Literature DB >> 3090496

Relation of vitreous amyloidosis to prealbumin.

O Sandgren, P Westermark, S Stenkula.   

Abstract

Amyloid fibrils were isolated from the vitreous of 9 patients with familial amyloidosis. The material of all patients contained proteins reacting in double immunodiffusion with an antiserum against an amyloid protein which previously has been shown to be prealbumin-related. Two out of five tested vitreous amyloid materials also showed a reaction of identity with antihuman prealbumin. It was shown by electrophoresis that the amyloid subunit consisted of two low molecular weight components, one in size similar to prealbumin and one slightly smaller, which appears to be a degradation product of prealbumin. The proportion between the two components seems to vary. It is concluded that besides the presence of an abnormal prealbumin, other factors are of importance for the formation of amyloid precipitates in the vitreous.

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Year:  1986        PMID: 3090496     DOI: 10.1159/000265422

Source DB:  PubMed          Journal:  Ophthalmic Res        ISSN: 0030-3747            Impact factor:   2.892


  2 in total

1.  Systemic senile amyloidosis. Identification of a new prealbumin (transthyretin) variant in cardiac tissue: immunologic and biochemical similarity to one form of familial amyloidotic polyneuropathy.

Authors:  P D Gorevic; F C Prelli; J Wright; M Pras; B Frangione
Journal:  J Clin Invest       Date:  1989-03       Impact factor: 14.808

2.  Amyloid fibril composition within hereditary Val30Met (p. Val50Met) transthyretin amyloidosis families.

Authors:  Ole Bernt Suhr; Jonas Wixner; Intissar Anan; Hans-Erik Lundgren; Priyantha Wijayatunga; Per Westermark; Elisabet Ihse
Journal:  PLoS One       Date:  2019-02-27       Impact factor: 3.240

  2 in total

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