BIOMAT Database Logo BIOMAT Database Logo

Protease nexin-2/amyloid beta-protein precursor in blood is a platelet-specific protein. 1991

W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
Department of Microbiology and Molecular Genetics, College of Medicine, University of California, Irvine 92717.

The protease inhibitor, protease nexin-2 (PN-2), is the secreted form of the amyloid beta-protein precursor (APP) which contains the Kunitz protease inhibitor domain. PN-2/APP is an abundant platelet alpha-granule protein which is secreted upon platelet activation. PN-2/APP mRNA is present in cultured endothelial cells and the protein has been detected in plasma. In the present studies we quantitated PN-2/APP in platelets, plasma and several different cell types of the vasculature to identify the repository of the protein in the circulatory system. We report that PN-2/APP is predominantly a platelet protein in the vascular compartment. Lysates of unstimulated umbilical vein endothelial cells, granulocytes or monocytes contained little PN-2/APP based on sensitive functional protease binding and immunoblotting assays. Quantitative immunoblotting studies demonstrated that normal citrated-plasma contains less than or equal to 60 pM PN-2/APP. In contrast, platelets can contribute up to 30 nM PN-2/APP, indicating that they are the major source of the protein in blood.

UI MeSH Term Description Entries
D009000 Monocytes Large, phagocytic mononuclear leukocytes produced in the vertebrate BONE MARROW and released into the BLOOD; contain a large, oval or somewhat indented nucleus surrounded by voluminous cytoplasm and numerous organelles. Monocyte
D011498 Protein Precursors Precursors, Protein
D011956 Receptors, Cell Surface Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands. Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D012016 Reference Values The range or frequency distribution of a measurement in a population (of organisms, organs or things) that has not been selected for the presence of disease or abnormality. Normal Range,Normal Values,Reference Ranges,Normal Ranges,Normal Value,Range, Normal,Range, Reference,Ranges, Normal,Ranges, Reference,Reference Range,Reference Value,Value, Normal,Value, Reference,Values, Normal,Values, Reference
D001792 Blood Platelets Non-nucleated disk-shaped cells formed in the megakaryocyte and found in the blood of all mammals. They are mainly involved in blood coagulation. Platelets,Thrombocytes,Blood Platelet,Platelet,Platelet, Blood,Platelets, Blood,Thrombocyte
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D004730 Endothelium, Vascular Single pavement layer of cells which line the luminal surface of the entire vascular system and regulate the transport of macromolecules and blood components. Capillary Endothelium,Vascular Endothelium,Capillary Endotheliums,Endothelium, Capillary,Endotheliums, Capillary,Endotheliums, Vascular,Vascular Endotheliums
D006098 Granulocytes Leukocytes with abundant granules in the cytoplasm. They are divided into three groups according to the staining properties of the granules: neutrophilic, eosinophilic, and basophilic. Mature granulocytes are the NEUTROPHILS; EOSINOPHILS; and BASOPHILS. Granulocyte
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D015151 Immunoblotting Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies. Dot Immunoblotting,Electroimmunoblotting,Immunoelectroblotting,Reverse Immunoblotting,Immunoblotting, Dot,Immunoblotting, Reverse,Dot Immunoblottings,Electroimmunoblottings,Immunoblottings,Immunoblottings, Dot,Immunoblottings, Reverse,Immunoelectroblottings,Reverse Immunoblottings

Related Publications

W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
Protease nexin-2/amyloid beta-protein precursor: a cerebral anticoagulant?
November 1993, The Journal of clinical investigation,
W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
Protease nexin-2/amyloid beta-protein precursor limits cerebral thrombosis.
December 2005, Proceedings of the National Academy of Sciences of the United States of America,
W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
Immunopurification and protease inhibitory properties of protease nexin-2/amyloid beta-protein precursor.
June 1990, The Journal of biological chemistry,
W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
The predominant form of the amyloid beta-protein precursor in human brain is protease nexin 2.
November 1991, Proceedings of the National Academy of Sciences of the United States of America,
W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
The amyloid precursor protein/protease nexin 2 Kunitz inhibitor domain is a highly specific substrate of mesotrypsin.
January 2010, The Journal of biological chemistry,
W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
Fibrillar amyloid beta-protein binds protease nexin-2/amyloid beta-protein precursor: stimulation of its inhibition of coagulation factor XIa.
June 2000, Biochemistry,
W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
Protease nexin-II, a potent antichymotrypsin, shows identity to amyloid beta-protein precursor.
October 1989, Nature,
W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
Increased severity of hemorrhage in transgenic mice expressing cerebral protease nexin-2/amyloid beta-protein precursor.
September 2007, Stroke,
W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
Zinc (II) selectively enhances the inhibition of coagulation factor XIa by protease nexin-2/amyloid beta-protein precursor.
April 1995, Thrombosis research,
W E Van Nostrand, and A H Schmaier, and J S Farrow, and D B Cines, and D D Cunningham
High level expression, purification, and characterization of the Kunitz-type protease inhibitor domain of protease nexin-2/amyloid beta-protein precursor.
July 1992, Biochemical and biophysical research communications,
Copied contents to your clipboard!