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Results for “Retinaldehyde”

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At least 127 records · Page 7Linked to original sources
PubMed2000

Visual pigment reconstitution in intact goldfish retina using synthetic retinaldehyde isomers.

A protocol has been developed for reconstituting visual pigments in intact retinae by delivering synthetic isomers of retinal incorporated in phospholipid vesicles. Calibration curves have been constructed relating the lambda(max) of the native porphyropsins (visual pigments based on 11-cis 3-dehydroretinal) of the rods and four spectral classes of cone in the goldfish, and the equivalent photosensitive pigments regenerated from 11-cis retinal (rhodopsins) and the commercially available isomer, 9-cis retinal (isorhodopsins). The relationship between the lambda(max) of rhodopsins and isorhodopsins appears to be linear, such that the difference in lambda(max) changes sign at about 380 nm. We therefore conclude that the protocol for reconstituting visual pigments with 9-cis retinal is suitable for all classes of vertebrate opsin-based photopigments.

Animals↗
PubMed2001

Visual cycle impairment in cellular retinaldehyde binding protein (CRALBP) knockout mice results in delayed dark adaptation.

Mutations in the human CRALBP gene cause retinal pathology and delayed dark adaptation. Biochemical studies have not identified the primary physiological function of CRALBP. To resolve this, we generated and characterized mice with a non-functional CRALBP gene (Rlbp1(-/-) mice). The photosensitivity of Rlbp1(-/-) mice is normal but rhodopsin regeneration, 11-cis-retinal production, and dark adaptation after illumination are delayed by >10-fold. All-trans-retinyl esters accumulate during the delay indicating that isomerization of all-trans- to 11-cis-retinol is impaired. No evidence of photoreceptor degeneration was observed in animals raised in cyclic light/dark conditions for up to 1 year. Albino Rlbp(-/-) mice are protected from light damage relative to the wild type. These findings support a role for CRALBP as an acceptor of 11-cis-retinol in the isomerization reaction of the visual cycle.

Animals↗
PubMed2004

Expression of retinaldehyde dehydrogenase II and sequential activation of 5' Hoxb genes in the mouse caudal hindbrain.

The precise anterior boundaries of Hox expression domains are critical for correct antero-posterior (A-P) patterning of the vertebrate longitudinal axis. Retinoic acid (RA) signalling has been shown to play an important role in the specification of pre-otic rhombomere boundaries, and in the regulation of 3' Hox expression within this territory. In addition, we recently showed that RA signalling controls 5'Hoxb gene expression in the caudal hindbrain, which had not been discovered before. We show here that the expression domain of these 5'Hoxb genes undergoes a sequential, colinear rostral expansion between E9.5 and E11.5 in the caudal hindbrain, and that this differential expansion occurs just rostrally to the localisation of the transcripts for the RA biosynthetic enzyme Raldh2 in the cervical mesenchyme.

Aldehyde Oxidoreductases↗