scholarly journals The Non-Core Regions of Human Lysozyme Amyloid Fibrils Influence Cytotoxicity

2010 ◽  
Vol 402 (5) ◽  
pp. 783-796 ◽  
Author(s):  
Maria F. Mossuto ◽  
Anne Dhulesia ◽  
Glyn Devlin ◽  
Erica Frare ◽  
Janet R. Kumita ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Human Lysozyme

scholarly journals A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme

Nature ◽  
2003 ◽  
Vol 424 (6950) ◽  
pp. 783-788 ◽  
Author(s):  
Mireille Dumoulin ◽  
Alexander M. Last ◽  
Aline Desmyter ◽  
Klaas Decanniere ◽  
Denis Canet ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Antibody Fragment ◽  
Human Lysozyme

Engineering a Camelid Antibody Fragment That Binds to the Active Site of Human Lysozyme and Inhibits Its Conversion into Amyloid Fibrils†

Biochemistry ◽  
2008 ◽  
Vol 47 (42) ◽  
pp. 11041-11054 ◽  
Author(s):  
Pak-Ho Chan ◽  
Els Pardon ◽  
Linda Menzer ◽  
Erwin De Genst ◽  
Janet R. Kumita ◽  
...  
Keyword(s):  
Active Site ◽  
Amyloid Fibrils ◽  
Antibody Fragment ◽  
Human Lysozyme

Oligomers, protofibrils and amyloid fibrils from recombinant human lysozyme (rHL): Fibrillation process and cytotoxicity evaluation for ARPE-19 cell line

2015 ◽  
Vol 126 ◽  
pp. 335-343 ◽  
Author(s):  
Eva D. Ruiz ◽  
Mario Almada ◽  
María G. Burboa ◽  
Pablo Taboada ◽  
Víctor Mosquera ◽  
...  
Keyword(s):  
Cell Line ◽  
Amyloid Fibrils ◽  
Human Lysozyme ◽  
Recombinant Human Lysozyme

Liquid crystalline ordering of paired helical filaments in neurofibrillary tangles of Alzheimer's disease

1986 ◽  
Vol 44 ◽  
pp. 348-349
Author(s):  
D.F. Clapin ◽  
V.J.A. Montpetit
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Neurofibrillary Tangles ◽  
Liquid Crystalline ◽  
Amyloid Fibrils ◽  
Geometric Analysis ◽  
Paired Helical Filaments ◽  
Microscopic Level ◽  
Light Microscopic Level ◽  
Regular Spacing

Alzheimer's disease is characterized by the accumulation of abnormal filamentous proteins. The most important of these are amyloid fibrils and paired helical filaments (PHF). PHF are located intraneuronally forming bundles called neurofibrillary tangles. The designation of these structures as "tangles" is appropriate at the light microscopic level. However, localized domains within individual tangles appear to demonstrate a regular spacing which may indicate a liquid crystalline phase. The purpose of this paper is to present a statistical geometric analysis of PHF packing.

scholarly journals A temporal and ultrastructural relationship between heparan sulfate proteoglycans and AA amyloid in experimental amyloidosis.

1991 ◽  
Vol 39 (10) ◽  
pp. 1321-1330 ◽  
Author(s):  
A D Snow ◽  
R Bramson ◽  
H Mar ◽  
T N Wight ◽  
R Kisilevsky
Keyword(s):  
Heparan Sulfate ◽  
Amyloid Fibrils ◽  
Dermatan Sulfate ◽  
Polyclonal Antibodies ◽  
Amyloid Deposition ◽  
Sulfate Proteoglycan ◽  
Aa Amyloidosis ◽  
Experimental Amyloidosis ◽  
Protein Core ◽  
Dermatan Sulfate Proteoglycan

Previous histochemical studies have suggested a close temporal relationship between the deposition of highly sulfated glycosaminoglycans (GAGs) and amyloid during experimental AA amyloidosis. In the present investigation, we extended these initial observations by using specific immunocytochemical probes to analyze the temporal and ultrastructural relationship between heparan sulfate proteoglycan (HSPG) accumulation and amyloid deposition in a mouse model of AA amyloidosis. Antibodies against the basement membrane-derived HSPG (either protein core or GAG chains) demonstrated a virtually concurrent deposition of HSPGs and amyloid in specific tissue sites regardless of the organ involved (spleen or liver) or the induction protocol used (amyloid enhancing factor + silver nitrate, or daily azocasein injections). Polyclonal antibodies to AA amyloid protein and amyloid P component also demonstrated co-localization to sites of HSPG deposition in amyloid sites, whereas no positive immunostaining was observed in these locales with a polyclonal antibody to the protein core of a dermatan sulfate proteoglycan (known as "decorin"). Immunogold labeling of HSPGs (either protein core or GAG chains) in amyloidotic mouse spleen or liver revealed specific localization of HSPGs to amyloid fibrils. In the liver, heparan sulfate GAGs were also immunolocalized to the lysosomal compartment of hepatocytes and/or Kupffer cells adjacent to sites of amyloid deposition, suggesting that these cells are involved in HSPG production and/or degradation. The close temporal and ultrastructural relationship between HSPGs and AA amyloid further implies an important role for HSPGs during the initial stages of AA amyloidosis.

Radioimmunoassay for urinary lysozyme in human serum from leukemic patients.

1978 ◽  
Vol 24 (12) ◽  
pp. 2155-2157 ◽  
Author(s):  
T L Peeters ◽  
Y R Depraetere ◽  
G R Vantrappen
Keyword(s):  
Human Serum ◽  
Monocytic Leukemia ◽  
Human Lysozyme ◽  
Normal Volunteers ◽  
Separation Step ◽  
Lysozyme Concentration

Abstract We present a radioimmunoassay for lysozyme in human serum, based upon human lysozyme isolated from the urine of leukemic patients and antiserum prepared against this lysozyme in the goat. In the separation step, a second antibody is used. By properly adjusting the concentrations of unlabeled and 125I-labeled lysozyme and of the antibodies, maximal precision (SD, 0.04 mg/litre) was obtained in the range 0.00 to 2.00 mg/litre. In 20 normal volunteers the lysozyme concentration was 4.6 +/- 0.8 mg/litre (mean +/- SD), in 13 patients with monocytic leukemia 34.4 +/- 8.6 mg/litre. Correlation with lysoplate determinations was excellent in leukemic sera (r = 0.97) but was poor in normal sera (r = 0.35), possibly owing to the existence of isoenzymes.

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