Lim, Hong Hwa; (1991) Characterization of human and rat homologues of the human brain n-chimaerin cdna. Doctoral thesis (Ph.D), UCL (University College London).

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Abstract

A 2.3 kb rat brain cDNA has been isolated which is homologous to human n-chimaerin cDNA, encoding a protein with similarity to the C1 regulatory domain of protein kinase C (N- terminal) and to the product of the human breakpoint cluster region gene (C-terminal). The extreme 5' (500 bp) rat cDNA sequence is in opposite orientation to that of the human and this orientation was verified using RACE (rapid amplification of cDNA ends). As a result, the rat cDNA encodes a protein containing at the N-terminal 35 amino acid residues in addition to the 299 amino acid residues encoded by the human cDNA. The latter polypeptide exhibits 97% sequence identity. The rat cDNA contains CACACCACAAACAC repeats (not found in the human) in the 3' untranslated region. The concentration of the 2.3 kb rat brain mRNA increases progressively from embryonic day 15 to postnatal day 40. In situ hybridization analysis demonstrated mRNA expression in neurones of the hippocampus, cortex and the Purkinje cells of the cerebellum. A related rat brain cDNA contains a unique 5' EcoRI fragment, which hybridized to the 5' RACE products generated from rat brain mRNA using rat n-chimaerin specific primers and detected an mRNA smaller than n-chimaerin mRNA. A related human cDNA, H631.1, contains additional sequences at the 5' end encoding a region with similarity to src homology 2 domain (SH2) and another identical to part of CRE-BP1 (cAMP response element binding protein-1). 5'RACE confirmed the presence of a brain mRNA encoding n-chimaerin with the additional SH2 domain. A partial human cDNA sequence encoding the SH2 and CRE-BP1 domains detected a 4 kb mRNA which in contrast to the n-chimaerin mRNA decreased with development in rat brain. The results indicate the existence of multiple mRNAs encoding n-chimaerin as well as larger proteins containing the n-chimaerin sequence.

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