Disease relevance of Setoflavin T

• Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: use of the fluorescent indicator, thioflavine T [1].
• Identification of immunoglobulin light chains in canine extramedullary plasmacytomas by thioflavine T and immunohistochemistry [2].
• Other round cell neoplasms (lymphosarcoma, histiocytoma, and mastocytoma) were negative with thioflavine T, indicating that positive staining with thioflavine T was specific for plasma cells (neoplastic and inflammatory) [2].

Psychiatry related information on Setoflavin T

• Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution [3].

High impact information on Setoflavin T

• In addition to beta-sheet structure, the oligomeric form of the protein is characterized by partial resistance to proteinase K digestion, affinity for amyloid-specific dye, thioflavine T, and fibrillar morphology [4].
• Consistent with this hypothesis, we also observe that magnesium inhibits alpha-synuclein aggregation, measured by immunoblot, cellulose acetate filtration, or thioflavine-T fluorescence [5].
• Fluorometry using thioflavine T also revealed that AApoAII fibril extension was inhibited by the addition of type B apoA-II in vitro [6].
• Fibrillogenesis at pH 2.0 occurs following a nucleation-dependent growth mechanism, as evidenced by the thioflavin T (ThT) assay [7].
• Aggregation of IAPP is considerably faster at a lower pH (4.0 +/- 0.3) than at high pH (8.8 +/- 0.3), as judged by turbidity and thioflavine-T fluorescence studies [8].

Chemical compound and disease context of Setoflavin T

• Four histologic staining methods used for detecting amyloid (Congo red, viewed in both normal and polarized light, Sirius red, Crystal violet and Thioflavine T) were applied to heart muscle autopsy samples from 19 patients who suffered from amyloidosis [9].

Biological context of Setoflavin T

• The kinetics of fibrillation were monitored by thioflavine-T (ThT) binding and the morphological changes by atomic force microscopy [10].
• Conversely, in vitro amyloid dyes Congo Red and Thioflavine T were demonstrated in the same experiments not to bind to the FDDNP binding site [11].
• With 250 nM thioflavine T, liver homogenates from a 17-month-old SAM-P/1 (senescence accelerated mouse-prone), which contained amyloid fibrils in murine senile amyloidosis (fASSAM) fluoresced brightly, whereas normal liver homogenates showed a negligible fluorescence [1].
• Seriously limited hydrolysis caused by higher peptide concentrations is consistent with monomeric/dimeric Abeta species participation in the process, confirmed by thioflavine T binding [12].

Anatomical context of Setoflavin T

• In a study of senile degenerative lesions-including Alzheimer's neurofibrillary changes, senile plaques and amyloid angiopathy-the hippocampal area of the brain was examined by thioflavine T fluorescence microscopy in 146 consecutive autopsy patients over the age of 49 [13].
• Thioflavine T cytoplasmic fluorescence was seen in the majority (18/29) of plasmacytomas and with inflammatory plasma cells present in control specimens [2].
• Thioflavine T and Dylon stainings, electron microscopy and immunohistochemistry revealed that thick amyloid deposits were present in the papillary dermis particularly beneath the epidermis [14].

Associations of Setoflavin T with other chemical compounds

• These fibrils were analyzed by electron microscopy, Congo red birefringence, thioflavine-T binding, and X-ray fiber diffraction, which unequivocally show their amyloid character [15].
• FT-IR spectra proved that hydrophilic HMSs adsorbed both Basic Yellow 1 and Acid Blue 45 by hydrogen bonding [16].
• Histopathology and electron microscopy of the kidneys revealed multifocal to coalescing deposits of proximal medullary interstitial amyloid, which fluoresced strongly with thioflavine T, and was sensitive to potassium permanganate treatment prior to Congo Red staining, thus indicating inflammatory (AA) origin [17].

Gene context of Setoflavin T

• Several techniques, including thioflavine-T fluorescence, turbidity, and negative-staining at the electron microscopy level, were used to assess amyloid formation [18].
• In the present work we have investigated whether apoE can affect the known spontaneous in vitro formation of amyloid-like fibrils by synthetic A beta analogues using a thioflavine-T assay for fibril formation, electron microscopy and Congo Red staining [19].
• Both a thioflavine-T (Th-T) fluorometric assay and circular dichroism (CD) spectroscopy showed the amyloid fibril formation of Abeta in PBS to be much higher than that of Abeta in PB [20].
• Using thioflavine T fluorescence and turbidity assays we demonstrated that the rate of aggregation for the Z AAT in the presence of LA at a molar ratio of 1:5 AAT to LA, in Tris-buffered saline, pH 7.4, is at least twice that of the Z protein alone or the M variant with and without LA [21].
• A thioflavine-T fluorometric assay and electron microscopic observations using negative staining together demonstrated that laminin inhibits A beta 40 fibril formation in vitro while it also inhibits A beta 40 fibril formation promoted by apoE4 [22].

Analytical, diagnostic and therapeutic context of Setoflavin T

• Amyloid formation was monitored by Congo-red staining and polarization microscopy of the peptide aggregates, by negative staining electron microscopy, and by quantitative fluorometry with thioflavine T [23].
• Both a thioflavine-T fluorometric assay and electron microscopy by negative staining demonstrated laminin to have a concentration-dependent inhibitory effect on Abeta42 fibril formation [24].
• This study confirms by immunohistochemistry that canine extramedullary plasmacytomas disproportionately express lambda light chains and establishes thioflavine T staining as a rapid histochemical method for diagnosis of these tumors [2].
• Nile Red, Congo red and Thioflavine T stainings were compared [25].
• After treatment of kidney sections with thioflavine T, the appearance and evolution of secretory function in the terminal segment of the afferent glomerular arteriole were assessed in terms of the granular cell index (GCI) and the juxtaglomerular cell granulation index (JGI) [26].

References