2011
DOI: 10.1155/2011/754109
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Proteomics in Molecular Diagnosis: Typing of Amyloidosis

Abstract: Amyloidosis is a group of disorders caused by deposition of misfolded proteins as aggregates in the extracellular tissues of the body, leading to impairment of organ function. Correct identification of the causal amyloid protein is absolutely crucial for clinical management in order to avoid misdiagnosis and inappropriate, potentially harmful treatment, to assess prognosis and to offer genetic counselling if relevant. Current diagnostic methods, including antibody-based amyloid typing, have limited ability to … Show more

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Cited by 27 publications
(28 citation statements)
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“…The approach to amyloid typing has evolved dramatically over the last 30 years, moving from limited, uninformative histology stains through to more specific immunohistochemistry supplemented by genetic analyses and, more recently, direct identification of the amyloid-forming protein in biopsy specimens using liquid chromatography (LC)-coupled tandem mass spectrometry (MS/MS) [2,4]. An obvious limitation of immunohistochemistry is the requirement of quality antibodies to target proteins.…”
Section: Amyloid Typing Methodsmentioning
confidence: 99%
See 1 more Smart Citation
“…The approach to amyloid typing has evolved dramatically over the last 30 years, moving from limited, uninformative histology stains through to more specific immunohistochemistry supplemented by genetic analyses and, more recently, direct identification of the amyloid-forming protein in biopsy specimens using liquid chromatography (LC)-coupled tandem mass spectrometry (MS/MS) [2,4]. An obvious limitation of immunohistochemistry is the requirement of quality antibodies to target proteins.…”
Section: Amyloid Typing Methodsmentioning
confidence: 99%
“…The disease can be localized or systemic and is classified according to the identity of the amyloid fibril-forming protein [1]. Once the presence of amyloidosis is confirmed in a tissue biopsy specimen, it is critical to identify the amyloid type accurately, as management differs substantially depending on the nature and source of the amyloid-forming protein, ranging from supportive care through to aggressive chemotherapy or organ transplantation [2]. With a new era of amyloid therapeutics upon us, such as antisense therapies, transthyretin stabilizers, and anti-amyloid fibril antibodies [3], accurate diagnosis has become more important than ever.…”
Section: Introductionmentioning
confidence: 99%
“…5 Proteomic analysis involves proteolytic cleavage of proteins within microdissected amyloidotic tissue and identification by mass spectometry. 6 This additional tool is being increasingly used in conjunction with immunohistochemistry to identify the amyloid fibril protein.…”
Section: Two Types Of Amyloid In a Single Heartmentioning
confidence: 99%
“…5 Current knowledge of factors influencing ASNase pharmacokinetics is limited. 5,6 Only the presence of inhibitory antibodies that bind asparaginase is known to significantly shorten the half-life of ASNase. 7 In our patient, we found no evidence of an immune response targeting the ASNase.…”
mentioning
confidence: 99%
“…Previously, proteomics was performed by N-terminal Edman degradation, which involved sequencing the proteins present. 62 Aside from being extremely time-consuming, there was also a limit on the number of proteins that can be tested at any one time. Proteomics currently is performed with mass spectrometry, which has the capability for high-throughput and identification of the entire proteome.…”
Section: Proteomicsmentioning
confidence: 99%