Retinol and retinaldehyde specifically increase alpha1-proteinase inhibitor in the human cornea. Biochem J 1997 Mar 15;322 ( Pt 3)(Pt 3):751-6
Date
03/15/1997Pubmed ID
9148745Pubmed Central ID
PMC1218251DOI
10.1042/bj3220751Scopus ID
2-s2.0-0030936718 (requires institutional sign-in at Scopus site) 16 CitationsAbstract
alpha1-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 alpha1-proteinase inhibitor levels were increased 3.8-fold. The maximal response was achieved 2 h after the addition of retinol (1 microM final concentration) to the culture medium. A similar increase in alpha1-proteinase inhibitor was observed with retinaldehyde (1 nM final concentration). Concentrations of alpha1-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 alpha1-proteinase inhibitor levels in the cornea or the other cells tested. The acute-phase cytokine, interleukin-6, increased alpha1-proteinase inhibitor levels in all tested tissues/cells except the cornea. These results demonstrate that alpha1-proteinase inhibitor levels are controlled differently in the cornea compared with other tissues/cells. alpha1-Proteinase inhibitor is the first protein identified whose levels are regulated by a mechanism supported by retinol and retinaldehyde but not retinoic acid.
Author List
Bosković G, Twining SSAuthor
Sally S. Twining PhD Assistant Dean, Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
CorneaHumans
Leukocyte Elastase
Organ Culture Techniques
Organ Specificity
Pancreatic Elastase
Retinaldehyde
Vitamin A
alpha 1-Antitrypsin
