Lactoferrin Glu561Asp facilitates secondary amyloidosis in the cornea

British Journal of Ophthalmology

Volumn 89, Issue 6, 2005, Pages 684-688

  Araki Sasaki, K ^a   Ando, Yukio ^a   Nakamura, M ^a   Kitagawa, K ^b   Ikemizu, S ^a   Kawaji, T ^a   Yamashita, T ^a   Ueda, M ^a   Hirano, K ^c   Yamada, M ^d   Matsumoto, K ^a   Kinoshita, S ^e   Tanihara, H ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

^b KANAZAWA MEDICAL UNIVERSITY   (Japan)

^c JAPANESE RED CROSS NAGOYA FIRST HOSPITAL   (Japan)

^d NATIONAL HOSPITAL ORGANIZATION TOKYO MEDICAL CENTER   (Japan)

^e KYOTO PREFECTURAL UNIVERSITY OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CONGO RED; GLUTAMIC ACID; LACTOFERRIN;

ADULT; AGED; AMYLOIDOSIS; ARTICLE; CLINICAL ARTICLE; CORNEA; CORNEA DISEASE; CORNEA EPITHELIUM; CORNEAL BIOPSY; DNA SEQUENCE; FEMALE; GENETIC ANALYSIS; HUMAN; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; IMMUNOREACTIVITY; INDUCED MUTATION; MALE; PATHOGENESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; RESTRICTION MAPPING; SINGLE STRAND CONFORMATION POLYMORPHISM; TRICHIASIS;

ADOLESCENT; ADULT; AGED; AGED, 80 AND OVER; AMYLOIDOSIS; CHILD; CONGO RED; CORNEAL DISEASES; EYELASHES; EYELID DISEASES; FEMALE; GENE FREQUENCY; GENETIC PREDISPOSITION TO DISEASE; HAIR DISEASES; HUMANS; IMMUNOENZYME TECHNIQUES; LACTOFERRIN; MALE; MIDDLE AGED; POLYMERASE CHAIN REACTION; POLYMORPHISM, SINGLE-STRANDED CONFORMATIONAL; SEQUENCE ANALYSIS, DNA;

EID: 20344373420     PISSN: 00071161     EISSN: None     Source Type: Journal    
DOI: 10.1136/bjo.2004.056804     Document Type: Article

References (27)

1. Glenner GG, Page DL. Amyloid, amyloidosis, and amyloidogenesis. Int Rev Exp Pathol 1976;15:1-92.
2. Tan SY, Pepys MB. Amyloidosis. Histopathology 1994;25:403-14.
3. Westermark P, Benson MD, Buxbaum JN, et al. Amyloid fibril protein nomenclature-2002. Amyloid 2002;9:197-200.
4. Gorevic PD, Munoz PC, Gorgone G, et al. Amyloidosis due to a mutation of the gelsolin gene in an American family with lattice corneal dystrophy type II. N Engl J Med 1991;325:1780-5.
5. Colon W, Lai Z, McCutchen SL, et al. FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formation. Ciba Found Symp 1996;199:228-38.
6. Goldsteins G, Persson H, Andersson K, et al. Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants. Proc Natl Acad Sci USA 1999;96:3108-13.
7. Sandgren O. Ocular amyloidosis with special reference to the hereditary forms with vitreous involvement. Surv Ophthalmol 1995;40:173-96.
8. Ando E, Ando Y, Okamura R, et al. Ocular manifestation of familial amyloidotic polyneuropathy type I: long term follow up. Br J Ophthalmol 1997;81:295-8.
9. Rodrigues M, Zimmerman LE. Secondary amyloidosis in ocular leprosy. Arch Ophthalmol 1971;85:277-9.
10. Hayasaka S, Setogawa T, Ohmura M. Secondary localized amyloidosis of the cornea caused by trichiasis. Ophthalmologica 1987;194:77-81.
11. Watts J, Frank H. Corneal amyloidosis. Br J Ophthalmol 1989;73:674-6.
12. Hill JC, Maske R, Bowen RM. Secondary localized amyloidosis of the cornea associated with tertiary syphilis. Cornea 1990;9:98-101.
13. Dutt S, Elner VM, Soong HK, et al. Secondary localized amyloidosis in interstitial keratitis. Clinicopathologic findings. Ophthalmology 1992;99:817-23.
14. Aso K, Wakakura M. Corneal amyloidosis complicated by trichiasis. Immunohistochemical identification of the amyloid light chain protein. Jpn J Ophthalmol 2000;44:191.
15. Kigasawa K, Mashima Y, Ogata T, et al. A histopathological study of corneal amyloidosis secondary to trichiasis. Nippon Ganka Gakkai Zassni 1996;100:394-400.
16. Ando Y, Nakamura M, Kai H, et al. A novel localized amyloidosis associated with lactoferrin in the cornea. Lab Invest 2002;82:757-66.
17. Okuda T, Matsumoto K, Ando Y, et al. A case of corneal lactoferrin amyloidosis secondary to trichiasis. Nippon Ganka Gakkai Zasshi 2003;107:105-8.
18. Madisen L, Hoar DI, Holroyd CD, et al. DNA banking: the effects of storage of blood and isolated DNA on the integrity of DNA. Am J Med Genet 1987;27:379-90.
19. Orita M, Suzuki Y, Sekiya T, et al. Rapid and sensitive detection of point mutations and DNA polymorphisms using the polymerase chain reaction. Genomics 1989;5:874-9.
20. Kim SJ, Yu DY, Pak KW, et al. Structure of the human lactoferrin gene and its chromosomal localization. Mol Cells 1998;8:663-8.
21. El-Salhy M, Suhr O. Endocrine cells in rectal biopsies from patients with familial amyloidotic polyneuropathy. Scand J Gastroenterol 1996;31:68-73.
22. Klintworth GK, Valnickova Z, Kielar RA, et al. Familial subepithelial corneal amyloidosis-a lactoferrin-related amyloidosis. Invest Ophthalmol Vis Sci 1997;38:2756-63.
23. Baker EN, Anderson BF, Baker HM, et al. Three-dimensional structure of lactoferrin. Implications for function, including comparisons with transferrin. Adv Exp Med Biol 1998;443:1-14.
24. Tsunoda I, Awano H, Kayama H, et al. Idiopathic AA amyloidosis manifested by autonomic neuropathy, vestibulocochleopathy, and lattice corneal dystrophy. J Neurol Neurosurg Psychiatry 1994;57:635-7.
25. Tsujikawa M, Kurahashi H, Tanaka T, et al. Identification of the gene responsible for gelatinous drop-like corneal dystrophy. Nat Genet 1999;21:420-3.
26. Tasa G, Kals J, Muru K, et al. A novel mutation in the M1S1 gene responsible for gelatinous droplike corneal dystrophy. Invest Ophthalmol Vis Sci 2001;42:2762-4.
27. Stewart H, Black GC, Donnai D, et al. A mutation within exon 14 of the TGFBI (BIGH3) gene on chromosome 5q31 causes an asymmetric, late-onset form of lattice corneal dystrophy. Ophthalmology 1999;106:964-70.