Structure of the Human Pancreatic Cholesterol Esterase Gene

B. Vijaya Kumar, Jose A. Aleman-Gomez, Niall Colwell, Angel Lopez-Candales, Matthew S. Bosner, Curtis A. Spilburg, Louis G. Lange, Mark Lowe

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

The gene for human pancreatic cholesterol esterase consists of 11 exons and 10 introns and is 9.2 kb in length. The last and longest exon (841 nucleotides) is unique to the human gene. Functional amino acids are encoded on separate exons. The leader sequence is encoded by a single exon which carries two additional N-terminal amino acids of the mature functional protein. A positive TATA element is identified 43 nucleotides from the start codon. Pulse-field gel electrophoresis and hybridization with various cDNA probes and direct sequence data revealed the existence of a CEase-like gene. Partial sequence analysis of this gene from a human cosmid library and human genomic DNA showed a premature stop signal in exon 10, shortly after the codon for the active-site histidine. Both the functional gene and the CEase-like gene have a polyadenylation signal in the 3ʹ-untranslated region. Thus, the complex gene structure for this intestinally active enzyme may provide in part a potential molecular explanation for the well-known heterogeneity of the intestinal absorption of cholesterol.

Original languageEnglish
Pages (from-to)6077-6081
Number of pages5
JournalBiochemistry
Volume31
Issue number26
DOIs
StatePublished - Feb 1 1992

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