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Updated: Aug 10, 2026

Dissection of Human Vitreous Body Elements for Proteomic Analysis
Published on: January 23, 2011
Prealbumin. A major constituent of vitreous amyloid
P D Gorevic1, M M Rodrigues, W H Spencer
1Department of Medicine, State University of New York, Stony Brook 11794-8161.
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.
Insights
Vitreous amyloid, linked to familial amyloidotic polyneuropathy, involves abnormal prealbumin protein. This study confirms prealbumin as the key component in both familial and non-familial vitreous amyloid cases.
Area of Science:
- Ophthalmology
- Neurology
- Biochemistry
Background:
- Familial amyloidotic polyneuropathy (types 1 and 2) can present with or be complicated by vitreous amyloid.
- Research indicates abnormal prealbumin is the primary component of amyloid fibrils in these conditions, with affected individuals exhibiting low blood prealbumin levels.
Observation:
- This study analyzed vitreous amyloid samples from two patients, one with non-familial and one with familial amyloidosis.
- Biochemical analysis using two-dimensional gels identified the amyloid protein as prealbumin monomer in both cases.
- Immunoelectron microscopy confirmed the presence of prealbumin fibrils using a specific antiserum.
Findings:
- Vitreous amyloid, in both familial and non-familial forms, is composed of prealbumin.
- The biochemical and immunohistologic characteristics of vitreous amyloid can be determined from samples obtained during vitrectomy.
Implications:
- Vitreous amyloid deposition may indicate systemic prealbumin amyloidosis.
- Vitrectomy samples offer a viable method for diagnosing and characterizing prealbumin amyloidosis, aiding in understanding familial amyloidotic polyneuropathy.
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