Shock membrane electropotential drops and limited diffusive distance of β-amyloids in cerebral neurons are detrimental enhancement to Alzheimer's diseases

Colloids and Surfaces B: Biointerfaces

Volumn 73, Issue 2, 2009, Pages 339-345

  Chang, Chi Huan ^a,b   Peng, Chiung Huei ^b   Chen, Kuan Chou ^c   Huang, Hsien Bin ^a   Chiu, Wen Ta ^d   Peng, Robert Y ^b  

^a NATIONAL CHUNG CHENG UNIVERSITY   (Taiwan)

^b HUNGKUANG UNIVERSITY   (Taiwan)

^c TAIPEI MEDICAL UNIVERSITY   (Taiwan)

^d TAIPEI MEDICAL UNIVERSITY   (Taiwan)

Author keywords

Amyloid; Diffusion; Membrane Nernst potential; Viscosity

Indexed keywords

ALZHEIMER'S DISEASE; COMPARTMENTATION; DETRIMENTAL EFFECTS; DIFFUSION COEFFICIENTS; ELECTROPOTENTIAL; EMPIRICAL EQUATIONS; EXTRACELLULAR; INHERENT VISCOSITY; ION BINDING; ION REDISTRIBUTION; MEMBRANE POTENTIALS; PRODUCTION OF HYDROGEN; TRANSIENT MEMBRANE;

AGGLOMERATION; CALCIUM; DIFFUSION; DROPS; ENZYME ACTIVITY; GLYCOPROTEINS; HYDROGEN; HYDROGEN PEROXIDE; MEMBRANES; NEURONS; VISCOSITY;

CELL MEMBRANES;

AMYLOID BETA PROTEIN;

ALZHEIMER DISEASE; ARTICLE; CELL MEMBRANE TRANSPORT; DIFFUSION; NERVE CELL MEMBRANE POTENTIAL; NERVE POTENTIAL; PREDICTION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DETERMINATION; PROTEIN TRANSPORT; SOLUBILITY; VISCOSITY;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; ANIMALS; BRAIN; CALCIUM; CHELATING AGENTS; DIFFUSION; ELECTROLYTES; HOMEOSTASIS; MEMBRANE POTENTIALS; MODELS, BIOLOGICAL; NEURONS; ORGAN SPECIFICITY; TIME FACTORS; VISCOSITY;

EID: 68749092584     PISSN: 09277765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2009.06.004     Document Type: Article

References (46)

1. Schnapp B.J., Reese T.S., and Bechtold R. Kinesin is bound with high affinity to squid axon organelles that move to the plus-end of microtubules. J. Cell Biol. 119 (1992) 389-399
2. K.J. Bohm, Conventional Kinesin, 2005. http://www.imb-jena.de/.kboehm/Kinesin.html.
3. B. Saxon, 2005. http://www.proweb.org/kinesin/FxnVessTrans.html.
4. Nakagawa T., Setou M., Seog D., Ogasawara K., Dohmae N., Takio K., et al. A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex. Cell 103 (2000) 569-581
5. Verhey K.J., Meyer D., Deehan R., Bleinis J., Schnapp B.J., Rapoport T.A., et al. Cargo of kinesin identified as jip scaffolding proteins and associated signaling molecules. J. Cell Biol. 152 (2001) 959-970. http://www.proweb.org/kinesin/LatesFindings.html (also review in http://www.proweb.org/kinesin/LatesFindings.html)
6. Scholey J.M. Kinesin-II, a membrane traffic motor in axons, axonemes and spindles. J. Cell Biol. 133 (1996) 1-4
7. J.M. Scholey, (2005). http://www.proweb.org/kinesin/FxnVessTrans.html.
8. Vale R.D., and Fletterick R.J. The design plan of kinesin motors. Ann. Rev. Cell Biol. 13 (1985) 745-777
9. Bohm K.J., Steinmetzer P., Daniel A., Vater W., Baum M., and Unger E. Kinesin-driven microtubule motility in the presence of alkaline-earth ions. Indication for calcium ion-dependent motility. Cell Motil. Cytoskeleton 37 (1997) 226-231
10. Bossy-Wetzel E., Schwarzenbacher R., and Lipton S. Molecular pathways to neurodegeneration. Nature Medicine 10 (2004) S2-S9
11. Bush A.I., Multhaup G., Moir R.D., Williamson T.G., Small D.H., Rumble B., et al. A novel zinc (II) binding site modulates the function of the βA4 amyloid protein precursor of Alzheimer's disease. J. Biol. Chem. 268 (1993) 16109-16112
12. Bush A.I., Pettingell W.H., Multhaup G., d Paradis M., Vonsattel J.P., Gusella J.F., et al. Rapid induction of Alzheimer A beta amyloid formation by zinc. Science 265 (1994) 1464-1467
13. Kamal A., Stokin G.B., Yang Z., Xia C.H., and Goldstein L.S. Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-1. Neuron 28 (2000) 449-459
14. Pigino G., Morfini G., Pelsman A., Mattson M.P., Brady S.t., and Busciglio J. Alzheimer's presenilin-1 mutations impair kinesin-based axonal transport. J. Neurosci. 23 (2003) 4499-4508
15. Mattson M.P. Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol. Rev. 77 (1997) 1081-1132
16. Chapman P.F., White G.L., Jones M.W., Cooper-Blacketer D., Marshall V.J., Irizarry M., et al. Impaired synaptic plasticity and learning in aged amyloid precursor protein transgenic mice. Nat. Neurosci. 2 (1999) 271-276
17. Barnham K.J., Ciccotosto G.D., Tickler A.K., Ali F.E., Smith D.G., Williamson N.A., et al. Neurotoxic, redox-competent Alzheimer's beta-amyloid is released from lipid membrane by methionine oxidation. J. Biol. Chem. 278 (2003) 42959-42965
18. Huang X., Atwood C.S., Moir R.D., Hartshorn M.A., Tanzi R.E., and Bush A.I. Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Aβ peptides. J. Biol. Chem. 9 (2004) 954-960
19. In: Gates B.C. (Ed). Catalytic Chemistry (1991), John Wiley & Sons Inc., Singapore
20. Atwood C.S., Huang X., Moir R.D., Tanzi R.E., and Bush A.I. Role of free radicals and metal ions in the pathogenesis of Alzheimer's disease. Met. Ions Biol. Syst. 36 (1999) 309-364
21. Mattson M.P. Pathways towards and away from Alzheimer's disease. Nature 430 (2004) 631-639
22. Butterfield D.A. β-amyloid-associated free radical oxidative stress and neurotoxicity: implications for Alzheimer's disease. Chem. Res. Toxicol. 10 (1997) 495-506
23. Parks J.K., Smith T.S., Trimmer P.A., Bennett Jr. J.P., and Parker Jr. W.D. Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro. J. Neurochem. 76 (2001) 1050-1056
24. Watson A.A., Fairlie D.P., and Craik D.J. Solution structure of methionine-oxidized amyloid peptide (1-40). Does oxidation affect conformational switching?. Biochemistry 37 (1998) 12700-12706
25. Emerit J., Edeas M., and Bricaire F. Neurodegenerative diseases and oxidative stress. Biomed. Pharmacother. 58 (2004) 39-46
26. Huang X., Cuajungco M.P., Atwood C.S., Hartshorn M.A., Tyndall J.D., Hanson G.R., et al. Cu(II) potentiation of Alzheimer's abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction. J. Biol. Chem. 274 (1999) 37111-37116
27. Huang X., Atwood C.S., Hartshorn M.A., Multhaup G., Goldstein L.E., Scrapa S.C., et al. The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry 38 (1999) 7609-7616
28. In: Huang X., Atwood C.S., Goldstein L.E., Hartshorn M.A., Saunders A.J., Moir R.D., et al. (Eds). Alzheimer's Disease and Related Disorders: Etiology, Pathogenesis and Therapeutics (1999), Wiley, Chichester, UK 383
29. Bossy-Wetzel E., Talantova M.V., Lee W.D., Scholzke M.N., Harrop A., Mathews E., et al. Crosstalk between nitric oxide and zinc pathways to neuronal cell death involving mitochondrial dysfunction and p38-activated K+ channels. Neuron 41 (2004) 351-365
30. Lovell M.A., Robertson J.D., Teesdale W.J., Campbell J.L., and Markesbery W.R. Copper, iron and zinc in Alzheimer's disease senile plaques. J. Neurol. Sci. 158 (1998) 47-52
31. Suh S.W., Jensen K.B., Jensen M.S., Silva D.S., Kesslak P.J., Danscher G., et al. Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains. Brain Res. 852 (2000) 274-278
32. Loeffler D.A., LeWitt P.A., Juneau P.L., Sima A.A., Nguyen H.U., DeMaggio A.J., et al. Increased regional brain concentrations of ceruloplasmin in neurodegenerative disorders. Brain Res. 738 (1996) 265-274
33. Atwood C.S., Huang X., Khatri A., Scarpa R.C., Kim Y.S., Moir R.D., et al. Copper catalyzed oxidation of Alzheimer Abeta. Cell. Mol. Biol. 46 (2000) 777-783 (Noisy-Le-Grand)
34. In: Laidler K.J., and Meiser J.H. (Eds). Physical Chemistry (1987), Benjamin/Cummings Publishing Co. Inc., Philadelphia, USA
35. Japan Polymer Chemistry Association. Polymer Chemistry. first ed. (1984), Kyowentou, Tokyo, Japan
36. In: Pan G. (Ed). Physical Chemistry (1981), Chung-Cheng Book Company, Taipei
37. In: Guyton A.C. (Ed). Human Physiology and Mechanisms of Disease (1996), W. B. Sunders Co., Philadelphia, Pennsylvania, USA
38. Lambert M.P., Barlow A.K., Chromy B.A., Edwards C., Freed R., Liosatos M., et al. Diffusible nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 6448-6453
39. Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 (2003) 486-489
40. Kamal A., Almenar-Queralt A., LeBlanc J.F., Roberts E.A., and Goldstein L.S. Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP. Nature 414 (2001) 643-648
41. Biomolecular mechanisms of enzyme action, and metabolism. In: Voet D., and Voet J.G. (Eds). Biochemistry. third ed. vol. 1 (2004), John Wiley & Sons Inc., N.Y., USA
42. In: Harper H.A., Rodwell V.W., and Mayes P.A. (Eds). Review of Physiological Chemistry (1977), Lange Medical Publications, Los Altos, California 94022, USA
43. Akisik M.F., Aisen A.M., Sandrasegaran K., Jennings S.G., Lin C., Sherman S., Lin J.A., and Rydberg M. Assessment of chronic pancreatitis: utility of diffusion-weighted MR imaging with secretin ehancement. Radiology 250 1 (2009) 103-109 (Epub 2008 Nov 10)
44. Vukoiević V., Ming Y., D'Addario C., Hansen M., Langel U., Schulz R., Johansson B., Rigier R., and Terenius L. FASEB J 22 10 (2008) 3537-3548 (Epub 2008 Jun 27)
45. Namioshi S., Chen Y., Edwards J., and Benson H.A. Enhanced transdermal delivery of a dipeptide by dermaportation. Biopolymers 90 5 (2008) 655-662
46. Lei L., Sun H., Liu D., and Li S. Transport of Val-Leu-Pro-Val-Pro in human intestinal epithelial (Caco-2) cell monolayers. J. Agric. Food Chem. 56 10 (2008) 3582-3586 (Epub 2008 Apr 29)