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The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors.

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  • 2000-10-18
Published in:
  • The Journal of biological chemistry. - 2001
Amino Acid Sequence
Amyloid beta-Protein Precursor
Androgen-Binding Protein
Animals
Brain Chemistry
Carrier Proteins
Cell Line
Chromatography, Gel
Chymotrypsin
Kallikreins
Kinetics
Membrane Proteins
Mice
Mice, Inbred C57BL
Mice, Knockout
Molecular Sequence Data
Mutation
Phosphatidylethanolamine Binding Protein
Phospholipid Transfer Proteins
Precipitin Tests
Prostatein
Protease Nexins
Rats
Receptors, Cell Surface
Recombinant Proteins
Secretoglobins
Sequence Analysis, Protein
Serine Endopeptidases
Serine Proteinase Inhibitors
Serpin E2
Spectrometry, Mass, Electrospray Ionization
Thrombin
Uteroglobin
English Serine proteases are involved in many processes in the nervous system and specific inhibitors tightly control their proteolytic activity. Thrombin is thought to play a role in tissue development and homeostasis. To date, protease nexin-1 is the only known endogenous protease inhibitor that specifically interferes with thrombotic activity and is expressed in the brain. In this study, we report the detection of a novel thrombin inhibitory activity in the brain of protease nexin-1(-/-) mice. Purification and subsequent analysis by tandem mass spectrometry identified this protein as the phosphatidylethanolamine-binding protein (PEBP). We demonstrate that PEBP exerts inhibitory activity against several serine proteases including thrombin, neuropsin, and chymotrypsin, whereas trypsin, tissue type plasminogen activator, and elastase are not affected. Since PEBP does not share significant homology with other serine protease inhibitors, our results define it as the prototype of a novel class of serine protease inhibitors. PEBP immunoreactivity is found on the surface of Rat-1 fibroblast cells and although its sequence contains no secretion signal, PEBP-H(6) can be purified from the conditioned medium upon recombinant expression.
Language
  • English
Open access status
bronze
Identifiers
Persistent URL
https://folia.unifr.ch/global/documents/53951
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