Affiliation:
1. Departments of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, U.S.A.
Abstract
α1-Proteinase inhibitor is a serpin and can inhibit most serine proteinases. The cornea is one of several extrahepatic tissues that synthesizes this inhibitor. In the presence of retinol, corneal α1-proteinase inhibitor levels were increased 3.8-fold. The maximal response was achieved 2 h after the addition of retinol (1 μM final concentration) to the culture medium. A similar increase in α1-proteinase inhibitor was observed with retinaldehyde (1 nM final concentration). Concentrations of α1-proteinase inhibitor in other tested cells (Hep G2, CaCo 2, MCF-7, monocytes and macrophages) remained unchanged in the presence of retinol. Retinoic acid did not affect α1-proteinase inhibitor levels in the cornea or the other cells tested. The acute-phase cytokine, interleukin-6, increased α1-proteinase inhibitor levels in all tested tissues/cells except the cornea. These results demonstrate that α1-proteinase inhibitor levels are controlled differently in the cornea compared with other tissues/cells. α1-Proteinase inhibitor is the first protein identified whose levels are regulated by a mechanism supported by retinol and retinaldehyde but not retinoic acid.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
13 articles.
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