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Prenylated protein methyltransferase of rat cerebellum is developmentally co‐expressed with its substrates
Author(s) -
Paz A.,
Ben-Baruch G.,
Marciano D.,
Egozi Y.,
Haklai R.,
Kloog Y.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80634-7
Subject(s) - cerebellum , synaptogenesis , granule cell , biology , methyltransferase , enzyme , biochemistry , microbiology and biotechnology , endocrinology , medicine , methylation , dentate gyrus , central nervous system , gene
High levels of prenylated protein methyltransferase are expressed in the developing rat cerebellum and are responsible for methylation of endogenous G‐proteins and 50–52 kDa synaptosomal proteins. Enzyme activity in cerebellar synaptosomes of 3 week postnatal rats is 2‐fold higher than that found in adult rat cerebellum. A 10‐fold rise in activity occurs at the end of the second and during the third postnatal weeks, followed by a subsequent decline. Expression of the enzymes' substrates follows the same pattern. The high methyltransferase activity in 3‐week‐old cerebellum coincides with the period of granule cell migration and synaptogenesis, suggesting a regulatory role for the enzyme and its substrates in cerebellar ontogenesis.