Identification and characterization of presenilin I‐467, I‐463 and I‐374

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‐4671463 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.