Congo Red and amyloids: history and relationship

被引:264
作者
Yakupova, Elmira I. [1 ]
Bobyleva, Liya G. [1 ]
Vikhlyantsev, Ivan M. [1 ,2 ]
Bobylev, Alexander G. [1 ,2 ]
机构
[1] Russian Acad Sci, Inst Theoret & Expt Biophys, Pushchino 142290, Moscow Region, Russia
[2] Pushchino State Inst Nat Sci, Fac Biophys & Biomed, Pushchino 142290, Moscow Region, Russia
基金
俄罗斯基础研究基金会; 俄罗斯科学基金会;
关键词
SEDIMENTATION-VELOCITY ANALYSIS; APPLE-GREEN BIREFRINGENCE; FIBRIL FORMATION; IN-VITRO; THIOFLAVIN-T; CIRCULAR-DICHROISM; BETA-PROTEIN; AGGREGATION PATHWAYS; SIZE-DISTRIBUTION; STRUCTURAL MODEL;
D O I
10.1042/BSR20181415
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Staining with Congo Red (CR) is a qualitative method used for the identification of amyloids in vitro and in tissue sections. However, the drawbacks and artefacts obtained when using this dye can be found both in vitro and in vivo. Analysis of scientific data from previous studies shows that CR staining alone is not sufficient for confirmation of the amyloid nature of protein aggregates in vitro or for diagnosis of amyloidosis in tissue sections. In the present paper, we describe the characteristics and limitations of other methods used for amyloid studies. Our historical review on the use of CR staining for amyloid studies may provide insight into the pitfalls and caveats related to this technique for researchers considering using this dye.
引用
收藏
页数:22
相关论文
共 205 条
[91]   'Apple-green birefringence' of amyloid stained by Congo red [J].
Howie, Alexander J. ;
Owen-Casey, Mared P. .
KIDNEY INTERNATIONAL, 2012, 82 (01) :114-114
[92]   Discrepancies between descriptions and illustrations of colours in Congo red-stained amyloid, and explanation of discrepant colours [J].
Howie, Alexander J. ;
Owen-Casey, Mared P. .
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, 2010, 17 (3-4) :109-117
[93]   Optical properties of amyloid stained by Congo red: History and mechanisms [J].
Howie, Alexander J. ;
Brewer, Douglas B. .
MICRON, 2009, 40 (03) :285-301
[94]   Alternate aggregation pathways of the Alzheimer β-amyloid peptide -: An in vitro model of preamyloid [J].
Huang, THJ ;
Yang, DS ;
Fraser, PE ;
Chakrabartty, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (46) :36436-36440
[95]   Amyloid fibril formation propensity is inherent into the hexapeptide tandemly repeating sequence of the central domain of silkmoth chorion proteins of the A-family [J].
Iconomidou, Vassiliki A. ;
Chryssikos, Georglos D. ;
Gionis, Vassilis ;
Galanis, Athanassios S. ;
Cordopatis, Paul ;
Hoenger, Andreas ;
Hamodrakas, Stavros J. .
JOURNAL OF STRUCTURAL BIOLOGY, 2006, 156 (03) :480-488
[96]   Histidine residues underlie Congo red binding to Aβ analogs [J].
Inouye, H ;
Nguyen, JT ;
Fraser, PE ;
Shinchuk, LM ;
Packard, AB ;
Kirschner, DA .
AMYLOID-INTERNATIONAL JOURNAL OF EXPERIMENTAL AND CLINICAL INVESTIGATION, 2000, 7 (03) :179-188
[97]   STRUCTURE OF BETA-CRYSTALLITE ASSEMBLIES FORMED BY ALZHEIMER BETA-AMYLOID PROTEIN ANALOGS - ANALYSIS BY X-RAY-DIFFRACTION [J].
INOUYE, H ;
FRASER, PE ;
KIRSCHNER, DA .
BIOPHYSICAL JOURNAL, 1993, 64 (02) :502-519
[98]   Small-angle scattering for structural biology-Expanding the frontier while avoiding the pitfalls [J].
Jacques, David A. ;
Trewhella, Jill .
PROTEIN SCIENCE, 2010, 19 (04) :642-657
[99]  
Jalandoni-Buan AC., 2010, Philippine Journal of Science, V139, P71
[100]   High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy [J].
Jaroniec, CP ;
MacPhee, CE ;
Bajaj, VS ;
McMahon, MT ;
Dobson, CM ;
Griffin, RG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (03) :711-716