Abstract:
:A nuclear protein, termed leucine-rich acidic nuclear protein (LANP), has been isolated from among rat cerebellar proteins whose expression was transiently increased during an early stage of postnatal development. The amino acid sequence, deduced from its cDNA, showed that LANP contains 247 amino acids consisting of two distinct structural domains: the N-terminal domain characterized by "leucine-rich repeat," which is found in many eukaryotic proteins and which potentially functions in mediating protein-protein interactions, and the C-terminal domain characterized by a cluster of acidic amino acids with a putative nuclear localization signal. Immunohistochemical study using an antibody against LANP revealed that the protein is localized mainly in nuclei of Purkinje cells. In the rat cerebellum on postnatal day 7, LANP mRNA was expressed moderately in the external granule and Purkinje cells and weakly in the internal granule cells. The expression in these cells, especially in Purkinje cells, increased in the second postnatal week and thereafter decreased to an adult level. The structural characteristics, localization, and the stage- and cell type-specific expression suggest a potential role of LANP in a signal transduction pathway that directs differentiation of cerebellar neurons.
journal_name
Proc Natl Acad Sci U S Aauthors
Matsuoka K,Taoka M,Satozawa N,Nakayama H,Ichimura T,Takahashi N,Yamakuni T,Song SY,Isobe Tdoi
10.1073/pnas.91.21.9670subject
Has Abstractpub_date
1994-10-11 00:00:00pages
9670-4issue
21eissn
0027-8424issn
1091-6490journal_volume
91pub_type
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