Photoreactions of cephalopod rhodopsin.
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Animals↗
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Primary intermediates of rhodopsin studied by low temperature spectrophotometry and laser photolysis. Bathorhodopsin, hypsorhodopsin and photorhodopsin.
The primary photochemical processes of rhodopsin studied by low temperature spectrophotometry and picosecond laser spectroscopy in our group was summarized. Low temperature spectroscopic experiments demonstrated that the retinylidene chromophores of hypso- and bathorhodopsins are in a twisted all-trans forms. Excitation of rhodopsin with 532 nm laser pulse (width: 25 psec) yielded a new bathochromic photoproduct "photorhodopsin"; its spectrum was located at longer wavelengths than that of bathorhodopsin. Photorhodopsin decays to bathorhodopsin with time constants of about 200 psec in squid and 40 psec in cattle. Squid and octopus hypsorhodopsins were produced within 25 psec by high energy pulse, but not by low energy pulse. Thus hypsorhodopsin is produced by two photon reactions (sequential two photochemical reactions) and decayed to bathorhodopsin with time constant of 125 psec.
Animals↗
Squid m-retinochrome. Two forms of metaretinochrome.
When retinochrome absorbs light, it bleaches to m-retinochrome, which may act as a direct supplier of 11-cis-retinal to protein opsin to form rhodopsin. The present experiments were aimed at further elucidating the molecular state of m-retinochrome. Retinochrome and m-retinochome were mixed each with sodium borohydride, subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the resultant fluorescence bands were examined. The reduced retinochrome showed only one band due to N-retinyl protein, whereas the reduced m-retinochrome had two bands. When extracted with successive volumes of n-hexane, m-retinochrome released the 11-cis-retinal chromophore in a time-course consisting of fast and slow phases. These findings indicated that m-retinochrome exists in two forms, with loose and tight coupling of the chromophore to the protein moiety. Those forms were usually balanced in a molar ratio of about 1:2, and the proportion of the tight form of m-retinochrome was increased in the presence of excess 11-cis-retinal. Based upon these findings, the role of m-retinochrome in the visual cells is discussed.
Animals↗
3-Dehydroretinal in the eye of a bioluminescent squid, Watasenia scintillans.
3-Dehydroretinal was found in the retina of a bioluminescent squid, Watasenia scintillans. The possible vitamin A2-visual pigment was localized in the ventral part of the eye and its proportion was about 15% of the total visual pigment.
Animals↗
Isolation and characterization of a retinal-binding protein from the squid retina.
A retinal-binding protein (RALBP) was isolated from the squid retina, and purified by anion-exchange and size-exclusion chromatography. The molecular weight was determined to be 51,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by gel filtration. The purified sample showed absorption maxima at about 330 and 400 nm in addition to a protein band, indicating the occurrence of retinol and retinal, respectively. The relative heights of these two peaks varied from preparation to preparation, depending on retinoid ligands. Irradiation of RALBP caused no marked change in absorption, but the amount of 11-cis-retinal decreased to form a photosteady state mixture with all-trans- and 13-cis-retinals. RALBP was fairly stable even in the presence of hydroxylamine (100 mM), but was affected by sodium borohydride (30 mM) or borane dimethylamine (400 mM), with the retinal reduced to retinol. When incubated with metaretinochrome-carrying membranes in the dark, RALBP specifically took up 11-cis-retinal and lost all-trans-retinol. Upon further incubation of this RALBP with opsin-containing membranes, rhodopsin was progressively formed in the dark. Squid RALBP may act as a shuttle in transferring the 11-cis-retinal from metaretinochrome to opsin in the visual cells.
Animals↗
IRBP-like proteins in the eyes of six cephalopod species--immunochemical relationship to vertebrate interstitial retinol-binding protein (IRBP) and cephalopod retinal-binding protein.
SDS polyacrylamide gel electrophoresis and immunoblotting were used to examine soluble proteins from the eyes of six species of cephalopods i.e. Lolliguncula brevis, Sepia officinalis, Octopus maya, Octopus bimaculoides, Rossia pacifica and Loligo opalescens. All species had a protein ("IRBP") with molecular weight virtually identical with vertebrate interstitial retinol-binding protein (IRBP) averaging 132,400 +/- 700 (n = 6). "IRBP" reacted on nitrocellulose blot transfers with rabbit antibovine IRBP and rabbit antifrog IRBP antibodies. Unlike vertebrate IRBP, cephalopod "IRBP" (from L. brevis) did not bind exogenous retinol or concanavalin A. The N-terminal amino acid appeared to be blocked in samples electroeluted from SDS gels. The antifrog IRBP antibodies also reacted with a series of proteins with molecular weights between 46,000 and 47,000, identified as retinal-binding protein (RALBP) with anti-RALBP antibodies. Anti-IRBP also reacted with pure RALBP prepared from Todarodes pacificus. Occasionally, anti-RALBP antibodies were seen to react weakly with "IRBP" in some cephalopods. We conclude that RALBP, cephalopod "IRBP" and vertebrate IRBP share a common but distant ancestry, and that a protein resembling IRBP appeared before the vertebrates diverged from the invertebrates. Both RALBP and IRBP appear to have analogous functions in shuttling retinoids between rhodopsin and the corresponding isomerizing system, retinochrome in the cephalopods and retinol isomerase in the vertebrates. The function of cephalopod "IRBP" is unknown.
Amino Acids↗
Retinal-binding protein as a shuttle for retinal in the rhodopsin-retinochrome system of the squid visual cells.
The molluscan visual cell is characterized by having two photopigment systems, rhodopsin and retinochrome. In connection with these systems, located separately in the rhabdomal microvilli and in the nucleated cell bodies, the physiological role of retinal-binding protein (RALBP) was investigated in the squid (Todarodes pacificus) by using 3-dehydroretinal (retinal 2) as a tracer for retinal chromophore. In dark-adapted eyes, squid RALBP is combined abundantly with 11-cis-retinal. However, upon incubation with an excess of all-trans-retinal or retinol, RALBP took up great amounts of each of them, releasing its native retinoid ligands. When an all-trans-retinal-rich RALBP thus produced was incubated in the dark with metaretinochrome 2-carrying membranes, the RALBP released all-trans-retinal to the membranes to regenerate retinochrome, taking up 11-cis-retinal 2 from metaretinochrome 2. Upon further incubation of this 11-cis-retinal 2-rich RALBP with metarhodopsin-carrying membranes, the RALBP released the 11-cis-retinal 2 to the membranes to form rhodopsin 2, receiving all-trans-retinal from metarhodopsin. These findings show that squid RALBP is capable of serving as a shuttle during the recycling of retinal in the rhodopsin-retinochrome conjugate system to maintain the photoreceptive function of the visual cells.
Animals↗
Light-induced, GTP-binding protein mediated membrane currents of Xenopus oocytes injected with rhodopsin of cephalopods.
Xenopus oocytes that were injected with rhabdomeric membranes of squid and octopus photoreceptors acquired light sensitivity. The injected oocytes showed a light-induced current having characteristics similar to other G-protein-mediated Cl- currents induced by the activation of other membrane receptors. Pretreatment of the oocytes with pertussis toxin before the injection suppressed the generation of the light-induced current, indicating an ability of cephalopod rhodopsin to cross-react with an endogenous G-protein of Xenopus oocytes.
Animals↗
The absorbance spectrum and photosensitivity of a new synthetic "visual pigment" based on 4-hydroxyretinal.
The firefly squid, Watasenia scintillans, is the only animal known to possess a visual pigment in which the chromophore is 4-hydroxyretinal. This paper describes the absorbance spectrum and some properties of a synthetic "A4" visual pigment generated from bovine opsin and 4-hydroxyretinal. The absorbance spectrum of this pigment is compared with (a) bovine rhodopsin and (b) a rhodopsin template with the same lambda max as the synthetic visual pigment. The A4 pigment is shown to have an absorbance spectrum that is almost identical to that of a rhodopsin template. It is also shown that the photosensitivity and thermal stability of the A4 pigment, dispersed in detergent micelles, is essentially similar to that of rhodopsin.
Animals↗
Phosphatidyl inositol-phospholipase C in squid photoreceptor membrane is activated by stable metarhodopsin via GTP-binding protein, Gq.
Phosphatidyl inositol-phospholipase C (PI-PLC) in squid retina was studied by immunoblotting and its activities were determined using [3H]phosphatidyl inositol bisphosphate ([3H]PIP2) as substrate. PI-PLC activity was found mostly in soluble fraction when the retina homogenate was treated with 400 mM KCl, but was associated with rhabdomal membranes under low salt conditions (20 mM Hepes). A protein with apparent molecular mass of 130kD was recognized by an antibody against PLC beta 4/norp A in both 400 mM KCl soluble and rhabdomal membrane fractions. A 42 kD protein recognized by antibody against the C-terminus of Gq alpha was also present in these two fractions. GTP gamma S stimulated only the PI-PLC activity associated with membrane and was magnesium dependent. PI-PLC activity was found to be (i) highly dependent upon calcium concentrations, (ii) enhanced by GTP but not by other nucleotides, and (iii) significantly stimulated by light at lower concentrations of GTP gamma S. The stimulation by light was still observed when irradiated membrane was incubated at 10 degrees C for 10 min and then mixed with GTP gamma S. These results suggest that stable metarhodopsin stimulates a PLC beta 4/norp A-like enzyme via a G-protein, Gq.
Animals↗
Growth and optical development of the ocular lens of the squid (Sepioteuthis lessoniana).
Lens focal properties (spherical aberration), diameter and relative anterior/posterior proportions were measured photographically for Japanese squid (Sepioteuthis lessoniana) at ages 4-6 weeks, 7-9 weeks and 7-8 months. The measures involved photographing the refractive effects of lenses in a physiological solution, with and without an index matching fluid (polyvinylpyrroloidone solution), on a parallel array of fine helium-neon laser beams. Spherical aberration was determined from measurement of back vertex distance. Similar measurements were made on lenses from the eyes of cuttlefish (Sepia officinalis). The cephalopod lens develops as hemispheric halves from separate ectodermal sources. The posterior component contributes, on average, about 60% of axial lens diameter in S. lessoniana of all ages and 55% in S. officinalis. However, these proportions vary widely in both species. All lenses of both species show that spherical aberration is neutralized, although small variations in back vertex distance (positive and negative spherical aberration) were measured. Preliminary measures indicate that the refractive index distribution within the cephalopod lens varies in a manner reminiscent of teleost lenses. Squid lenses from animals 7-9 weeks of age were optimally corrected for spherical aberration. Some squid of this age, from a separate tank, showed a high incidence of cataract development. In each case, lens opacification was caused by deterioration of the posterior lens component.
Aging↗
Role of microtubules and axolinin in membrane excitation of the squid giant axon.
The squid giant axon possesses numerous microtubules and a large pool of axolinin, both of which are preferentially localized at the peripheral region of the axoplasm just underlying the axolemma. A series of perfusion experiments presents evidence that microtubules localized in the clad are directly associated with the membrane excitability. The internal perfusons which cause microtubules to depolymerize reduce the excitability and those supporting microtubule assembly increase the peak sodium current. Direct evidence that microtubules are essential for membrane excitation is obtained by the restoration of diminished membrane excitability. The restoration system consists of squid brain or axoplasmic tubulin, axolinin, ATP, Mg2+, and cAMP or of porcine brain tubulin, tubulin-tyrosine ligase, axolinin, GTP, ATP, Mg2+, and cAMP. The former restoration system causes the diminished excitability to recover in such a way that the Na conductance, resting potential, and Na reversal potentials are much improved. One hypothesis is that tyrosinated tubulin is polymerized into microtubules underneath the axolemma. Axolinin binds to the axolemma at one end of the rod-like molecule and cross-links the assembled microtubules with the other end, thereby reconstructing cytoskeletons just underneath the axolemma which are necessary for membrane excitation.
Alkaloids↗
Isolation of intermediate filaments from neuronal tissues by cycles of assembly/disassembly.
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Animals↗
Inhibition of translocation reactions by vanadate.
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Animals↗
Transport and metabolism of calcium ions in nerve.
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Acetates↗
Energetic aspects of nerve conduction: the relationships between heat production, electrical activity and metabolism.
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Action Potentials↗
Analytical models of propagation in excitable cells.
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Action Potentials↗