Photoreceptors in a primitive mammal, the South American opossum, Didelphis marsupialis aurita: characterization with anti-opsin immunolabeling. 1995

P K Ahnelt, and J N Hokoç, and P Röhlich
Department of General and Comparative Physiology, University of Vienna, Austria.

The retinas of placental mammals appear to lack the large number and morphological diversity of cone subtypes found in diurnal reptiles. We have now studied the photoreceptor layer of a South American marsupial (Didelphis marsupialis aurita) by peanut agglutinin labeling of the cone sheath and by labeling of cone outer segments with monoclonal anti-visual pigment antibodies that have been proven to consistently label middle-to-long wavelength (COS-1) and short-wavelength (OS-2) cone subpopulations in placental mammals. Besides a dominant rod population (max. = 400,000/mm2) four subtypes of cones (max. = 3000/mm2) were identified. The outer segments of three cone subtypes were labeled by COS-1: a double cone with a principal cone containing a colorless oil droplet, a single cone with oil droplet, and another single cone. A second group of single cones lacking oil droplets was labeled by OS-2 antibody. The topography of these cone subtypes showed striking anisotropies. The COS-1 labeled single cones without oil droplets were found all over the retina and constituted the dominant population in the area centralis located in the temporal quadrant of the upper, tapetal hemisphere. The population of OS-2 labeled cones was also ubiquitous although slightly higher in the upper hemisphere (200/mm2). The COS-1 labeled cones bearing an oil droplet, including the principal member of double cones, were concentrated (800/mm2) in the inferior, non-tapetal half of the retina. The two spectral types of single cones resemble those of dichromatic photopic systems in most placental mammals. The additional set of COS-1 labeled cones is a distinct marsupial feature. The presence of oil droplets in this cone subpopulation, its absence in the area centralis, and the correlation with the non-tapetal inferior hemisphere suggest a functional specialization, possibly for mesopic conditions. Thus, sauropsid features have been retained but probably with a modified function.

UI MeSH Term Description Entries
D007150 Immunohistochemistry Histochemical localization of immunoreactive substances using labeled antibodies as reagents. Immunocytochemistry,Immunogold Techniques,Immunogold-Silver Techniques,Immunohistocytochemistry,Immunolabeling Techniques,Immunogold Technics,Immunogold-Silver Technics,Immunolabeling Technics,Immunogold Silver Technics,Immunogold Silver Techniques,Immunogold Technic,Immunogold Technique,Immunogold-Silver Technic,Immunogold-Silver Technique,Immunolabeling Technic,Immunolabeling Technique,Technic, Immunogold,Technic, Immunogold-Silver,Technic, Immunolabeling,Technics, Immunogold,Technics, Immunogold-Silver,Technics, Immunolabeling,Technique, Immunogold,Technique, Immunogold-Silver,Technique, Immunolabeling,Techniques, Immunogold,Techniques, Immunogold-Silver,Techniques, Immunolabeling
D009893 Opossums New World marsupials of the family Didelphidae. Opossums are omnivorous, largely nocturnal and arboreal MAMMALS, grow to about three feet in length, including the scaly prehensile tail, and have an abdominal pouch in which the young are carried at birth. Didelphidae,Opossum
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000911 Antibodies, Monoclonal Antibodies produced by a single clone of cells. Monoclonal Antibodies,Monoclonal Antibody,Antibody, Monoclonal
D012168 Retinal Pigments Photosensitive protein complexes of varied light absorption properties which are expressed in the PHOTORECEPTOR CELLS. They are OPSINS conjugated with VITAMIN A-based chromophores. Chromophores capture photons of light, leading to the activation of opsins and a biochemical cascade that ultimately excites the photoreceptor cells. Retinal Photoreceptor Pigment,Retinal Pigment,Visual Pigment,Visual Pigments,Retinal Photoreceptor Pigments,Photoreceptor Pigment, Retinal,Photoreceptor Pigments, Retinal,Pigment, Retinal,Pigment, Retinal Photoreceptor,Pigment, Visual,Pigments, Retinal,Pigments, Retinal Photoreceptor,Pigments, Visual
D017299 Rod Opsins Photosensitive proteins expressed in the ROD PHOTORECEPTOR CELLS. They are the protein components of rod photoreceptor pigments such as RHODOPSIN. Rod-Opsin,Opsins, Rod,Rod Opsin
D017949 Retinal Cone Photoreceptor Cells Photosensitive afferent neurons located primarily within the FOVEA CENTRALIS of the MACULA LUTEA. There are three major types of cone cells (red, blue, and green) whose photopigments have different spectral sensitivity curves. Retinal cone cells operate in daylight vision (at photopic intensities) providing color recognition and central visual acuity. Cone Photoreceptors,Cones (Retina),Cone Photoreceptor Cells,Photoreceptors, Cone,Retinal Cone,Retinal Cone Cells,Retinal Cone Photoreceptors,Cell, Cone Photoreceptor,Cell, Retinal Cone,Cells, Cone Photoreceptor,Cells, Retinal Cone,Cone (Retina),Cone Cell, Retinal,Cone Cells, Retinal,Cone Photoreceptor,Cone Photoreceptor Cell,Cone Photoreceptor, Retinal,Cone Photoreceptors, Retinal,Cone, Retinal,Cones, Retinal,Photoreceptor Cell, Cone,Photoreceptor Cells, Cone,Photoreceptor, Cone,Photoreceptor, Retinal Cone,Photoreceptors, Retinal Cone,Retinal Cone Cell,Retinal Cone Photoreceptor,Retinal Cones
D019887 Peanut Agglutinin Lectin purified from peanuts (ARACHIS HYPOGAEA). It binds to poorly differentiated cells and terminally differentiated cells and is used in cell separation techniques. Peanut Lectin,Agglutinin, Peanut,Lectin, Peanut
D037102 Lectins Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition. Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal

Related Publications

P K Ahnelt, and J N Hokoç, and P Röhlich
January 1989, Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas,
P K Ahnelt, and J N Hokoç, and P Röhlich
January 1990, Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas,
P K Ahnelt, and J N Hokoç, and P Röhlich
March 2000, The Journal of comparative neurology,
P K Ahnelt, and J N Hokoç, and P Röhlich
January 1982, Anatomischer Anzeiger,
P K Ahnelt, and J N Hokoç, and P Röhlich
January 1982, Transactions of the Royal Society of Tropical Medicine and Hygiene,
P K Ahnelt, and J N Hokoç, and P Röhlich
July 1974, Journal of reproduction and fertility,
P K Ahnelt, and J N Hokoç, and P Röhlich
June 1997, Toxicon : official journal of the International Society on Toxinology,
P K Ahnelt, and J N Hokoç, and P Röhlich
August 1970, Electroencephalography and clinical neurophysiology,
P K Ahnelt, and J N Hokoç, and P Röhlich
June 1970, The Journal of parasitology,
P K Ahnelt, and J N Hokoç, and P Röhlich
September 1981, The Journal of comparative neurology,
Copied contents to your clipboard!