We are analyzing https://link.springer.com/article/10.1007/s12013-010-9138-4.

Title:
Novel Cell- and Tissue-Based Assays for Detecting Misfolded and Aggregated Protein Accumulation Within Aggresomes and Inclusion Bodies | Cell Biochemistry and Biophysics
Description:
Aggresomes and related inclusion bodies appear to serve as storage depots for misfolded and aggregated proteins within cells, which can potentially be degraded by the autophagy pathway. A homogenous fluorescence-based assay was devised to detect aggregated proteins inside aggresomes and inclusion bodies within an authentic cellular context. The assay employs a novel red fluorescent molecular rotor dye, which is essentially nonfluorescent until it binds to structural features associated with the aggregated protein cargo. Aggresomes and related structures were generated within cultured cells using various potent, cell permeable, proteasome inhibitors: MG-132, lactacystin, epoxomicin and bortezomib, and then selectively detected with the fluorescent probe. Employing the probe in combination with various fluorescein-labeled primary antibodies facilitated co-localization of key components of the autophagy system (ubiquitin, p62, and LC3) with aggregated protein cargo by fluorescence microscopy. Furthermore, cytoplasmic aggregates were highlighted in SK-N-SH human neuroblastoma cells incubated with exogenously supplied amyloid beta peptide 1–42. SMER28, a small molecule modulator of autophagy acting via an mTOR-independent mechanism, prevented the accumulation of amyloid beta peptide within these cells. The described assay allows assessment of the effects of protein aggregation directly in cells, without resorting to the use of non-physiological protein mutations or genetically engineered cell lines. With minor modification, the assay was also adapted to the analysis of frozen or formalin-fixed, paraffin-embedded tissue sections, with demonstration of co-localization of aggregated cargo with β-amyloid and tau proteins in brain tissue sections from Alzheimer’s disease patients.
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Keywords {🔍}

protein, cells, dye, proteostat, aggregated, fluorescence, tissue, inclusion, bodies, proteins, amyloid, cell, aggregation, article, cargo, autophagy, fluorescent, disease, antibody, google, scholar, aggresomes, accumulation, sections, pubmed, flow, cas, fig, pbs, peptide, treated, assay, alzheimers, min, tau, shown, human, cytometry, observed, tht, antibodies, aggregates, incubated, brain, studies, signal, molecular, proteasome, colocalization, microscopy,

Topics {✒️}

fluorescein-labeled p62-reactive antibody fluorescein-labeled lc3-reactive antibody fluorescein-labeled ubiquitin-reactive antibody fluorescein-conjugated p62-reactive antibody characteristic crossed-β-sheet structure tau-reactive monoclonal antibody sk-n-sh cells fluorescein-labeled p62 antibody post-mortem brain tissue anti-fade mounting medium ethics committee/irb approvals fluorescein-labeled antibodies reactive huntingtin-induced cell death schiff acid–base reactions quantitative high-throughput screening article download pdf protein post-translational modifications fluorescein-conjugated antibody directed protein cargo accumulating solvent-exposed side chains paraffin-embedded tissue sections human β-amyloid peptide ubiquitin-conjugated proteins organized microtubule-dependent retrograde transport homogenous fluorescence-based assay fixative-induced auto-fluorescence formalin-fixed paraffin-embedded tissues alexa fluor® 488 bmc cell biology ubiquitin-binding scaffold protein flow cytometry-based analysis fluorescein-labeled p62 membrane-bound vacuolar structures tht-based fluorescence assays microscope slide-mounted specimen human brain tissue ubiquitin–proteasome system ubiquitin-proteasome system enhance bortezomib-induced apoptosis fluorescein-conjugated antibody proteasome-mediated proteolysis beta-sheet conformation full access cell line tau-reactive antibody dye-based approach relative composite image proteasome inhibitor constitutes specific proteasome inhibitor post-translational modifications

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         headline:Novel Cell- and Tissue-Based Assays for Detecting Misfolded and Aggregated Protein Accumulation Within Aggresomes and Inclusion Bodies
         description:Aggresomes and related inclusion bodies appear to serve as storage depots for misfolded and aggregated proteins within cells, which can potentially be degraded by the autophagy pathway. A homogenous fluorescence-based assay was devised to detect aggregated proteins inside aggresomes and inclusion bodies within an authentic cellular context. The assay employs a novel red fluorescent molecular rotor dye, which is essentially nonfluorescent until it binds to structural features associated with the aggregated protein cargo. Aggresomes and related structures were generated within cultured cells using various potent, cell permeable, proteasome inhibitors: MG-132, lactacystin, epoxomicin and bortezomib, and then selectively detected with the fluorescent probe. Employing the probe in combination with various fluorescein-labeled primary antibodies facilitated co-localization of key components of the autophagy system (ubiquitin, p62, and LC3) with aggregated protein cargo by fluorescence microscopy. Furthermore, cytoplasmic aggregates were highlighted in SK-N-SH human neuroblastoma cells incubated with exogenously supplied amyloid beta peptide 1–42. SMER28, a small molecule modulator of autophagy acting via an mTOR-independent mechanism, prevented the accumulation of amyloid beta peptide within these cells. The described assay allows assessment of the effects of protein aggregation directly in cells, without resorting to the use of non-physiological protein mutations or genetically engineered cell lines. With minor modification, the assay was also adapted to the analysis of frozen or formalin-fixed, paraffin-embedded tissue sections, with demonstration of co-localization of aggregated cargo with β-amyloid and tau proteins in brain tissue sections from Alzheimer’s disease patients.
         datePublished:2010-12-05T00:00:00Z
         dateModified:2010-12-05T00:00:00Z
         pageStart:173
         pageEnd:185
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            Inclusion bodies
            Proteasome inhibitor
            Ubiquitin–proteasome system
            Misfolded proteins
            p62 protein
            LC3
            Autophagy
            Alzheimer’s disease
            Protein homeostasis
            Proteostasis
            Biochemistry
            general
            Pharmacology/Toxicology
            Biotechnology
            Cell Biology
            Biological and Medical Physics
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      headline:Novel Cell- and Tissue-Based Assays for Detecting Misfolded and Aggregated Protein Accumulation Within Aggresomes and Inclusion Bodies
      description:Aggresomes and related inclusion bodies appear to serve as storage depots for misfolded and aggregated proteins within cells, which can potentially be degraded by the autophagy pathway. A homogenous fluorescence-based assay was devised to detect aggregated proteins inside aggresomes and inclusion bodies within an authentic cellular context. The assay employs a novel red fluorescent molecular rotor dye, which is essentially nonfluorescent until it binds to structural features associated with the aggregated protein cargo. Aggresomes and related structures were generated within cultured cells using various potent, cell permeable, proteasome inhibitors: MG-132, lactacystin, epoxomicin and bortezomib, and then selectively detected with the fluorescent probe. Employing the probe in combination with various fluorescein-labeled primary antibodies facilitated co-localization of key components of the autophagy system (ubiquitin, p62, and LC3) with aggregated protein cargo by fluorescence microscopy. Furthermore, cytoplasmic aggregates were highlighted in SK-N-SH human neuroblastoma cells incubated with exogenously supplied amyloid beta peptide 1–42. SMER28, a small molecule modulator of autophagy acting via an mTOR-independent mechanism, prevented the accumulation of amyloid beta peptide within these cells. The described assay allows assessment of the effects of protein aggregation directly in cells, without resorting to the use of non-physiological protein mutations or genetically engineered cell lines. With minor modification, the assay was also adapted to the analysis of frozen or formalin-fixed, paraffin-embedded tissue sections, with demonstration of co-localization of aggregated cargo with β-amyloid and tau proteins in brain tissue sections from Alzheimer’s disease patients.
      datePublished:2010-12-05T00:00:00Z
      dateModified:2010-12-05T00:00:00Z
      pageStart:173
      pageEnd:185
      license:https://creativecommons.org/licenses/by-nc/2.0
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         Aggresome
         Inclusion bodies
         Proteasome inhibitor
         Ubiquitin–proteasome system
         Misfolded proteins
         p62 protein
         LC3
         Autophagy
         Alzheimer’s disease
         Protein homeostasis
         Proteostasis
         Biochemistry
         general
         Pharmacology/Toxicology
         Biotechnology
         Cell Biology
         Biological and Medical Physics
         Biophysics
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                  address:
                     name:Enzo Life Sciences, Farmingdale, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Eric Chan
            affiliation:
                  name:Enzo Life Sciences
                  address:
                     name:Enzo Life Sciences, Farmingdale, USA
                     type:PostalAddress
                  type:Organization
            type:Person
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            affiliation:
                  name:Enzo Life Sciences
                  address:
                     name:Enzo Life Sciences, Farmingdale, USA
                     type:PostalAddress
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            type:Person
            name:Lijun Dai
            affiliation:
                  name:Enzo Life Sciences
                  address:
                     name:Enzo Life Sciences, Farmingdale, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Paul W. Sheppard
            affiliation:
                  name:Enzo Life Sciences
                  address:
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                     type:PostalAddress
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            type:Person
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      affiliation:
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            address:
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               type:PostalAddress
            type:Organization
      name:Eric Chan
      affiliation:
            name:Enzo Life Sciences
            address:
               name:Enzo Life Sciences, Farmingdale, USA
               type:PostalAddress
            type:Organization
      name:Thomas P. Nicholson
      affiliation:
            name:Enzo Life Sciences
            address:
               name:Enzo Life Sciences, Farmingdale, USA
               type:PostalAddress
            type:Organization
      name:Lijun Dai
      affiliation:
            name:Enzo Life Sciences
            address:
               name:Enzo Life Sciences, Farmingdale, USA
               type:PostalAddress
            type:Organization
      name:Paul W. Sheppard
      affiliation:
            name:Enzo Life Sciences
            address:
               name:Enzo Life Sciences, Farmingdale, USA
               type:PostalAddress
            type:Organization
      name:Wayne F. Patton
      affiliation:
            name:Enzo Life Sciences
            address:
               name:Enzo Life Sciences, Farmingdale, USA
               type:PostalAddress
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      email:[email protected]
PostalAddress:
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      name:Enzo Life Sciences, Farmingdale, USA
      name:Enzo Life Sciences, Farmingdale, USA
      name:Enzo Life Sciences, Farmingdale, USA
      name:Enzo Life Sciences, Farmingdale, USA
      name:Enzo Life Sciences, Farmingdale, USA

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