ZIB

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

Presence of non-fibrillar amyloid β protein in skin biopsies of Alzheimer's disease (AD), Down's syndrome and non-AD normal persons (1994)

Wen, G. Y. ; Wisniewski, H. M. ; Blondal, H. ; [et al.]

Springer

Acta neuropathologica 88 (1994), S. 201-206

add to mindlist on the mindlist

Details

ISSN: 1432-0533

Keywords: Amyloid β protein ; Skin biopsy Alzheimer's disease ; Down's syndrome

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract A total of 66 skin biopsies from persons with Alzheimer's disease (AD) or Down's syndrome (DS) and from persons without AD were used in this study. The age range was from 7 to 89 years. Positive immunoreactivity of skin biopsies to monoclonal antibody 4G8, which is reactive to amino acid residue 17–24 of synthetic amyloid β protein (Aβ), and 4G8-Fab (the antigen-binding fragment of 4G8 IgG, reactive only to amyloid plaque) was observed in the epidermis-dermis junction or the basement membrane of the epidermis and in some blood vessels of the biopsy skins of 13/18 (72%) AD, 9/10 (90%) DS, and 14/38 (37%) non-AD control cases. The Fisher exact probability test revealed a significant difference (P=0.0415 one-tailed) in immunoreactivity between AD and age-matched controls. There was also a significant difference (P=0.0152 one-tailed; P=0.0200 two-tailed) between DS and age-matched control in the same test. Immuno-gold electron microscopy examination of these cases with positive immunoreactivity revealed that the gold particles were deposited along the basement membrane of the epidermis. Amyloid fibrils were not observed in the regions with gold particles. Results of this study suggest that Aβ is associated with the basement membrane of skin and is present in amorphous, non-fibrillar form as soluble Aβ.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00293394

Permalink

Library	Location	Call Number	Volume/Issue/Year	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

Some factors determining protein aggregation during ultrafiltration (1993)

Kim, K. J. ; Chen, V. ; Fane, A. G.

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 42 (1993), S. 260-265

add to mindlist on the mindlist

Details

ISSN: 0006-3592

Keywords: fouling ; ultrafiltration ; protein aggregates ; field emission scanning electron microscopy (FESEM) ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: The factors contributing to protein aggregation in albumin ultrafiltration were investigated as a function of operation conditions. The nature of protein deposits was examined by electron microscopy. Protein aggregation appears to occur as a result of rapid supersaturation of protein molecules and high solvent velocity (shear) in the concentrated layer near the membrane surface. The shear occurring in the solvent flow on the membrane surface probably unfolds protein molecules and thus promotes flocculation due to collision between particles. © 1993 John Wiley & Sons, Inc.

Additional Material: 6 Ill.