Characterization of the genomic structure of the mouse APLP1 gene.
Amyloid beta protein (beta A4), the major component of the core of amyloid plaques in Alzheimer disease, is derived from the transmembrane amyloid precursor proteins (APPs). Our recent studies showed that a murine member of the evolutionarily conserved APP family, amyloid precursor-like protein 1 (APLP1), is specifically localized to the cerebral cortex postsynaptic density and may thus participate in brain synaptic function. To investigate regulatory mechanisms of APLP1 synthesis at the genomic level, we isolated and characterized genomic clones containing the mouse APLP1 gene. Sequence analysis revealed a genomic structure consisting of 17 exons and a promoter region that is devoid of apparent TATA and CCAAT boxes. The 5' region contains putative binding sites for AP-1, heat-shock protein, and Sp1, suggesting that multiple elements are potentially involved in regulating transcription of the APLP1 gene.
Zhong
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S
Department of Neuroscience and Cell Biology, UMDNJ-Robert Wood Johnson Medical School, Piscataway, USA.
Wu
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K
Black
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Schaar
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DG
D000544:Alzheimer Disease / Q000209:etiology / Q000235:genetics; D016564:Amyloid beta-Protein Precursor / Q000031:analogs & derivatives* / Q000235:genetics; D000818:Animals; D001483:Base Sequence; D016384:Consensus Sequence; D018076:DNA, Complementary / Q000235:genetics; D019143:Evolution, Molecular; D005091:Exons; D005809:Genes, Regulator; D016678:Genome; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data
C489697:APLP1 protein, human; D016564:Amyloid beta-Protein Precursor; C078201:Aplp1 protein, mouse; D018076:DNA, Complementary