Literature DB >> 3658350

Prealbumin. A major constituent of vitreous amyloid.

P D Gorevic1, M M Rodrigues, W H Spencer, P C Munoz, A W Allen, A Z Verne.   

Abstract

Vitreous amyloid may be the presenting clinical manifestation of types 1 and 2 familial amyloidotic polyneuropathy or complicate the course of these syndromes. Recent studies have shown that the major subunit protein composing amyloid fibrils in these conditions is a variant or abnormal prealbumin molecule and that affected individuals have low levels of this protein in their blood. The authors studied material obtained at vitrectomy from two cases of vitreous amyloid. One of these was nonfamilial and the other familial. Two-dimensional gels of solubilized protein from pelleted and washed vitreous amyloid in both cases were found to consist of material with the molecular weight and isofocusing coordinates of prealbumin monomer. Reactivity of fibrils with a monospecific antiserum to prealbumin was confirmed by colloidal gold immunoelectron microscopy. Non-familial as well as familial vitreous amyloid may in fact be systemic forms of amyloidosis due to deposition of prealbumin which can be characterized by biochemical or immunohistologic studies of material obtained at vitrectomy.

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Year:  1987        PMID: 3658350     DOI: 10.1016/s0161-6420(87)33531-6

Source DB:  PubMed          Journal:  Ophthalmology        ISSN: 0161-6420            Impact factor:   12.079


  3 in total

1.  Ultrastructural immunolabelling of amyloid fibrils in acquired and hereditary amyloid neuropathies.

Authors:  D Adams; G Said
Journal:  J Neurol       Date:  1996-01       Impact factor: 4.849

2.  A homozygous transthyretin variant associated with senile systemic amyloidosis: evidence for a late-onset disease of genetic etiology.

Authors:  D R Jacobson; P D Gorevic; J N Buxbaum
Journal:  Am J Hum Genet       Date:  1990-07       Impact factor: 11.025

3.  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

  3 in total

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