[1] Staining methods for identification of amyloid in tissue

Westermark, Gunilla T.; Johnson, Kenneth H.; Westermark, Per

doi:10.1016/s0076-6879(99)09003-5

Cited by 270 publications

(230 citation statements)

References 28 publications

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“…Congo red staining, a classical method for detection of amyloid [31], revealed red spots in the cells expressing proSP-C L188Q or proSP-C ΔExon4 ( Fig. 2A).…”

Section: Aggregation Behaviour Of Prosp-c L188q Prosp-c δExon4 Anmentioning

confidence: 99%

Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C

Nerelius

Martin

Peng

et al. 2008

Biochemical Journal

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International audienceThe newly synthesized surfactant protein C precursor (proSP-C) is an integral endoplasmic reticulum (ER) membrane protein with a single metastable polyVal α-helical transmembrane domain that comprises two thirds of the mature peptide. More than 20 mutations in the ER-lumenal, C-terminal domain of proSP-C (CTC), are associated with interstitial lung disease (ILD), and some of the mutations cause intracellular accumulation of cytotoxic protein aggregates and a corresponding decrease in mature SP-C. Here it is shown that (i) human embryonic kidney cells expressing the ILD associated mutants proSP-CL188Q and proSP-CΔExon4 accumulate Congo red positive amyloid-like inclusions, while cells transfected with the mutant proSP-CI73T do not, (ii) transfection of CTC into cells expressing proSP-CL188Q results in a stable CTC/proSP-CL188Q complex, increased proSP-CL188Q half life and reduced formation of Congo red positive deposits, (iii) replacement of the metastable polyVal transmembrane segment with a stable polyLeu likewise prevents formation of amyloid-like proSP-CL188Q aggregates, and (iv) binding of recombinant CTC to non-helical SP-C blocks SP-C amyloid fibril formation. These data suggest that CTC can prevent the polyVal segment of proSP-C from promoting formation of amyloid-like deposits during biosynthesis, by binding to non-helical conformations. Mutations in the Brichos domain of proSP-C may lead to ILD via loss of CTC chaperone function

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“…Congo red staining, a classical method for detection of amyloid [31], revealed red spots in the cells expressing proSP-C L188Q or proSP-C ΔExon4 ( Fig. 2A).…”

Section: Aggregation Behaviour Of Prosp-c L188q Prosp-c δExon4 Anmentioning

confidence: 99%

Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C

Nerelius

Martin

Peng

et al. 2008

Biochemical Journal

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“…Control fibrils were isolated from the amyloidotic spleen of a wild hare (Lepus europaeus) [20]. All preparations displayed characteristic red-green dichroism in cross-polarized light microscopy (DMR XA2-QWIN; Leica Microsystems, Milton Keynes, UK) after staining with alkaline alcoholic Congo red [21,22], a fibrillar ultrastructure by negative stain transmission electron microscopy [23] and specific binding by serum amyloid P component [24,25]; their purity and protein content were analysed by reduced SDS-PAGE (ExcelGels; GE Healthcare, Chalfont St. Giles, UK) [16].…”

Section: Amyloid Fibrilsmentioning

confidence: 99%

“…Each batch of immunostaining included positive (CJD brain tissue, including cases with PrP amyloid deposits) and negative (primary antibody substituted with normal human serum) control sections. Separate adjacent sections stained with Congo red [21,22] were examined alongside the above by a neuropathologist and a biomedical scientist with extensive experience in interpretation of PrP immunohistochemistry.…”

Section: Ga Tennent Et Almentioning

confidence: 99%

Disease‐associated prion protein is not detectable in human systemic amyloid deposits

Tennent

Head

Bishop

et al. 2007

The Journal of Pathology

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Cerebral and cardiac amyloid deposits have been reported after scrapie infection in transgenic mice expressing variant prion protein (PrP C ) lacking the glycophosphatidylinositol anchor. The amyloid fibril protein in the systemic amyloid deposits was not characterized, and there is no clinical or pathological association between prion diseases and systemic amyloidosis in humans. Nevertheless, in view of the potential clinical significance of these murine observations, we tested both human amyloidotic tissues and isolated amyloid fibrils for the presence of PrP Sc , the prion protein conformation associated with transmissible spongiform encephalopathy (TSE). We also sequenced the complete prion protein gene, PRNP, in amyloidosis patients. No specific immunohistochemical staining for PrP Sc was obtained in the amyloidotic cardiac and other visceral tissues of patients with different types of systemic amyloidosis. No protease-resistant prion protein, PrP res , was detectable by Western blotting of amyloid fibrils isolated from cardiac and other systemic amyloid deposits. Only the complete normal wild-type PRNP gene sequence was identified, including the usual distribution of codon 129 polymorphisms. These reassuringly negative results do not support the idea that there is any relationship of prions or TSE with human systemic amyloidosis, including cardiac amyloid deposition.

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“…Alginate‐embedded formalin‐fixed slabs and islets from the pancreas donors were stained with Congo red according to Puchtler and Sweat,12 and the presence of amyloid was determined in polarized light 13…”

Section: Methodsmentioning

confidence: 99%

Transplantation of macroencapsulated human islets within the bioartificial pancreas βAir to patients with type 1 diabetes mellitus

Carlsson

Espes

Sedigh

et al. 2018

American Journal of Transplantation

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131

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Macroencapsulation devices provide the dual possibility of immunoprotecting transplanted cells while also being retrievable, the latter bearing importance for safety in future trials with stem cell–derived cells. However, macroencapsulation entails a problem with oxygen supply to the encapsulated cells. The βAir device solves this with an incorporated refillable oxygen tank. This phase 1 study evaluated the safety and efficacy of implanting the βAir device containing allogeneic human pancreatic islets into patients with type 1 diabetes. Four patients were transplanted with 1‐2 βAir devices, each containing 155 000‐180 000 islet equivalents (ie, 1800‐4600 islet equivalents per kg body weight), and monitored for 3‐6 months, followed by the recovery of devices. Implantation of the βAir device was safe and successfully prevented immunization and rejection of the transplanted tissue. However, although beta cells survived in the device, only minute levels of circulating C‐peptide were observed with no impact on metabolic control. Fibrotic tissue with immune cells was formed in capsule surroundings. Recovered devices displayed a blunted glucose‐stimulated insulin response, and amyloid formation in the endocrine tissue. We conclude that the βAir device is safe and can support survival of allogeneic islets for several months, although the function of the transplanted cells was limited (Clinicaltrials.gov: NCT02064309).

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[1] Staining methods for identification of amyloid in tissue

Cited by 270 publications

References 28 publications

Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C

Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C

Disease‐associated prion protein is not detectable in human systemic amyloid deposits

Transplantation of macroencapsulated human islets within the bioartificial pancreas βAir to patients with type 1 diabetes mellitus

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