alcian-blue and Amyloidosis

alcian-blue has been researched along with Amyloidosis* in 4 studies

Reviews

1 review(s) available for alcian-blue and Amyloidosis

ArticleYear
Histochemistry of amyloid. General considerations, light microscopical and ultrastructural examinations.
    Experimental pathology. Supplement, 1975, Volume: 1

    Topics: Alcian Blue; Amyloid; Amyloidosis; Congo Red; Histocytochemistry; Humans; Microscopy, Electron; Microscopy, Fluorescence; Optical Rotation; Periodic Acid-Schiff Reaction; Spectrophotometry, Infrared; Staining and Labeling; Tolonium Chloride; X-Ray Diffraction

1975

Other Studies

3 other study(ies) available for alcian-blue and Amyloidosis

ArticleYear
Masson Trichrome and Sulfated Alcian Blue Stains Distinguish Light Chain Deposition Disease From Amyloidosis in the Lung.
    The American journal of surgical pathology, 2021, 03-01, Volume: 45, Issue:3

    Light chain deposition disease, characterized by nonamyloidogenic deposits of immunoglobulin light chains, is rare in the lung and possibly underdiagnosed due to low clinical suspicion and lack of readily accessible tests. We encountered a case of pulmonary light chain deposition disease (PLCDD) in which light chain deposits appeared crimson red with a Masson trichrome (MT) stain and salmon pink with a sulfated Alcian blue (SAB) stain. This prompted us to characterize a series of PLCDD cases and assess the utility of MT and SAB stains to distinguish them from amyloidosis. From the pathology archives of 2 institutions spanning 10 years, we identified 11 cases of PLCDD, including 7 diagnosed as such and 4 determined retrospectively. The deposits in all cases of PLCDD stained crimson red with MT and salmon pink with SAB, while the cases of pulmonary amyloid (n=10) stained blue-gray and blue-green, respectively. The immunoglobulin light chain nature of the deposits was confirmed in 10 of 11 cases by either immunofluorescence microscopy (n=5) or mass spectrometry (n=5). Transmission electron microscopy revealed osmiophilic, electron-dense deposits in all cases analyzed (n=3). An extranodal marginal zone lymphoma of mucosa-associated lymphoid tissue type was diagnosed in 10 cases and 1 represented a plasma cell neoplasm. Our study highlights the importance of considering PLCDD in the differential diagnosis of amyloid-like deposits in the lung and the value of performing MT and SAB stains to distinguish between PLCDD and amyloidosis.

    Topics: Adult; Aged; Alcian Blue; Amyloidosis; Azo Compounds; Biomarkers; Biopsy; Coloring Agents; Diagnosis, Differential; Eosine Yellowish-(YS); Female; Humans; Immunoglobulin Light Chains; Lung; Lung Diseases; Male; Methyl Green; Middle Aged; Predictive Value of Tests; Retrospective Studies; Staining and Labeling

2021
Peptide p5 binds both heparinase-sensitive glycosaminoglycans and fibrils in patient-derived AL amyloid extracts.
    Biochemical and biophysical research communications, 2013, Jun-21, Volume: 436, Issue:1

    In previously published work, we have described heparin-binding synthetic peptides that preferentially recognize amyloid deposits in a mouse model of reactive systemic (AA) amyloidosis and can be imaged by using positron and single photon emission tomographic imaging. We wanted to extend these findings to the most common form of visceral amyloidosis, namely light chain (AL); however, there are no robust experimental animal models of AL amyloidosis. To further define the binding of the lead peptide, p5, to AL amyloid, we characterized the reactivity in vitro of p5 with in situ and patient-derived AL amyloid extracts which contain both hypersulfated heparan sulfate proteoglycans as well as amyloid fibrils. Histochemical staining demonstrated that the peptide specifically localized with tissue-associated AL amyloid deposits. Although we anticipated that p5 would undergo electrostatic interactions with the amyloid-associated glycosaminoglycans expressing heparin-like side chains, no significant correlation between peptide binding and glycosaminoglycan content within amyloid extracts was observed. In contrast, following heparinase I treatment, although overall binding was reduced, a positive correlation between peptide binding and amyloid fibril content became evident. This interaction was further confirmed using synthetic light chain fibrils that contain no carbohydrates. These data suggest that p5 can bind to both the sulfated glycosaminoglycans and protein fibril components of AL amyloid. Understanding these complex electrostatic interactions will aid in the optimization of synthetic peptides for use as amyloid imaging agents and potentially as therapeutics for the treatment of amyloid diseases.

    Topics: Alcian Blue; Amyloid; Amyloidosis; Benzothiazoles; Carbohydrates; Glycosaminoglycans; Heparin; Heparin Lyase; Humans; Peptides; Protein Binding; Static Electricity; Thiazoles

2013
Novel CHST6 gene mutations in 2 unrelated cases of macular corneal dystrophy.
    Cornea, 2011, Volume: 30, Issue:6

    To investigate the possible mutations in the carbohydrate sulfotransferase 6 (CHST6) gene of 2 unrelated cases of macular corneal dystrophy (MCD) and to report atypical stromal deposits in one of them.. Corneal tissues were stained with antisulfated keratan sulfate (KS), antitransforming growth factor beta 1-induced protein (TGFBIp), thioflavin-T, alcian blue, and Masson trichrome. Sequencing was performed to identify potential mutations in the CHST6 gene and the fourth and twelfth exons of the TGFBI gene.. Alcian blue staining revealed the presence of multiple subepithelial and intrastromal mucopolysaccharide deposits, confirming the diagnosis of MCD in both cases. Immunofluorescence staining in case 1 revealed the presence of sulfated KS only in the keratocytes and select endothelial cells, consistent with MCD type IA. Preferential expression of sulfated KS was observed in keratocytes and extracellular stromal matrix in case 2, consistent with MCD type II. Atypical subepithelial and superficial stromal deposits were observed in case 1, which stained positively with alcian blue, eosin, Masson trichrome, and thioflavin-T indicating the presence of hyaline and amyloid materials. CHST6 gene sequencing revealed 2 heterozygous mutations in case 1 (a p.Arg211Gln and a novel mutation of p.Arg177Gly) and a novel homozygous mutation of p.Pro186Arg in case 2. No mutations were found in exons 4 or 12 of the TGFBI gene in case 1.. Secondary hyalinosis and amyloidosis occur in a case of MCD type IA with a novel p.Arg177Gly mutation in CHST6. A novel p.Pro186Arg mutation in CHST6 is associated with MCD type II in an African American.

    Topics: Adult; Alcian Blue; Amyloidogenic Proteins; Amyloidosis; Carbohydrate Sulfotransferases; Coloring Agents; Corneal Dystrophies, Hereditary; Corneal Stroma; DNA Mutational Analysis; Extracellular Matrix Proteins; Female; Humans; Keratoplasty, Penetrating; Male; Point Mutation; Polymerase Chain Reaction; Staining and Labeling; Sulfotransferases; Transforming Growth Factor beta

2011