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(American Journal of Pathology. 1999;155:1953-1965.)
© 1999 American Society for Investigative Pathology

Regular Articles

Human Vascular Adhesion Protein-1 in Smooth Muscle Cells

Kimmo Jaakkola^*, Katja Kaunismäki^*, Sami Tohka^*, Gennady Yegutkin^*, Esko Vänttinen, Tapani Havia, Lauri J. Pelliniemi^§, Martti Virolainen^¶, Sirpa Jalkanen^* and Marko Salmi^*

From the National Public Health Institute and MediCity Research Laboratory,^*
University of Turku, Turku; the Departments of Medicine
and Surgery,
Turku University Central Hospital, Turku; the Laboratory of Electron Microscopy,^§
University of Turku, Turku; and the Department of Pathology,^¶
Helsinki University Central Hospital, Helsinki, Finland

Human vascular adhesion protein-1 (VAP-1) is a dual-function molecule with adhesive and enzymatic properties. In addition to synthesis in endothelial cells, where it mediates lymphocyte binding, VAP-1 is expressed in smooth muscle cells. Here we studied the expression, biochemical structure, and function of VAP-1 in muscle cells and compared it to those in endothelial cells. VAP-1 is expressed on the plasma membrane of all types of smooth muscle cells, but it is completely absent from cardiac and skeletal muscle cells. In tumors, VAP-1 is retained on all leiomyoma cells, whereas it is lost in half of leiomyosarcoma samples. In smooth muscle VAP-1 predominantly exists as a ~165-kd homodimeric glycoprotein, but a trimeric (~250 kd) form of VAP-1 is also found. It contains N-linked oligosaccharide side chains and abundant sialic acid decorations. In comparison, in endothelial cells dimeric VAP-1 is larger, no trimeric forms are found, and VAP-1 does not have N-glycanase-sensitive oligosaccharides. Unlike endothelial VAP-1, VAP-1 localized on smooth muscle cells does not support binding of lymphocytes. Instead, it deaminates exogenous and endogenous primary amines. In conclusion, VAP-1 in smooth muscle cells is structurally and functionally distinct from VAP-1 present on endothelial cells.

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