Conserved and divergent patterns of Reelin expression in the zebrafish central nervous system.
The protein Reelin is suggested to function in cell-cell interactions and in mediating neuronal migrations in layered central nervous system structures. With the aim of shedding light on the development of the teleost telencephalon, which forms through the process of eversion and results in the formation of a nonlaminar pallium, we isolated a zebrafish ortholog of the reelin gene and studied its expression in developing and adult brain. The pattern of expression is highly dynamic during the first 24-72 hours of development. By 5 days postfertilization, high amounts of reelin mRNA are found in the dorsal telencephalon, thalamic and hypothalamic regions, pretectal nuclei, optic tectum, cerebellum, hindbrain, reticular formation, and spinal cord, primarily confined to postmitotic neurons. This pattern persists in 1- to 3-month-old zebrafish. This study, together with reports on reelin expression in other vertebrates, shows that reelin mRNA distribution is conserved in many regions of the vertebrate brain. A major exception is that reelin is expressed in the majority of the cells of the dorsal regions of the everted telencephalon in zebrafish embryos, whereas it is restricted to specific neuronal populations in the developing telencephalon of amniotes. To better understand the origin of these differences, we analyzed reelin expression in the telencephalon of an amphibian. Telencephalic reelin expression in Xenopus laevis shows more similarities with the sauropsidian than with the teleostean pattern. Thus, the differences in the telencephalic expression of reelin between teleosts and tetrapods are likely to be due to different roles for Reelin during eversion, a process that is specific for the teleost telencephalon.
Department of Anatomy and Developmental Biology, University College London, WC1E 6BT London, United Kingdom.
Arianna
A
Costagli
Marika
M
Kapsimali
Stephen W
SW
Wilson
Marina
M
Mione
D000375:Aging / Q000378:metabolism; D000818:Animals; D015816:Cell Adhesion Molecules, Neuronal / Q000235:genetics* / Q000302:isolation & purification*; D002454:Cell Differentiation / Q000502:physiology*; D002490:Central Nervous System / Q000196:embryology / Q000254:growth & development / Q000378:metabolism*; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification; D004027:Diencephalon / Q000196:embryology / Q000254:growth & development / Q000378:metabolism; D004625:Embryo, Nonmammalian; D019143:Evolution, Molecular; D016326:Extracellular Matrix Proteins / Q000235:genetics* / Q000302:isolation & purification*; D018507:Gene Expression Regulation, Developmental / Q000502:physiology*; D007150:Immunohistochemistry; D007814:Larva / Q000166:cytology / Q000254:growth & development / Q000378:metabolism; D008636:Mesencephalon / Q000196:embryology / Q000254:growth & development / Q000378:metabolism; D009419:Nerve Tissue Proteins; D009474:Neurons / Q000166:cytology / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D000091042:Reelin Protein; D012249:Rhombencephalon / Q000196:embryology / Q000254:growth & development / Q000378:metabolism; D012697:Serine Endopeptidases; D013687:Telencephalon / Q000196:embryology / Q000254:growth & development / Q000378:metabolism; D029867:Xenopus Proteins / Q000235:genetics / Q000302:isolation & purification; D014982:Xenopus laevis / Q000196:embryology / Q000254:growth & development / Q000378:metabolism; D015027:Zebrafish / Q000196:embryology / Q000254:growth & development / Q000378:metabolism*
D015816:Cell Adhesion Molecules, Neuronal; D018076:DNA, Complementary; D016326:Extracellular Matrix Proteins; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger; D000091042:Reelin Protein; D029867:Xenopus Proteins; D012697:Serine Endopeptidases