Abstract | PURPOSE: METHODS: RESULTS: A protein was identified in two corneas with FSCA that was not present in normal corneas or in corneas with other disorders. The amino acid sequences of two peptides derived from this protein were identical to portions of lactoferrin. The unique protein reacted with rabbit antihuman lactoferrin after Western blotting. The presence of lactoferrin in the amyloid within affected corneas was confirmed using the immunoperoxidase method on formalin-fixed, paraffin-embedded tissue sections and lactoferrin antiserum. CONCLUSIONS: Corneal tissue with FSCA contains lactoferrin, and this is the first form of amyloidosis found to be associated with this protein. Because lactoferrin is a product of lacrimal glands, the corneal lactoferrin may be derived from the tears. Because the gene for lactoferrin is on chromosome 3 (3q21-q23), this locus is a potential site for the FSCA gene.
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Authors | G K Klintworth, Z Valnickova, R A Kielar, K H Baratz, R J Campbell, J J Enghild |
Journal | Investigative ophthalmology & visual science
(Invest Ophthalmol Vis Sci)
Vol. 38
Issue 13
Pg. 2756-63
(Dec 1997)
ISSN: 0146-0404 [Print] United States |
PMID | 9418728
(Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Amyloid
- Eye Proteins
- Lactoferrin
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Topics |
- Adolescent
- Amino Acid Sequence
- Amyloid
(metabolism)
- Amyloidosis
(genetics, metabolism, pathology)
- Blotting, Western
- Chromatography, High Pressure Liquid
- Corneal Diseases
(genetics, metabolism, pathology)
- Electrophoresis, Polyacrylamide Gel
- Epithelium, Corneal
(chemistry, metabolism, pathology)
- Eye Proteins
(genetics, isolation & purification, metabolism)
- Humans
- Immunoenzyme Techniques
- Lactoferrin
(genetics, isolation & purification, metabolism)
- Male
- Molecular Sequence Data
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