From candelas to photoisomerizations in the mouse eye by rhodopsin bleaching in situ and the light-rearing dependence of the major components of the mouse ERG

被引:178
作者
Lyubarsky, AL [1 ]
Daniele, LL [1 ]
Pugh, EN [1 ]
机构
[1] Univ Penn, Dept Ophthalmol, FM Kirby Ctr Mol Ophthalmol, Philadelphia, PA 19104 USA
关键词
rhodopsin bleaching; electroretinogram; a-wave; b-wave; rods; cones;
D O I
10.1016/j.visres.2004.09.019
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
To quantify the rate at which light in a ganzfeld produces photoisomerizations in mouse rods in situ, we measured the rate of rhodopsin bleaching in eyes of recently euthanized mice with fully dilated pupils. The amount of rhodopsin declined as a first-order (exponential) function of the duration of the exposure at the luminance of 920 scot cd m(-2): the rate constants of bleaching were 8.3 x 10(-6) and 2.8 x 10(-5) s(-1) (scot cd(-1) m(-1))(-1) for C57B1/6 and 129P3/J mice, respectively. When the similar to3-fold difference in effective areas of the pupils of the mice are taken into consideration, the bleaching rates for both strains become essentially the same, 2.6 x 10(-6) fraction rhodopsin (scot Td s)(-1). Assuming 7 x 10(7) rhodopsin molecules per rod, this bleaching rate yields the result that a flash of 1 scot Td s produces 181 photoisomerizations per rod, a value close to that derived from analysis of the collecting area of the rod for axially propagating light. We measured the electroretinograms of mice of the two strains reared under controlled illumination conditions (2 and 100 lux), and compared their properties, using the calibrations to determine the absolute sensitivities of the b-wave and a-waves. The intensity that produces a half-saturating rod b-wave response is 0.3-0.6 photoisomerizations rod(-1), and the amplification constant of the rod a-wave is 5-6 s(-2) photoisomerization(-1), with little dependence on the strain. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:3235 / 3251
页数:17
相关论文
共 42 条
[1]   DENSITY AND PHOTOSENSITIVITY OF HUMAN RHODOPSIN IN LIVING RETINA [J].
ALPERN, M ;
PUGH, EN .
JOURNAL OF PHYSIOLOGY-LONDON, 1974, 237 (02) :341-370
[2]   RHODOPSIN KINETICS IN HUMAN EYE [J].
ALPERN, M .
JOURNAL OF PHYSIOLOGY-LONDON, 1971, 217 (22) :447-&
[3]   SELF-SCREENING OF RHODOPSIN IN ROD OUTER SEGMENTS [J].
ALPERN, M ;
FULTON, AB ;
BAKER, BN .
VISION RESEARCH, 1987, 27 (09) :1459-+
[4]  
Barlow H B, 1971, Vision Res, VSuppl 3, P87
[5]   THE PHOTOCURRENT, NOISE AND SPECTRAL SENSITIVITY OF RODS OF THE MONKEY MACACA-FASCICULARIS [J].
BAYLOR, DA ;
NUNN, BJ ;
SCHNAPF, JL .
JOURNAL OF PHYSIOLOGY-LONDON, 1984, 357 (DEC) :575-607
[6]  
BAYLOR DA, 1979, J PHYSIOL-LONDON, V288, P613
[7]  
BRETON ME, 1994, INVEST OPHTH VIS SCI, V35, P295
[8]  
CARTERDAWSON LD, 1979, J COMP NEUROL, V188, P245, DOI 10.1002/cne.901880204
[9]   Disruption of the 11-cis-retinol dehydrogenase gene leads to accumulation of cis-retinols and cis-retinyl esters [J].
Driessen, CAGG ;
Winkens, HJ ;
Hoffmann, K ;
Kuhlmann, LD ;
Janssen, BPM ;
van Vugt, AHM ;
Van Hooser, JP ;
Wieringa, BE ;
Deutman, AF ;
Palczewski, K ;
Ruether, K ;
Janssen, JJM .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (12) :4275-4287
[10]  
ENOCH JM, 1981, VERTEBRATE PHOTORECE, P139