Pathological self-aggregation of β(2)-microglobulin

a challenge for protein biophysics.

Gennaro Esposito, Alessandra Corazza, Vittorio Bellotti

    Research output: Contribution to journalReview article

    Abstract

    The pathological aggregation of b(2)-microglobulin (b2m) is examined starting from the relevance of some structural aspects of the protein. The systemic deposition of b2m fibrils has been ascribed to several factors, but no conclusive evidence emerged so far. The characterization of b2m aggregates by direct investigation through electron microscopy, atomic force microscopy, solid state NMR and other solid state techniques provides important structural and morphological information on the assembly, but no clues about the mechanism of the aggregation process. The most relevant mechanistic hypotheses are critically reviewed. In addition to the mechanisms exclusively based on structural features, also the recently reported prion-like conversion is analyzed and shown to hardly comply with some established conditions of the fibrillogenic process. An alternative mechanism is recalled that does not require rare events and involves only the full-length protein in proximity of collagen, i.e. the environment that physiologically supports deposition.

    Original languageEnglish (US)
    Pages (from-to)165-183
    Number of pages19
    JournalSub-Cellular Biochemistry
    Volume65
    StatePublished - Dec 1 2012

    Fingerprint

    Biophysics
    Agglomeration
    Atomic Force Microscopy
    Prions
    Electron microscopy
    Atomic force microscopy
    Electron Microscopy
    Proteins
    Collagen
    Nuclear magnetic resonance

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology
    • Cancer Research

    Cite this

    Pathological self-aggregation of β(2)-microglobulin : a challenge for protein biophysics. / Esposito, Gennaro; Corazza, Alessandra; Bellotti, Vittorio.

    In: Sub-Cellular Biochemistry, Vol. 65, 01.12.2012, p. 165-183.

    Research output: Contribution to journalReview article

    Esposito, Gennaro ; Corazza, Alessandra ; Bellotti, Vittorio. / Pathological self-aggregation of β(2)-microglobulin : a challenge for protein biophysics. In: Sub-Cellular Biochemistry. 2012 ; Vol. 65. pp. 165-183.
    @article{83c07ce630b2469a8b10e5e916543357,
    title = "Pathological self-aggregation of β(2)-microglobulin: a challenge for protein biophysics.",
    abstract = "The pathological aggregation of b(2)-microglobulin (b2m) is examined starting from the relevance of some structural aspects of the protein. The systemic deposition of b2m fibrils has been ascribed to several factors, but no conclusive evidence emerged so far. The characterization of b2m aggregates by direct investigation through electron microscopy, atomic force microscopy, solid state NMR and other solid state techniques provides important structural and morphological information on the assembly, but no clues about the mechanism of the aggregation process. The most relevant mechanistic hypotheses are critically reviewed. In addition to the mechanisms exclusively based on structural features, also the recently reported prion-like conversion is analyzed and shown to hardly comply with some established conditions of the fibrillogenic process. An alternative mechanism is recalled that does not require rare events and involves only the full-length protein in proximity of collagen, i.e. the environment that physiologically supports deposition.",
    author = "Gennaro Esposito and Alessandra Corazza and Vittorio Bellotti",
    year = "2012",
    month = "12",
    day = "1",
    language = "English (US)",
    volume = "65",
    pages = "165--183",
    journal = "Sub-Cellular Biochemistry",
    issn = "0306-0225",
    publisher = "Plenum Publishers",

    }

    TY - JOUR

    T1 - Pathological self-aggregation of β(2)-microglobulin

    T2 - a challenge for protein biophysics.

    AU - Esposito, Gennaro

    AU - Corazza, Alessandra

    AU - Bellotti, Vittorio

    PY - 2012/12/1

    Y1 - 2012/12/1

    N2 - The pathological aggregation of b(2)-microglobulin (b2m) is examined starting from the relevance of some structural aspects of the protein. The systemic deposition of b2m fibrils has been ascribed to several factors, but no conclusive evidence emerged so far. The characterization of b2m aggregates by direct investigation through electron microscopy, atomic force microscopy, solid state NMR and other solid state techniques provides important structural and morphological information on the assembly, but no clues about the mechanism of the aggregation process. The most relevant mechanistic hypotheses are critically reviewed. In addition to the mechanisms exclusively based on structural features, also the recently reported prion-like conversion is analyzed and shown to hardly comply with some established conditions of the fibrillogenic process. An alternative mechanism is recalled that does not require rare events and involves only the full-length protein in proximity of collagen, i.e. the environment that physiologically supports deposition.

    AB - The pathological aggregation of b(2)-microglobulin (b2m) is examined starting from the relevance of some structural aspects of the protein. The systemic deposition of b2m fibrils has been ascribed to several factors, but no conclusive evidence emerged so far. The characterization of b2m aggregates by direct investigation through electron microscopy, atomic force microscopy, solid state NMR and other solid state techniques provides important structural and morphological information on the assembly, but no clues about the mechanism of the aggregation process. The most relevant mechanistic hypotheses are critically reviewed. In addition to the mechanisms exclusively based on structural features, also the recently reported prion-like conversion is analyzed and shown to hardly comply with some established conditions of the fibrillogenic process. An alternative mechanism is recalled that does not require rare events and involves only the full-length protein in proximity of collagen, i.e. the environment that physiologically supports deposition.

    UR - http://www.scopus.com/inward/record.url?scp=84894446315&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=84894446315&partnerID=8YFLogxK

    M3 - Review article

    VL - 65

    SP - 165

    EP - 183

    JO - Sub-Cellular Biochemistry

    JF - Sub-Cellular Biochemistry

    SN - 0306-0225

    ER -