Egyszerű nézet

dc.contributor.author Chiquet C,
dc.contributor.author Dkhissi-Benyahya O,
dc.contributor.author Chounlamountri N,
dc.contributor.author Szél, Ágoston
dc.contributor.author Degrip WJ,
dc.date.accessioned 2015-02-25T10:03:41Z
dc.date.available 2015-02-25T10:03:41Z
dc.date.issued 2002
dc.identifier 0037121627
dc.identifier.citation pagination=1323-1333; journalVolume=115; journalIssueNumber=4; journalTitle=NEUROSCIENCE;
dc.identifier.uri http://repo.lib.semmelweis.hu//handle/123456789/1377
dc.identifier.uri doi:10.1016/S0306-4522(02)00327-5
dc.description.abstract The aim of this study is to characterize calbindin-positive photoreceptors and their opsin content in the retina of nocturnal prosimians (Microcebus murinus), New World monkeys (Callithrix jacchus), Old World monkeys (Macaca fascicularis), and humans. To identify the calbindin and opsin content of cones, combined multiple labeling with different fluorescent probes, antibodies directed against calbindin, short, and mid-long wavelength opsins, and lectin peanut agglutinin cytochemistry were used. With the exception of Microcebus, calbindin is present in the cones of all primates but is absent from rods. The distribution of calbindin is similar in human and macaque cones, with dense label in the inner segment, cell body, axon and cone pedicle. Cones in marmoset also show dense staining in the cell body, axon and pedicle but only light label in the inner segment. Primate cone outer segments do not contain calbindin. In the primates studied, three patterns of calbindin and opsin localization are observed. In macaque and marmoset all short and mid-long wavelength cones contain calbindin. In humans, all mid-long wavelength cones contain calbindin whereas all short wavelength cones are devoid of calbindin as confirmed by confocal microscopy. In the nocturnal prosimian Microcebus none of the mid-long or short wavelength cones contain calbindin. In addition to primates, calbindin is absent in cones of other nocturnal species but is present in cones of diurnal species suggesting a difference in the role of calbindin possibly related to the adaptational states or other photoreceptor properties.
dc.relation.ispartof urn:issn:0306-4522
dc.title Characterization of calbindin-positive cones in primates
dc.type Journal Article
dc.date.updated 2015-02-10T11:47:11Z
dc.language.rfc3066 en
dc.identifier.mtmt 1416701
dc.identifier.wos 000179668400028
dc.identifier.pubmed 12453500
dc.contributor.department SE/AOK/I/Humánmorfológiai és Fejlődésbiológiai Intézet
dc.contributor.institution Semmelweis Egyetem


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