scholarly journals Ultraviolet and violet receptors express identical mRNA encoding an ultraviolet-absorbing opsin: identification and histological localization of two mRNAs encoding short-wavelength-absorbing opsins in the retina of the butterfly Papilio xuthus

2000 ◽  
Vol 203 (19) ◽  
pp. 2887-2894 ◽  
Author(s):  
J. Kitamoto ◽  
K. Ozaki ◽  
K. Arikawa
Keyword(s):  
Amino Acid ◽  
Visual Pigment ◽  
Short Wavelength ◽  
Photoreceptor Cells ◽  
Visual Pigments ◽  
Amino Acid Sequences ◽  
Papilio Xuthus ◽  
Different Types ◽  
Identical Amino Acid Sequence

This paper describes the primary structures of two opsins of short-wavelength-absorbing visual pigments deduced from the mRNA sequences in the retina of the Japanese yellow swallowtail butterfly Papilio xuthus. A phylogenetic analysis of the amino acid sequences indicates that one of these visual pigments is of the ultraviolet-absorbing type and that the other is of the blue-absorbing type. We identified the photoreceptor cells that express these mRNAs by histological in situ hybridization. The mRNA of the ultraviolet type is expressed in two distinct photoreceptor types previously identified as ultraviolet and violet receptors, providing the first molecular biological evidence that different types of spectral receptor probably express a visual pigment with an identical amino acid sequence. The mRNA of the blue type is expressed exclusively in cells classified as blue receptors.

scholarly journals Two visual pigments in a single photoreceptor cell: identification and histological localization of three mRNAs encoding visual pigment opsins in the retina of the butterfly Papilio xuthus.

1998 ◽  
Vol 201 (9) ◽  
pp. 1255-1261 ◽  
Author(s):  
J Kitamoto ◽  
K Sakamoto ◽  
K Ozaki ◽  
Y Mishina ◽  
K Arikawa
Keyword(s):  
In Situ Hybridization ◽  
Visual Pigment ◽  
Photoreceptor Cell ◽  
Wavelength Region ◽  
Photoreceptor Cells ◽  
Visual Pigments ◽  
Cell Identification ◽  
Papilio Xuthus

This paper describes the localization of newly identified visual pigment opsins in the tiered retina of the Japanese yellow swallowtail Papilio xuthus. We first cloned three cDNAs encoding visual pigment opsins, PxRh1, PxRh2 and PxRh3, and then carried out histological in situ hybridization to localize their mRNAs in the retina. By combining the present data with our previous electrophysiological results, we concluded that both PxRh1 and PxRh2 correspond to visual pigments expressed in photoreceptor cells sensitive in the green wavelength region (green receptors), whereas PxRh3 corresponds to a pigment in red receptors. The in situ hybridization studies showed that some photoreceptor cells express two opsin mRNAs. In the ventral half of the eye, all green receptors in the distal tier were labelled by both PxRh1 and PxRh2 probes. The labelling by the PxRh2 and PxRh3 probes was detected throughout the eye in the proximal tier; in 18 % of ommatidia, the probes labelled the same photoreceptor cell. These results suggest that the possible co-localization of two different visual pigments will broaden the sensitivity spectrum of the photoreceptor cells.

The photoreceptors and visual pigments in the retina of the white sturgeon, Acipenser transmontanus

1990 ◽  
Vol 68 (7) ◽  
pp. 1544-1551 ◽  
Author(s):  
A. J. Sillman ◽  
M. D. Spanfelner ◽  
E. R. Loew
Keyword(s):  
Vitamin A ◽  
Visual Pigment ◽  
Visual Pigments ◽  
Spectrophotometric Analysis ◽  
White Sturgeon ◽  
Acipenser Transmontanus ◽  
Light Regimen ◽  
Cone Pigment ◽  
Spectral Absorbance

The photoreceptors in the retina of the white sturgeon, Acipenser transmontanus (Chondrostei), were studied by means of scanning electron microscopy, in situ microspectrophotometry, and spectrophotometric analysis of visual pigment extracts. The white sturgeon retina is simple in that it contains only two morphologically distinct photoreceptors. The retina is dominated by rods with large outer segments, but there is a substantial population (40%) of single cones. Evidence was found for only one rod visual pigment and one cone visual pigment. Peak spectral absorbance (λmax) of the rod pigment is near 539 nm, whereas λmax of the cone pigment is near 605 nm. Both visual pigments are porphyropsin types with chromophores based on vitamin A2. No detectable rhodopsin based on vitamin A1 is ever present, regardless of season or light regimen. The results are discussed in terms of the sturgeon's behavior, as well as the implications for the evolution of color vision.

scholarly journals Multiple visual pigments in a photoreceptor of the salamander retina.

1996 ◽  
Vol 108 (1) ◽  
pp. 27-34 ◽  
Author(s):  
C L Makino ◽  
R L Dodd
Keyword(s):  
Absorption Spectra ◽  
Visual Pigment ◽  
Photoreceptor Cells ◽  
Visual Pigments ◽  
Wavelength Band ◽  
Absorption Bands ◽  
Maximal Sensitivity ◽  
Retinal Chromophore ◽  
Wavelength Discrimination ◽  
Pigment Absorption

Although a given retina typically contains several visual pigments, each formed from a retinal chromophore bound to a specific opsin protein, single photoreceptor cells have been thought to express only one type of opsin. This design maximizes a cell's sensitivity to a particular wavelength band and facilitates wavelength discrimination in retinas that process color. We report electrophysiological evidence that the ultraviolet-sensitive cone of salamander violates this rule. This cell contains three different functional opsins. The three opsins could combine with the two different chromophores present in salamander retina to form six visual pigments. Whereas rods and other cones of salamander use both chromophores, they appear to express only one type of opsin per cell. In visual pigment absorption spectra, the bandwidth at half-maximal sensitivity increases as the pigment's wavelength maximum decreases. However, the bandwidth of the UV-absorbing pigment deviates from this trend; it is narrow like that of a red-absorbing pigment. In addition, the UV-absorbing pigment has a high apparent photosensitivity when compared with that of red- and blue-absorbing pigments and rhodopsin. These properties suggest that the mechanisms responsible for spectrally tuning visual pigments separate two absorption bands as the wavelength of maximal sensitivity shifts from UV to long wavelengths.

Identification of a Novel Gene SRG4 Expressed at Specific Stages of Mouse Spermatogenesis

2004 ◽  
Vol 36 (5) ◽  
pp. 351-359 ◽  
Author(s):  
Xiao-Wei Xing ◽  
Lu-Yun Li ◽  
Gang Liu ◽  
Jun-Jiang Fu ◽  
Xiao-Jun Tan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Mouse Testis ◽  
Amino Acid Residues ◽  
Complex Process ◽  
Testis Cdna Library ◽  
New Gene ◽  
Testis Cdna ◽  
Gene 4

Abstract Spermatogenesis is a complex process. Two spermatocytes expression sequence tags (ESTs) BG101130 and BG100990 were found. Their putative amino acid sequences have high homology with rat Spag4 (sperm antigen 4). By electrical hybridization, a novel cDNA encoding polypeptide of 348 amino acid residues was identified from a mouse testis cDNA library. The new gene was designated as SRG4 (Spermatogenesis related gene 4) (GenBank accession No. AY307077). Results of Northern blot and RTPCR revealed that SRG4 expressed specifically in mouse testis. Changes of SRG4 expression in mouse different development stages were observed by RT-PCR. The SRG4 mRNA was hardly detected in 2 weeks postpartum, and expressed abundantly from 3 weeks later, reaching top lever at 4–5 weeks, while slightly down in aging mouse testis. Results of in situ hybridization showed that SRG4 gene expressed abundantly in spermatocytes, round spermatids. This indicated SRG4 gene may play an important role in mouse meiotic divisions of spermatocytes.

scholarly journals Protein-, (Poly)peptide-, and Amino Acid-Based Nanostructures Prepared via Polymerization-Induced Self-Assembly

Polymers ◽  
2021 ◽  
Vol 13 (16) ◽  
pp. 2603
Author(s):  
Spyridon Varlas ◽  
Georgia L. Maitland ◽  
Matthew J. Derry
Keyword(s):  
Amino Acid ◽  
Block Copolymer ◽  
Self Assembly ◽  
Vital Role ◽  
Amino Acid Sequences ◽  
Direct Construction ◽  
High Concentrations ◽  
Proteins And Peptides ◽  
Novel Protein

Proteins and peptides, built from precisely defined amino acid sequences, are an important class of biomolecules that play a vital role in most biological functions. Preparation of nanostructures through functionalization of natural, hydrophilic proteins/peptides with synthetic polymers or upon self-assembly of all-synthetic amphiphilic copolypept(o)ides and amino acid-containing polymers enables access to novel protein-mimicking biomaterials with superior physicochemical properties and immense biorelevant scope. In recent years, polymerization-induced self-assembly (PISA) has been established as an efficient and versatile alternative method to existing self-assembly procedures for the reproducible development of block copolymer nano-objects in situ at high concentrations and, thus, provides an ideal platform for engineering protein-inspired nanomaterials. In this review article, the different strategies employed for direct construction of protein-, (poly)peptide-, and amino acid-based nanostructures via PISA are described with particular focus on the characteristics of the developed block copolymer assemblies, as well as their utilization in various pharmaceutical and biomedical applications.

scholarly journals In search of the visual pigment template

2000 ◽  
Vol 17 (4) ◽  
pp. 509-528 ◽  
Author(s):  
VICTOR I. GOVARDOVSKII ◽  
NANNA FYHRQUIST ◽  
TOM REUTER ◽  
DMITRY G. KUZMIN ◽  
KRISTIAN DONNER
Keyword(s):  
Visual Pigment ◽  
Good Description ◽  
Visual Pigments ◽  
Rod Outer Segments ◽  
Absorbance Spectrum ◽  
Outer Segments ◽  
Bovine Rhodopsin ◽  
Α Band ◽  
Absorbance Spectra

Absorbance spectra were recorded by microspectrophotometry from 39 different rod and cone types representing amphibians, reptiles, and fishes, with A1- or A2-based visual pigments and λmax ranging from 357 to 620 nm. The purpose was to investigate accuracy limits of putative universal templates for visual pigment absorbance spectra, and if possible to amend the templates to overcome the limitations. It was found that (1) the absorbance spectrum of frog rhodopsin extract very precisely parallels that of rod outer segments from the same individual, with only a slight hypsochromic shift in λmax, hence templates based on extracts are valid for absorbance in situ; (2) a template based on the bovine rhodopsin extract data of Partridge and De Grip (1991) describes the absorbance of amphibian rod outer segments excellently, contrary to recent electrophysiological results; (3) the λmax/λ invariance of spectral shape fails for A1 pigments with small λmax and for A2 pigments with large λmax, but the deviations are systematic and can be readily incorporated into, for example, the Lamb (1995) template. We thus propose modified templates for the main “α-band” of A1 and A2 pigments and show that these describe both absorbance and spectral sensitivities of photoreceptors over the whole range of λmax. Subtraction of the α-band from the full absorbance spectrum leaves a “β-band” described by a λmax-dependent Gaussian. We conclude that the idea of universal templates (one for A1- and one for A2-based visual pigments) remains valid and useful at the present level of accuracy of data on photoreceptor absorbance and sensitivity. The sum of our expressions for the α- and β-band gives a good description for visual pigment spectra with λmax > 350 nm.

scholarly journals Adaptation of a deep-sea cephalopod to the photic environment. Evidence for three visual pigments.

1988 ◽  
Vol 92 (1) ◽  
pp. 55-66 ◽  
Author(s):  
S Matsui ◽  
M Seidou ◽  
S Horiuchi ◽  
I Uchiyama ◽  
Y Kito
Keyword(s):  
Deep Sea ◽  
Visual Pigment ◽  
Small Area ◽  
High Performance ◽  
Outer Segment ◽  
High Sensitivity ◽  
Photoreceptor Cells ◽  
High Performance Liquid Chromatographic ◽  
Visual Pigments ◽  
Environmental Light

Watasenia scintillans, a bioluminescent deep-sea squid, has a specially developed eye with a large open pupil and three visual pigments. Photoreceptor cells (outer segment: 476 micron; inner segment: 99 micron) were long in the small area of the ventral retina receiving downwelling light, whereas they were short (outer segment: 207 micron; inner segment: 44 micron) in the other regions of the retina. The short photoreceptor cells contained the visual pigment with retinal (lambda max approximately 484 nm), probably for the purpose of adapting to their environmental light. The outer segment of the long photoreceptor cells consisted of two strata, a pinkish proximal area and a yellow distal area. The visual pigment with 3-dehydroretinal (lambda max approximately 500 nm) was located in the pinkish proximal area, giving high sensitivity at longer wavelengths. A newly found pigment (lambda max approximately 471 nm) was in the yellow distal area. The small area of the ventral retina containing two visual pigments is thought to have a high and broad spectral sensitivity, which is useful for distinguishing the bioluminescence of squids of the same species in their environmental downwelling light. These findings were obtained by partial bleaching of the extracted pigment from various areas of the retina and by high-performance liquid chromatographic analysis of the chromophore, complemented by microscopic observations.

scholarly journals Isolation and Characterization of a Novel Member of the Relaxin/Insulin Family from the Testis of the Frog Rana esculenta*

Endocrinology ◽  
2001 ◽  
Vol 142 (7) ◽  
pp. 3231-3238 ◽  
Author(s):  
Gianluca de Rienzo ◽  
Francesco Aniello ◽  
Margherita Branno ◽  
Sergio Minucci
Keyword(s):  
In Situ Hybridization ◽  
Amino Acid ◽  
Messenger Rna ◽  
Rana Esculenta ◽  
Amino Acid Sequences ◽  
Characteristic Functional ◽  
Isolation And Characterization ◽  
Single Transcript ◽  
A Domains

Abstract A complementary DNA (cDNA) encoding a frog relaxin/insulin member family (fRLX) from testis cDNA library was isolated and characterized. The fRLX cDNA predicted a 155-amino acid protein with a low homology to mammalian RLF and relaxin. Northern blot analysis revealed a single transcript expressed in the interstitial compartment, RT-PCR, evidenced that fRLX is expressed at low levels in the oviduct and ovary too. The predicted mature fRLX protein, composed of the signal peptide, B, C, and A domains, has conserved amino acid sequences in the characteristic functional domains. A different expression of the transcript was found during the frog reproductive cycle, with a peak in Spring. After administration of ethane dimethane sulfonate, by in situ hybridization, fRLX messenger RNA disappeared from the interstitial compartment and reappeared again at the time of generating of a new population of Leydig cells (LC), strongly indicating that LC are the interstitial cell type expressing fRLX. Preliminary results obtained by in situ hybridization, performed on testis of hypophysectomized frogs evidenced a pituitary control of fRLX expression. This study is the first cloning of a relaxin/insulin family member in a nonmammalian vertebrate. In addition, because fRLX expression changes during the annual cycle suggesting its involvement in spermatogenesis, fRLX may be considered a new marker for the study of spermatogenesis in the Rana esculenta.

Cone visual pigments of the Australian marsupials, the stripe-faced and fat-tailed dunnarts: Sequence and inferred spectral properties

2004 ◽  
Vol 21 (3) ◽  
pp. 223-229 ◽  
Author(s):  
JESSICA STRACHAN ◽  
LING-YU E. CHANG ◽  
MATTHEW J. WAKEFIELD ◽  
JENNIFER A. MARSHALL GRAVES ◽  
SAMIR S. DEEB
Keyword(s):  
Amino Acid ◽  
Tammar Wallaby ◽  
Visual Pigments ◽  
Amino Acid Sequences ◽  
Coding Sequences ◽  
Cone Opsin ◽  
Evolutionarily Conserved ◽  
Cone Pigment ◽  
Cone Pigments ◽  
Sminthopsis Macroura

Studies of color vision in marsupial mammals have been very limited. Two photoreceptor genes have been characterized from the tammar wallaby, but a third cone pigment was suggested by microspectrophotometric measurements on cone photoreceptors in two other species, including the fat-tailed dunnart, Sminthopsis crassicaudata. To determine the sequence and infer absorption maxima of the cone photoreceptor pigments of S. crassicaudata and the related stripe-faced dunnart (Sminthopsis macroura), we have used evolutionarily conserved sequences of the cone pigments of other species, including the tammar wallaby, to design primers to amplify the S. macroura and S. crassicaudata pigment sequences by the polymerase chain reaction (PCR) using genomic DNA or retinal cDNA as a template. These primers will be useful for amplifying cone opsin coding sequences from a variety of vertebrates. Amplified products were directly sequenced to determine gene structure and coding sequences. The inferred amino acid sequences of the cone visual pigments indicated that both species have middle-wave-sensitive (MWS) pigments with a predicted absorption maximum (λmax) at 530 nm, and ultraviolet-sensitive (UVS) pigments with a predicted λmax at 360 nm. The MWS pigments of the two species differ by two, and UVS by three amino acid positions. No evidence was obtained for a third cone pigment in either species.

The visual pigments of wild white sturgeon (Acipenser transmontanus)

1995 ◽  
Vol 73 (4) ◽  
pp. 805-809 ◽  
Author(s):  
A. J. Sillman ◽  
M. E. Sorsky ◽  
E. R. Loew
Keyword(s):  
Vitamin A ◽  
Fresh Water ◽  
Visual Pigment ◽  
Visual Pigments ◽  
White Sturgeon ◽  
Acipenser Transmontanus ◽  
Estuarine Water ◽  
Cone Pigments ◽  
Partial Bleaching

The visual pigments of the anadromous white sturgeon (Acipenser transmontanus) taken from relatively saline estuarine water were characterized by means of in situ microspectrophotometry and partial bleaching analysis of a digitonin extract. The three cone pigments (λmax = 605, 539, and ca. 460 nm) and one rod pigment (λmax = 541 nm) of the wild sturgeon are the same as those of cultured sturgeon that spend their entire lives in fresh water. All the visual pigments incorporate a chromophore based on vitamin A2. Unlike other anadromous fishes during the "saline phase," the white sturgeon shows no evidence of the presence of any vitamin A1 based visual pigment in the retina.

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