page
- Kleiner, 1994, Quantitative zymography: detection of picogram quantities of gelatinases, Anal. Biochem., 218, 325, 10.1006/abio.1994.1186 · DOI
- Koo, 1993, Amyloid β-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth, Proc. Natl. Acad. Sci. U.S.A., 90, 4748, 10.1073/pnas.90.10.4748 · DOI
- Krystosek, 1981, Plasminogen activator secretion by granule neurons in cultures of developing cerebellum, Science, 213, 7810
- Mahler, 1997, Differential expression of fibronectin, tenascin-C and NCAMs in cultured hippocampal astrocytes activated by kainate, bacterial lipopolysaccharide or basic fibroblast growth factor, Brain Res., 775, 63, 10.1016/S0006-8993(97)00901-3 · DOI
- Mattson, 1992, β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity, J. Neurosci., 12, 376, 10.1523/JNEUROSCI.12-02-00376.1992 · DOI
- McCawley, 2001, Matrix metalloproteinases: they’re not just for matrix anymore!, Curr. Opin. Cell Biol., 13, 534, 10.1016/S0955-0674(00)00248-9 · DOI · Paper page
- Muir, 1992, Stromelysin generates a fibronectin fragment that inhibits Schwann cell proliferation, J. Cell Biol., 116, 177, 10.1083/jcb.116.1.177 · DOI
- Peress, 1995, Localization of tissue inhibitor of matrix metalloproteinases in Alzheimer’s disease and normal brain, J. Neuropathol. Exp. Neurol., 54, 16, 10.1097/00005072-199501000-00002 · DOI · Paper page
- Perides, 1995, Glial hyaluronate-binding protein: a product of metalloproteinase digestion of versican?, Biochem. J., 312, 377, 10.1042/bj3120377 · DOI
- Pike, 1993, Neurodegeneration induce by β-amyloid peptides in vitro: the role of peptide assembly state, J. Neurosci., 13, 1676, 10.1523/JNEUROSCI.13-04-01676.1993 · DOI · Paper page
- Roher, 1994, Proteolysis of Aß peptide from Alzheimer disease brain by gelatinase A, Biochem. Biophys. Res. Commun., 205, 1755, 10.1006/bbrc.1994.2872 · DOI
- Rosenberg, 1994, Injury-induced 92-kilodalton gelatinase and urokinase expression in rat brain, Lab. Invest., 71, 417
- Rossi, 1996, Synergistic induction of nitric oxide by beta-amyloid and cytokines in astrocytes, Biochem. Biophys. Res. Commun., 225, 474, 10.1006/bbrc.1996.1197 · DOI
- Selkoe, 1994, Alzheimer’s disease: a central role for amyloid, J. Neuropathol. Exp. Neurol., 53, 438, 10.1097/00005072-199409000-00003 · DOI
- Sreenath, 1992, Expression of matrix metalloproteinase genes in transformed rat cell lines of high and low metastatic potential, Cancer Res., 52, 4942
- Strauss, 1992, Detection of interleukin-6 and a2-macroglobulin immunoreactivity in cortex and hippocampus of Alzheimer’s disease patients, Lab. Invest., 66, 223
- Tsirka, 1995, Excitotoxin-induced degeneration and seizure are mediated by tissue plasminogen activator, Nature, 377, 340, 10.1038/377340a0 · DOI
- Tucker, 2000, The plasmin system is induced by and degrades amyloid-β-aggregates, J. Neurosci., 20, 3937, 10.1523/JNEUROSCI.20-11-03937.2000 · DOI
- D. Van Gool, G. Carmeliet, E. Triau, J.J. Cassiman, R.D., Appearance of localized immunoreactivity for the alpha 4 integrin subunit and for fibronectin in brains from Alzheimer’s, Lewy body dementia patients and aged controls, Neurosci. Lett. 170 (1994) 71–73. · DOI
- Vassalli, 1994, Membrane proteases in focus, Nature, 370, 14, 10.1038/370014a0 · DOI
- Wysocki, 1990, Fibronectin profiles in normal and chronic wound fluid, Lab. Invest., 63, 825
- Xie, 1993, Fibronectin fragments bind to and penetrate cartilage tissue resulting in proteinase expression and cartilage damage, Biochim. Biophys. Acta, 1182, 189, 10.1016/0925-4439(93)90140-V · DOI
- Xie, 1992, Fibronectin fragments in osteoarthritic synovial fluid, J. Rheumatol., 19, 1448
- Yamada, 1995, White matter microglia produce membrane-type matrix metalloprotease, an activator of gelatinase A, in human brain tissues, Acta Neuropathol., 90, 421, 10.1007/BF00294800 · DOI
- Yankner, 1992, Commentary and perspective on studies of beta-amyloid neurotoxicity, Neurobiol. Aging, 13, 615, 10.1016/0197-4580(92)90067-8 · DOI
- Zhang, 1997, Zymographic measurement of gelatinase activity in brain tissue after detergent extraction and affinity-support purification, J. Neurosci. Methods, 76, 15, 10.1016/S0165-0270(97)00065-4 · DOI
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Yan, P., Hu, X., Song, H., Yin, K., Bateman, R. J., Cirrito, J. R., Xiao, Q., Hsu, F. F., Turk, J. W., Xu, J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602440200 · Cited by 380
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Miners, J. S., Barua, N., Kehoe, P. G., Gill, S., & Love, S. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182345e46 · Cited by 265
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Yang, C.-N., Wu, M.-F., Liu, C.-C., Jung, W.-H., Chang, Y.-C., Lee, W.-P., Shiao, Y.-J., Wu, C.-L., Liou, H.-H., Lin, S.-K., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx278 · Cited by 27
Metadata
- Authors
- Deb, S., Wenjun Zhang, J., & Gottschall, P. E.
- Venue
- Brain Research
- Publisher
- Elsevier BV
- Published
- 2003-04
- Volume
- 970
- Issue
- 1-2
- Pages
- 205-213
- ISSN
- 0006-8993
- Cited by
- 81
- References
- 4
- Language
- en
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