Induction of intracellular signalling in human endothelial cells by the hyaluronan-binding protease involves two distinct pathways.

Recently a novel plasma serine protease with high affinity to hyaluronic acid and glycosaminoglycans, such as heparin and heparan sulfate, has been described and termed hyaluronan-binding protease (HABP). HABP cleaves kininogen in vitro, releasing the vasoactive peptide bradykinin, and activates plasminogen activators, suggesting a vascular cell-directed physiological function of this novel plasma protease. Here we show that HABP stimulates human umbilical vein endothelial cells (HUVECs) by activating two distinct cell-surface receptors.

Novel mutation in the ALS2 gene in juvenile amyotrophic lateral sclerosis.

We present a 32-year-old Turkish male with juvenile amyotrophic lateral sclerosis 2 and a previously unrecognized homozygous deletion in exon 4 of the ALS2 gene (553delA). Disease progression is more rapid than in the ALS2 phenotype cases described to date. The patient's consanguineous parents carry the mutation in the heterozygous state as do his two unaffected brothers.

Inhibition of bFGF/EGF-dependent endothelial cell proliferation by the hyaluronan-binding protease from human plasma.

Recently we identified a plasma serine protease with a high affinity to glycosaminoglycans like heparin or hyaluronic acid, termed hyaluronan-binding protease (HABP). Since glycosaminoglycans are found on cell surfaces and in the extracellular matrix a physiological role of this plasma protease in a pericellular environment was postulated. Here we studied the influence of HABP on the regulation of endothelial cell growth.