Amyloid-beta (25–35) peptide induces the release of pro-matrix metalloprotease 9 (pro-MMP-9) from human neutrophils

Molecular and Cellular Biochemistry

Volumn 397, Issue 1-2, 2014, Pages 117-123

  Achilli, Cesare ^a   Ciana, Annarita ^a   Minetti, Giampaolo ^a  

^a UNIVERSITY OF PAVIA   (Italy)

Author keywords

Alzheimer s disease; Amyloid beta; MMP 9; Neutrophils

Indexed keywords

AMYLOID BETA PROTEIN[25-35]; GELATINASE B; AMYLOID BETA PROTEIN; ENZYME PRECURSOR; MMP9 PROTEIN, HUMAN; PRO-MATRIX METALLOPROTEINASE 9;

ALZHEIMER DISEASE; AMYLOID PLAQUE; ARTICLE; BIOACCUMULATION; CONTROLLED STUDY; CYTOLYSIS; DEGRANULATION; ENZYME ACTIVATION; ENZYME RELEASE; HUMAN; HUMAN CELL; LEUKOCYTE ACTIVATION; NERVOUS SYSTEM INFLAMMATION; NEUROMODULATION; NEUROPATHOLOGY; NEUTROPHIL; NEUTROPHIL CHEMOTAXIS; NORMAL HUMAN; RESPIRATORY BURST; FEMALE; INFLAMMATION; MALE; METABOLISM; PATHOLOGY; SECRETION (PROCESS);

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; ENZYME PRECURSORS; FEMALE; HUMANS; INFLAMMATION; MALE; MATRIX METALLOPROTEINASE 9; NEUTROPHILS;

EID: 84912044519     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-014-2178-0     Document Type: Article

References (32)

1. Seeman P, Seeman N (2011) Alzheimer’s disease: β-amyloid plaque formation in human brain. Synapse 65:1289–1297. doi:10.1002/syn.20957
2. Millucci L, Ghezzi L, Bernardini G, Santucci A (2010) Conformations and biological activities of amyloid beta peptide 25–35. Curr Protein Pept Sci 11:54–67. doi:10.2174/138920310790274626
3. Howell S, Nalbantoglu J, Crine P (1995) Neutral endopeptidase can hydrolyze beta-amyloid (1–40) but shows no effect on beta-amyloid precursor protein metabolism. Peptides 16:647–652. doi:10.1016/0196-9781(95)00021-B
4. Kurochkin IV, Goto S (1994) Alzheimer’s beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme. FEBS Lett 345:33–37. doi:10.1016/0014-5793(94)00387-4
5. Eckman EA, Reed DK, Eckman CB (2001) Degradation of the Alzheimer’s amyloid beta peptide by endothelin-converting enzyme. J Biol Chem 276:24540–24548. doi:10.1074/jbc.M007579200
6. Hu J, Igarashi A, Kamata M, Nakagawa H (2001) Angiotensin-converting enzyme degrades Alzheimer amyloid beta-peptide (A beta); retards A beta aggregation, deposition, fibril formation; and inhibits cytotoxicity. J Biol Chem 276:47863–47868. doi:10.1074/jbc.M104068200
7. Tucker HM, Kihiko M, Caldwell JN, Wright S, Kawarabayashi T, Price D, Walker D, Scheff S, McGillis JP, Rydel RE, Estus S (2000) The plasmin system is induced by and degrades amyloid-beta aggregates. J Neurosci 20:3937–3946
8. Backstrom JR, Lim GP, Cullen MJ, Tökés ZA (1996) Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-beta peptide (1–40). J Neurosci 16:7910–7919
9. Vandooren J, Van den Steen PE, Opdenakker G (2013) Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decade. Crit Rev Biochem Mol Biol 48:222–272. doi:10.3109/10409238.2013.770819
10. Rosenberg GA (2009) Matrix metalloproteinases and their multiple roles in neurodegenerative diseases. Lancet Neurol 8:205–216. doi:10.1016/S1474-4422(09)70016-X
11. Ransohoff RM, Brown MA (2012) Innate immunity in the central nervous system. J Clin Investig 122:1164–1171. doi:10.1172/JCI58644
12. Fiala M, Cribbs DH, Rosenthal M, Bernard G (2007) Phagocytosis of amyloid-beta and inflammation: two faces of innate immunity in Alzheimer’s disease. J Alzheimer’s Dis 11:457–463
13. Baik SH, Cha MY, Hyun YM, Cho H, Hamza B, Kim DK, Han SH, Choi H, Kim KH, Moon M, Lee J, Kim M, Irimia D, Mook-Jung I (2014) Migration of neutrophils targeting amyloid plaques in Alzheimer’s disease mouse model. Neurobiol Aging 35:1286–1292. doi:10.1016/j.neurobiolaging.2014.01.003
14. Tiffany HL, Lavigne MC, Cui YH, Wang JM, Leto TL, Gao JL, Murphy PM (2001) Amyloid-beta induces chemotaxis and oxidant stress by acting at formylpeptide receptor 2, a G protein-coupled receptor expressed in phagocytes and brain. J Biol Chem 276:23645–23652. doi:10.1074/jbc.M101031200
15. Della Bianca V, Dusi S, Bianchini E, Dal Prà I, Rossi F (1999) Beta-amyloid activates the O-2 forming NADPH oxidase in microglia, monocytes, and neutrophils. A possible inflammatory mechanism of neuronal damage in Alzheimer’s disease. J Biol Chem 274:15493–15499
16. Park HY, Park JI, Baek DW, Lee SY, Lee MJ, Jin JO, Kim JW, Hong YS, Lee YH, Kwak JY (2006) Modulation of neutrophil apoptosis by beta-amyloid proteins. Int Immunopharmacol 6:1061–1069. doi:10.1016/j.intimp.2006.01.019
17. Faurschou M, Borregaard N (2003) Neutrophil granules and secretory vesicles in inflammation. Microbes Infect 5:1317–1327. doi:10.1016/j.micinf.2003.09.008
18. Schägger H (2006) Tricine–SDS-PAGE. Nat Protoc 1:16–22. doi:10.1038/nprot.2006.4
19. Böyum A (1968) Isolation of mononuclear cells and granulocytes from human blood. Isolation of monuclear cells by one centrifugation, and of granulocytes by combining centrifugation and sedimentation at 1 g. Scand J Clin Lab Investig Suppl 97:77–89
20. Achilli C, Ciana A, Balduini C, Risso A, Minetti G (2011) Application of gelatin zymography for evaluating low levels of contaminating neutrophils in red blood cell samples. Anal Biochem 409:296–297. doi:10.1016/j.ab.2010.10.019
21. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
22. Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350–4354
23. Pike CJ, Burdick D, Walencewicz AJ, Glabe CG, Cotman CW (1993) Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J Neurosci 13:1676–1687
24. Boland K, Behrens M, Choi D, Manias K, Perlmutter DH (1996) The serpin–enzyme complex receptor recognizes soluble, nontoxic amyloid-beta peptide but not aggregated, cytotoxic amyloid-beta peptide. J Biol Chem 271:18032–18044
25. Berridge MV, Herst PM, Tan AS (2005) Tetrazolium dyes as tools in cell biology: new insights into their cellular reduction. Biotechnol Annu Rev 11:127–152. doi:10.1016/S1387-2656(05)11004-7
26. 4) nanoparticles for boron neutron capture therapy (BNCT) application. Nanomedicine: NBM 10:589–597. doi:10.1016/j.nano.2013.10.003
27. Dahlgren C, Stendahl O (1983) Role of myeloperoxidase in luminol-dependent chemiluminescence of polymorphonuclear leukocytes. Infect Immun 39:736–741
28. Ra HJ, Parks WC (2007) Control of matrix metalloproteinase catalytic activity. Matrix Biol 26:587–596. doi:10.1016/j.matbio.2007.07.001
29. Mattson MP, Begley JG, Mark RJ, Furukawa K (1997) Abeta25–35 induces rapid lysis of red blood cells: contrast with Abeta1–42 and examination of underlying mechanisms. Brain Res 771:147–153. doi:10.1016/S0006-8993(97)00824-X
30. Näslund J, Haroutunian V, Mohs R, Davis KL, Davies P, Greengard P, Buxbaum JD (2000) Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline. JAMA 283:1571–1577. doi:10.1001/jama.283.12.1571
31. Fridman R, Toth M, Peña D, Mobashery S (1995) Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2). Cancer Res 55:2548–2555
32. Ramos-DeSimone N, Hahn-Dantona E, Sipley J, Nagase H, French DL, Quigley JP (1999) Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion. J Biol Chem 274:13066–13076