Clinical proteomics for diagnosis and typing of systemic amyloidoses

Francesca Brambilla, Francesca Lavatelli, Giampaolo Merlini, Pierluigi Mauri

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Amyloidoses are characterized by deposition of misfolded proteins as β-pleated sheet fibrils in organs. Despite the similar morphologic appearance of fibrils, at least 28 different proteins have been identified as causative agents of amyloidosis in humans, 14 of which responsible for systemic forms. Correct identification of the amyloidogenic proteins in each patient is crucial for clinical management, in order to avoid misdiagnosis, inappropriate treatment, and to assess the prognosis. Amyloidosis, being essentially a protein deposition disorder, is an attractive venue for the application of proteomics methodologies; among the different possible analytic goals, the most important is the unequivocal diagnosis and typing of the amyloid deposits. Amyloidosis typing has been traditionally based on a multidisciplinary approach, requiring detailed clinical evaluation and immunohistochemical studies together with biochemical and genetic tests. However, drawbacks of immunohistochemistry-based techniques have driven the search for alternative methods for direct amyloid typing. In particular, MS-based proteomics, recently introduced in the clinical practice with or without the previous 2DE separation of proteins, has revolutionized amyloid typing. This review provides a description of current proteomics methods for the identification of the amyloidogenic proteins, with special attention to the most innovative MS-based techniques.

Original languageEnglish
Pages (from-to)136-143
Number of pages8
JournalProteomics - Clinical Applications
Volume7
Issue number1-2
DOIs
Publication statusPublished - Jan 2013

Fingerprint

Amyloidosis
Proteomics
Amyloid
Amyloidogenic Proteins
Proteins
Amyloid Plaques
Diagnostic Errors
Molecular Biology
Deposits
Immunohistochemistry
Therapeutics

Keywords

  • Amyloidosis typing
  • Clinical proteomics
  • Laser microdissection (LMD)
  • MudPIT
  • Quantitative analysis

ASJC Scopus subject areas

  • Clinical Biochemistry

Cite this

Clinical proteomics for diagnosis and typing of systemic amyloidoses. / Brambilla, Francesca; Lavatelli, Francesca; Merlini, Giampaolo; Mauri, Pierluigi.

In: Proteomics - Clinical Applications, Vol. 7, No. 1-2, 01.2013, p. 136-143.

Research output: Contribution to journalArticle

@article{c18a1119b610440ba26180ca73d90b4a,
title = "Clinical proteomics for diagnosis and typing of systemic amyloidoses",
abstract = "Amyloidoses are characterized by deposition of misfolded proteins as β-pleated sheet fibrils in organs. Despite the similar morphologic appearance of fibrils, at least 28 different proteins have been identified as causative agents of amyloidosis in humans, 14 of which responsible for systemic forms. Correct identification of the amyloidogenic proteins in each patient is crucial for clinical management, in order to avoid misdiagnosis, inappropriate treatment, and to assess the prognosis. Amyloidosis, being essentially a protein deposition disorder, is an attractive venue for the application of proteomics methodologies; among the different possible analytic goals, the most important is the unequivocal diagnosis and typing of the amyloid deposits. Amyloidosis typing has been traditionally based on a multidisciplinary approach, requiring detailed clinical evaluation and immunohistochemical studies together with biochemical and genetic tests. However, drawbacks of immunohistochemistry-based techniques have driven the search for alternative methods for direct amyloid typing. In particular, MS-based proteomics, recently introduced in the clinical practice with or without the previous 2DE separation of proteins, has revolutionized amyloid typing. This review provides a description of current proteomics methods for the identification of the amyloidogenic proteins, with special attention to the most innovative MS-based techniques.",
keywords = "Amyloidosis typing, Clinical proteomics, Laser microdissection (LMD), MudPIT, Quantitative analysis",
author = "Francesca Brambilla and Francesca Lavatelli and Giampaolo Merlini and Pierluigi Mauri",
year = "2013",
month = "1",
doi = "10.1002/prca.201200097",
language = "English",
volume = "7",
pages = "136--143",
journal = "Proteomics - Clinical Applications",
issn = "1862-8346",
publisher = "Wiley-VCH Verlag",
number = "1-2",

}

TY - JOUR

T1 - Clinical proteomics for diagnosis and typing of systemic amyloidoses

AU - Brambilla, Francesca

AU - Lavatelli, Francesca

AU - Merlini, Giampaolo

AU - Mauri, Pierluigi

PY - 2013/1

Y1 - 2013/1

N2 - Amyloidoses are characterized by deposition of misfolded proteins as β-pleated sheet fibrils in organs. Despite the similar morphologic appearance of fibrils, at least 28 different proteins have been identified as causative agents of amyloidosis in humans, 14 of which responsible for systemic forms. Correct identification of the amyloidogenic proteins in each patient is crucial for clinical management, in order to avoid misdiagnosis, inappropriate treatment, and to assess the prognosis. Amyloidosis, being essentially a protein deposition disorder, is an attractive venue for the application of proteomics methodologies; among the different possible analytic goals, the most important is the unequivocal diagnosis and typing of the amyloid deposits. Amyloidosis typing has been traditionally based on a multidisciplinary approach, requiring detailed clinical evaluation and immunohistochemical studies together with biochemical and genetic tests. However, drawbacks of immunohistochemistry-based techniques have driven the search for alternative methods for direct amyloid typing. In particular, MS-based proteomics, recently introduced in the clinical practice with or without the previous 2DE separation of proteins, has revolutionized amyloid typing. This review provides a description of current proteomics methods for the identification of the amyloidogenic proteins, with special attention to the most innovative MS-based techniques.

AB - Amyloidoses are characterized by deposition of misfolded proteins as β-pleated sheet fibrils in organs. Despite the similar morphologic appearance of fibrils, at least 28 different proteins have been identified as causative agents of amyloidosis in humans, 14 of which responsible for systemic forms. Correct identification of the amyloidogenic proteins in each patient is crucial for clinical management, in order to avoid misdiagnosis, inappropriate treatment, and to assess the prognosis. Amyloidosis, being essentially a protein deposition disorder, is an attractive venue for the application of proteomics methodologies; among the different possible analytic goals, the most important is the unequivocal diagnosis and typing of the amyloid deposits. Amyloidosis typing has been traditionally based on a multidisciplinary approach, requiring detailed clinical evaluation and immunohistochemical studies together with biochemical and genetic tests. However, drawbacks of immunohistochemistry-based techniques have driven the search for alternative methods for direct amyloid typing. In particular, MS-based proteomics, recently introduced in the clinical practice with or without the previous 2DE separation of proteins, has revolutionized amyloid typing. This review provides a description of current proteomics methods for the identification of the amyloidogenic proteins, with special attention to the most innovative MS-based techniques.

KW - Amyloidosis typing

KW - Clinical proteomics

KW - Laser microdissection (LMD)

KW - MudPIT

KW - Quantitative analysis

UR - http://www.scopus.com/inward/record.url?scp=84872788378&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84872788378&partnerID=8YFLogxK

U2 - 10.1002/prca.201200097

DO - 10.1002/prca.201200097

M3 - Article

VL - 7

SP - 136

EP - 143

JO - Proteomics - Clinical Applications

JF - Proteomics - Clinical Applications

SN - 1862-8346

IS - 1-2

ER -