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PMID: 1420178 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Structure and novel exons of the human tau gene.

Biochemistry ·Vol. 31 ·No. 43 ·1992-11-03 ·Pages 10626-33

Andreadis A, Brown WM, Kosik KS

Abstract

The microtubule-binding protein tau is important in establishing and maintaining neuronal morphology and is a major component of the neurofibrillary tangles (NFTs) characteristic of Alzheimer's brain. The neuron-specific tau transcript undergoes complex alternative splicing. The human tau gene has been cloned and mapped. The restriction analysis and partial sequencing of the gene shows that it contains (1) four alternatively spliced exons previously described in rodent and bovine but not in human tau cDNAs and (2) two CpG islands, one associated with the promoter region, the other with exon 9. Examination of human tau mRNA indicates that the human cerebrocortical splicing pattern differs from that previously reported for the murine and bovine tau mRNAs, despite conserved exon organization in all three genes.

MeSH Terms
Alternative Splicing Amino Acid Sequence Animals Base Sequence DNA Dinucleoside Phosphates/genetics Exons Humans Molecular Sequence Data Polymerase Chain Reaction RNA, Messenger/genetics Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid tau Proteins/genetics
Chemicals
Dinucleoside Phosphates RNA, Messenger tau Proteins cytidylyl-3'-5'-guanosine DNA
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Andreadis A
Department of Neurology (Neuroscience), Harvard Medical School, Boston, Massachusetts.
Brown W M
Kosik K S
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1992-11-03
Pages
10626-33
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Grants
NIA NIH HHS · AG06601 · United States
Databases
GENBANK
M86481, M93652, X61371, X61372, X61373, X61374, X61375, X65732, X65733, X65734
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