Micropurification techniques in the analysis of amyloid proteins

Kaplan, Batia

doi:10.1136/jcp.56.2.86

Cited by 27 publications

(15 citation statements)

References 47 publications

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“…The biochemical micromethods of extraction and characterization of amyloid fibrils applied here were used by us previously and were found to be helpful when revealing rare amyloid types or when the immunohistochemical findings were either unexpected or questionable [13,15,16]. In the present case, these techniques aided in achieving a precise diagnosis of the disorder.…”

Section: Discussionmentioning

confidence: 85%

Co-deposition of amyloidogenic immunoglobulin light and heavy chains in localized pulmonary amyloidosis

et al. 2005

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Localized pulmonary amyloidosis is a rare condition whose pathogenesis is insufficiently understood. In the present study, we report a case of localized pulmonary amyloidosis associated with lung-restricted lymphoplasmacytoid lymphoma, monoclonal for immunoglobulin (Ig) G lambda (lambda). Biochemical microtechniques have been applied for extraction, purification, and characterization of amyloid proteins. Surprisingly, chemical analysis of these proteins revealed a not-previously-described case of combined deposits containing Ig fragments of gamma heavy chain (variable domain) and lambda light chain (constant domain). In view of the absence of circulating monoclonal Ig, this case supports the hypothesis that localized amyloid is formed by local plasmacytoid cells.

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Section: Discussionmentioning

confidence: 85%

Co-deposition of amyloidogenic immunoglobulin light and heavy chains in localized pulmonary amyloidosis

et al. 2005

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“…Extraction of amyloid fibril proteins from frozen and formalinfixed tissues or from amyloid-containing histopathological tissue sections followed by immunostaining or amino acid sequence analyses is another useful way to characterize amyloid deposits [62][63][64], especially in cases when the immunohistochemical data are negative or inconclusive.…”

Section: Other Diagnostic Methodsmentioning

confidence: 99%

Diagnosis and Therapeutic Approaches to Transthyretin Amyloidosis

Ando

Ueda

2012

CMC

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Hereditary amyloidogenic transthyretin (TTR) (ATTR) amyloidosis is an autosomal dominant form of fatal hereditary amyloidosis. Owing to progress in biochemical and molecular genetic analyses, this disease is now believed to occur worldwide. As of today, reports of about 120 different points of single or double mutations, or a deletion in the TTR gene have been reported, and several different phenotypes of ATTR amyloidosis have been documented. In addition, since liver transplantation has been established to halt the progression of hereditary ATTR amyloidosis in the early stage, rapid and reliable diagnostic system for ATTR amyloidosis is needed. On the other hand, senile systemic amyloidosis (SSA) derived from wild-type (WT) TTR affects primarily in the heart and lungs and occasionally in carpal ligaments in the elderly. To perform accurate diagnosis and effective treatments, we should distinguish between hereditary ATTR amyloidosis and SSA by means of genetic and proteomic analyses. The liver transplantation for hereditary ATTR amyloidosis has become a well-established treatment, because the main source of serum variant TTR is shut out. However, this treatment has several problems, such as expensive medical costs, lifelong administration of immunosuppressants, non-indication for the mutated-TTR gene carriers without clinical symptoms, shortage of liver donors, and further development of cardiac and ocular disorders. Therefore, we and other ATTR amyloidosis research groups have been investigating the possibility of stabilization of variant TTR, gene therapy, and immunotherapy for ATTR amyloidosis on the basis of TTR amyloid formation mechanism. We present here the current diagnostic procedure and therapeutic approaches for the disease.

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“…36,37 In fact, previous biochemical studies on Ab 2 M proteins were performed using larger amounts of fresh (unfixed) tissues obtained at autopsy 5,8,12 or at carpal tunnel release operations. 4,10 In these studies, the classical amyloid isolation methods, which include the water extraction method of Pras 10,12,38 and the guanidine hydrochloride solubilization technique, 4,5,8 were successfully used, but these methods were found unsuitable for biochemical examination of small fixed biopsy specimens.…”

Section: Discussionmentioning

confidence: 99%

Gastrointestinal β2microglobulin amyloidosis in hemodialysis patients: biochemical analysis of amyloid proteins in small formalin-fixed paraffin-embedded tissue specimens

et al. 2005

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We present here a first report on the biochemical analysis of intestinal amyloid deposits found in two cases of hemodialysis-related amyloidosis. A new microtechnique was applied for extraction and immunochemical/ chemical characterization of amyloid proteins in small amounts of fixed tissue, thus allowing precise identification of b 2 microglobulin amyloid (Ab 2 M) in both cases studied. The molecular mass of the identified amyloid b 2 M was close to that of intact b 2 M (12 kDa), with no evidence of the products of proteolytic fragmentation of these molecules. The isoelectrofocusing of the purified Ab 2 M demonstrated a shift to more acidic pI as compared to the normal b 2 M analyzed under the same experimental conditions. The obtained data suggest that the intestinal amyloid deposits in dialysis-related amyloidosis contain disease-specific b 2 M isoforms, which could play a role in the pathogenesis of amyloid disease. The new methodology used might be useful in obtaining precise diagnosis of amyloidosis that is necessary for appropriate therapy, and also provide new important information on the chemical structure of amyloid proteins.

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Micropurification techniques in the analysis of amyloid proteins

Cited by 27 publications

References 47 publications

Co-deposition of amyloidogenic immunoglobulin light and heavy chains in localized pulmonary amyloidosis

Co-deposition of amyloidogenic immunoglobulin light and heavy chains in localized pulmonary amyloidosis

Diagnosis and Therapeutic Approaches to Transthyretin Amyloidosis

Gastrointestinal β2microglobulin amyloidosis in hemodialysis patients: biochemical analysis of amyloid proteins in small formalin-fixed paraffin-embedded tissue specimens

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