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Journal of Histochemistry and Cytochemistry
Volume 52 (4): 491-499, 2004
Copyright ©The Histochemical Society, Inc.

Cell Type-specific Expression of ß-Carotene 15,15'-Mono-oxygenase in Human Tissues

Annika Lindqvist and Stefan Andersson

Departments of Obstetrics–Gynecology and Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas

Correspondence to: Stefan Andersson, U. of Texas Southwestern Medical Center, Obstetrics–Gynecology, F2.106, 5323 Harry Hines Blvd, Dallas, TX 75390-9032. E-mail: stefan.andersson{at}utsouthwestern.edu

We studied the cell type-specific expression of human ß-carotene 15,15'-mono-oxygenase (BCO1), an enzyme that catalyzes the first step in the conversion of dietary provitamin A carotenoids to vitamin A. Immunohistochemical analysis using two monoclonal antibodies against different epitopes of the protein revealed that BCO1 is expressed in epithelial cells in a variety of human tissues, including mucosa and glandular cells of stomach, small intestine, and colon, parenchymal cells in liver, cells that make up the exocrine glands in pancreas, glandular cells in prostate, endometrium, and mammary tissue, kidney tubules, and in keratinocytes of the squamous epithelium of skin. Furthermore, BCO1 is detected in steroidogenic cells in testis, ovary, and adrenal gland, as well as skeletal muscle cells. Epithelia in general are structures that are very sensitive to vitamin A deficiency, and although the extraintestinal function of BCO1 is unclear, the finding that the enzyme is expressed in all epithelia examined thus far leads us to suggest that BCO1 may be important for local synthesis of vitamin A, constituting a back-up pathway of vitamin A synthesis during times of insufficient dietary intake of vitamin A.

(J Histochem Cytochem 52:491–499, 2004)

Key Words: ß-carotene • 15,15'-mono-oxygenase • human • epithelia • vitamin A • ß-carotene • immunohistochemistry


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