Retinal anatomy and function of the transthyretin null mouse

被引:15
作者
Bui, BV
Armitage, JA
Fletcher, EL
Richardson, SJ
Schreiber, G
Vingrys, AJ
机构
[1] Univ Melbourne, Dept Optometry & Vis Sci, Carlton, Vic 3053, Australia
[2] Univ Melbourne, Russell Grimwade Sch Biochem & Mol Biol, Parkville, Vic 3010, Australia
基金
英国医学研究理事会; 澳大利亚研究理事会;
关键词
vitamin A; retina; photoreceptor; retinal degeneration; mouse; electroretinogram (ERG); transthyretin (TTR);
D O I
10.1006/exer.2001.1070
中图分类号
R77 [眼科学];
学科分类号
100212 ;
摘要
Vitamin A (retinol) is vital for the normal development and function of many tissues in the body including the eye. The purpose of this project was to characterize the retinal anatomy and function of the transthyretin (TTR) null mouse. Mice lacking TTR have been constructed by homologous recombination. Immunocytochemistry was performed to localize short and mid-long wavelength cone opsins as well as morphological examination of the entire retina In wild-type and TTR null mice. Visual function was assessed using the electroretinogram (ERG) and resulting waveforms were analysed in terms of receptoral and postreceptoral components, Retinal morphology of the TTR null mouse was normal. In addition, short and mid-long wavelength cone opsins were localized normally in both TTR null and wild-type retinae. Consistent with these findings, TTR null mice show no anomalies of receptoral (P3) nor post-receptoral (b-wave) ERG components compared with wild-type mice, The results suggest that although circulating plasma levels of retinol and retinol binding protein (RBP) are extremely low, this reduction has little effect on the retinal structure or function of the TTR null mouse. These data are consistent with the existence of mechanisms for the transport of retinol to the retina independent of the classical retinol-RBP-TTR complex. (C) 2001 Academic Press.
引用
收藏
页码:651 / 659
页数:9
相关论文
共 48 条
[1]  
[Anonymous], 1997, EYE VISUAL OPTICAL I, DOI DOI 10.1017/CBO9780511609541
[2]  
BEMI R, 1994, J BIOL CHEM, V269, P23395
[3]   PREALBUMIN AND RETINOL BINDING-PROTEIN SERUM CONCENTRATIONS IN THE INDIANA TYPE HEREDITARY AMYLOIDOSIS [J].
BENSON, MD ;
DWULET, FE .
ARTHRITIS AND RHEUMATISM, 1983, 26 (12) :1493-1498
[4]  
Biesalski HK, 1999, AM J CLIN NUTR, V69, P931
[5]  
BIRCH DG, 1995, INVEST OPHTH VIS SCI, V36, P1603
[6]   STRUCTURE OF PRE-ALBUMIN - SECONDARY, TERTIARY AND QUATERNARY INTERACTIONS DETERMINED BY FOURIER REFINEMENT AT 1.8-A [J].
BLAKE, CCF ;
GEISOW, MJ ;
OATLEY, SJ ;
RERAT, B ;
RERAT, C .
JOURNAL OF MOLECULAR BIOLOGY, 1978, 121 (03) :339-356
[7]   RETINOL-BINDING PROTEIN - THE SERUM TRANSPORT PROTEIN FOR VITAMIN-A [J].
BLANER, WS .
ENDOCRINE REVIEWS, 1989, 10 (03) :308-316
[8]   TRANSPORT AND STORAGE OF VITAMIN-A [J].
BLOMHOFF, R ;
GREEN, MH ;
BERG, T ;
NORUM, KR .
SCIENCE, 1990, 250 (4979) :399-404
[9]  
BRETON ME, 1994, INVEST OPHTH VIS SCI, V35, P295
[10]   VISUAL CYCLE IN THE MAMMALIAN EYE - RETINOID-BINDING PROTEINS AND THE DISTRIBUTION OF 11-CIS RETINOIDS [J].
BRIDGES, CDB ;
ALVAREZ, RA ;
FONG, SI ;
GONZALEZFERNANDEZ, F ;
LAM, DMK ;
LIOU, GI .
VISION RESEARCH, 1984, 24 (11) :1581-+