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Cited by 102

The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.

Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Aβ1–42, in differentiated PC12 cells

Burdick, Debra, Kosmoski, Joseph, Knauer, Mary F, Glabe, Charles G·1997·Brain Research
DOI 10.1016/s0006-8993(96)01262-0
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Abstract

A central question in Alzheimer's disease (AD) is the role of amyloid in pathogenesis. Recent discoveries implicating the longer A beta 1-42 form of amyloid in pathogenesis led us to characterize the interaction of A beta with cells to elucidate differences that might account for these observations. We characterized the adsorption, internalization and degradation of radiolabeled A beta in NGF-differentiated PC12 cells under conditions that are not acutely toxic. All A beta peptides examined absorb to the surface of PC12 cells and are internalized; however the adsorption and internalization of A beta 1-42 is significantly greater than that of A beta 1-40 and A beta 1-28. The adsorption of A beta 1-42 is decreased by treatment of the cells with neuraminidase, but not heparitinase. The fate of the internalized A beta 1-42 is also very different than shorter A beta peptides; a fraction of the internalized A beta 1-42 accumulates intracellularly and is resistant to degradation for at least 3 days while A beta 1-40 and shorter peptides are eliminated with a half life of about 1 h. A beta 1-42 does not appear to inhibit lysosomal hydrolases, since A beta 1-28 is degraded at the same rate in the presence or absence of A beta 1-42. The intracellular A beta 1-42 is located in a dense organellar compartment and colocalizes with the lysosomal markers Lucifer Yellow and horseradish peroxidase. These data indicate that there are significant differences in the cell surface adsorption, inter…

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Crossref · 10.1016/s0006-8993(96)01262-0

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9 of 9 references verified0 citation errors · 0 not checkable

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Claims other papers make about this one

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  • Previous studies have demonstrated internalization of synthetic Aβ peptides in neurons of hippocampal slices and in neuronal models in culture.

    “Previous studies have demonstrated internalization of synthetic A␤ peptides in neurons of hippocampal slices (65,70) and in neuronal models in culture (65,(71)(72)(73).”

    From Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E (2007) · cites this paper as [71]

Citations

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Research works printed but not linked: 9

  1. Avruch, J. and Wallach, D.F.H., Preparation and properties of plasma membrane and endoplasmic reticulum fragments from isolated rat fat cells, Biochim. Biophys. Acta, 233, (1971) 334–347. · DOI
  2. Cabral, D., Unger, W., Boulton, M. and Marshall, J., A microsystem to assay lysosomal activities in cultured retinal pigment epithelial cells, Curr. Eye Res., 7 (1988) 1097–1104. · DOI
  3. Dyrks, T., Weidemann, A., Multhaup, G., Salbaum, J.M., Lemaire, H.G., Kang, J., Muller-Hill, B., Masters, C.L. and Beyreuther, K., Identification, transmembrane orientation and biogenesis of the amyloid A4 precursor of Alzheimer's disease, EMBO. J., 7 (1988) 949–957. · DOI
  4. Knauer, M.F., Soreghan, B., Burdick, D., Kosmoski, J. and Glabe, C.G., Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein, Proc. Natl. Acad. Sci. USA, 89 (1992) 7437–7441.
  5. Masters, C.L., Simms, G., Weinman, N.A., Multhaup, G., McDonald, B.L. and Beyreuther, K., Amyloid plaque core protein in alzheimers disease and Down syndrome, Proc. Natl. Acad. Sci. USA, 82 (1985) 4245–4249.
  6. Prusiner, S.B. and DeArmond, S.J., Prion diseases and neurodegeneration, Ann. Rev. Neurosci., 17 (1994) 311–339. · DOI
  7. Roher, A.E., Lowenson, J.D., Clarke, S., Woods, A.S., Cotter, R.J., Gowing, E. and Ball., M.J., beta-Amyloid-(1–42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease, Proc. Natl. Acad. Sci. USA, 90 (1993) 10836–10840. · DOI · Paper page
  8. Selkoe, D.J., 1994. Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell. Biol., 10, 373–403. · DOI
  9. Vitek, M.P., Bhattacharya, K., Glendening, J.M., Stopa, E., Vlassara, H., Bucala, R., Manogue, K. and Cerami, A., Advanced glycation end products contribute to amyloidosis in Alzheimer disease, Proc. Natl. Acad. Sci. USA, 91 (1994) 4766–4770.

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Metadata

Authors
Burdick, D., Kosmoski, J., Knauer, M. F., & Glabe, C. G.
Venue
Brain Research
Publisher
Elsevier BV
Published
1997-01
Volume
746
Issue
1-2
Pages
275-284
ISSN
0006-8993
DOI
10.1016/s0006-8993(96)01262-0
Cited by
102
References
9
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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