Premium
Xefiltin, a new low molecular weight neuronal intermediate filament protein of Xenopus laevis , shares sequence features with goldfish gefiltin and mammalian α‐internexin and differs in expression from XNIF and NF‐L
Author(s) -
Zhao Yangu,
Szaro Ben G.
Publication year - 1997
Publication title -
journal of comparative neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.855
H-Index - 209
eISSN - 1096-9861
pISSN - 0021-9967
DOI - 10.1002/(sici)1096-9861(19970120)377:3<351::aid-cne4>3.0.co;2-1
Subject(s) - biology , xenopus , neurofilament , protein subunit , microbiology and biotechnology , intermediate filament , forebrain , in situ hybridization , central nervous system , biochemistry , neuroscience , gene expression , cytoskeleton , gene , cell , immunohistochemistry , immunology
The nervous system of the postmetamorphic frog Xenopus laevis , like that of other amphibians, shows continued growth and a high capacity for regeneration, especially in its visual system. This characteristic has been attributed, in part, to the retention in adults of traits that in mammals are limited to embryos. In mammals, the progressive maturation of neurons is marked by successive changes in neuronal intermediate filament (nIF) subunit composition. For example, in mammalian forebrain, newly differentiating neurons first express the low molecular weight nIF protein α‐internexin. As neurons mature, α‐internexin expression declines, and expression of the low molecular weight neurofilament triplet protein (NF‐L) increases. Thus, a systematic examination of the expression of low molecular weight nIF proteins in the postmetamorphic frog might reveal whether the nIF subunit composition of its neurons more closely resembles that of embryonic as opposed to adult mammals. Previously, X. leavis has been shown to express both NF‐L and XNIF, a novel low molecular weight nIF protein that most closely resembles mammalian α‐internexin. We have now discovered a new, low molecular weight nIF protein with even higher homology to α‐internexin. We named this protein xefiltin, because it shared highest sequence identity with gefiltin, an α‐internexin‐like nIF protein from the goldfish visual system. In situ hybridization with probes to xefiltin, XNIF and NF‐L showed that transcripts of all three were expressed widely throughout the post‐metamorphic frog nervous system, but with distinctly different patterns of expression. For example, xefiltin was the most abundantly expressed of the three in retinal ganglion cells and in neurons of the habenular nucleus and telencephalon, whereas XNIF and NF‐L were found at higher levels than xefiltin in peripheral sensory ganglia and in structures caudal to the mesencephalon. In general, the combined distributions of xefiltin and XNIF paralleled the distribution of α‐internexin in mammalian embryos. Thus, we speculate that the persistence of α‐internexin‐like nIF proteins in the amphibian nervous system may be important for its continued potential for growth and plasticity. J. Comp. Neurol. 377:351–364, 1997. © 1997 Wiley‐Liss, Inc.