Abstract
We cloned a novel isoform of presenilin I (presenilin I-374) besides previously published presenilin I-467 and I-463 in human lymphocytes. Presenilin I-463 was identical to presenilin I-467 except a 12 bp nucleotides deletion in its amino terminal region. Another isoform, presenilin I-374 was produced by an alternative splicing with an additional exon consisting of 92 bp nucleotides (exon 11), which resulted in the frame shift with a stop codon to generate a truncated presenilin consisting of 374 amino acids. The transcripts for presenilin I-467/463 was ubiquitously detected while that for presenilin I-374 was selectively detected in liver, spleen, kidney. Abnormal behavior of presenilin I on gel electrophoresis was found with affinity-purified antibodies against presenilin I.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alzheimer Disease / metabolism
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Amino Acid Sequence
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Antibodies
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Base Sequence
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Brain / metabolism*
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Cloning, Molecular
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DNA Primers
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DNA, Complementary
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Exons
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Humans
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Kidney / metabolism
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Leukocytes / metabolism
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Liver / metabolism
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Membrane Proteins* / biosynthesis*
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Membrane Proteins* / chemistry
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Molecular Sequence Data
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Organ Specificity
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Peptide Fragments / chemical synthesis
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Peptide Fragments / immunology
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Polymerase Chain Reaction
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Presenilin-1
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Protein Biosynthesis
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Recombinant Proteins / biosynthesis
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Sequence Deletion
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Sequence Homology, Amino Acid
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Spleen / metabolism
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Transcription, Genetic
Substances
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Antibodies
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DNA Primers
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DNA, Complementary
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Membrane Proteins
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PSEN1 protein, human
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Peptide Fragments
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Presenilin-1
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Recombinant Proteins
Associated data
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GENBANK/U40379
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GENBANK/U40380