Author
Douglas M. Tollefsen
Other affiliations: McMaster University Medical Centre, Cornell University, University of Colorado Boulder ...read more
Bio: Douglas M. Tollefsen is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Heparin cofactor II & Thrombin. The author has an hindex of 43, co-authored 110 publications receiving 7339 citations. Previous affiliations of Douglas M. Tollefsen include McMaster University Medical Centre & Cornell University.
Topics: Heparin cofactor II, Thrombin, Dermatan sulfate, Heparin, Antithrombin
Papers published on a yearly basis
Papers
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TL;DR: A large cohort of infants studied consecutively in the postnatal period allowed us to determine the normal development of the human coagulation system in the full-term infant and found that near-adult values are achieved for most components by 6 months of life.
1,003 citations
TL;DR: The postnatal maturation towards adult levels was accelerated in premature infants as compared with the fullterm infants and with adults.
614 citations
TL;DR: It is suggested that HCII is the only thrombin inhibitor in human plasma that can be activated by dermatan sulfate.
428 citations
TL;DR: A previously unrecognized heparin-dependent inhibitor of thrombin from human plasma is isolated and is a relatively ineffective inhibitor of coagulation factor Xa.
408 citations
TL;DR: The smallest fragment of dermatan sulfate that bound to heparin cofactor II with high affinity was isolated, and it was found that clustering of these disaccharides must occur during biosynthesis to form the high-affinity binding site for HCII.
306 citations
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TL;DR: A novel signaling mechanism in which thrombin cleaves its receptor's amino-terminal extension to create a new receptor amino terminus that functions as a tethered ligand and activates the receptor is revealed.
2,992 citations
TL;DR: Current analyses of genetic defects in Drosophila melanogaster, mice, and humans confirm most of these activities in vivo and identify additional processes that involve cell surface heparan sulfate proteoglycans.
Abstract: The heparan sulfate on the surface of all adherent cells modulates the actions of a large number of extracellular ligands. Members of both cell surface heparan sulfate proteoglycan families, the transmembrane syndecans and the glycosylphosphoinositide-linked glypicans, bind these ligands and enhance formation of their receptor-signaling complexes. These heparan sulfate proteoglycans also immobilize and regulate the turnover of ligands that act at the cell surface. The extracellular domains of these proteoglycans can be shed from the cell surface, generating soluble heparan sulfate proteoglycans that can inhibit interactions at the cell surface. Recent analyses of genetic defects in Drosophila melanogaster, mice, and humans confirm most of these activities in vivo and identify additional processes that involve cell surface heparan sulfate proteoglycans. This chapter focuses on the mechanisms underlying these activities and on the cellular functions that they regulate.
2,680 citations
TL;DR: The membrane has long been viewed as an inert cellophane-like membrane that lines the circulatory system with its primary essential function being the maintenance of vessel wall permeability.
2,368 citations
1,803 citations
TL;DR: A review of state-of-the-art knowledge on the composition and functions of the endothelial glycocalyx can be found in this article, where the contribution of the glyocalyx to diabetes, ischemia/reperfusion, and atherosclerosis is also reviewed.
Abstract: This review aims at presenting state-of-the-art knowledge on the composition and functions of the endothelial glycocalyx. The endothelial glycocalyx is a network of membrane-bound proteoglycans and glycoproteins, covering the endothelium luminally. Both endothelium- and plasma-derived soluble molecules integrate into this mesh. Over the past decade, insight has been gained into the role of the glycocalyx in vascular physiology and pathology, including mechanotransduction, hemostasis, signaling, and blood cell–vessel wall interactions. The contribution of the glycocalyx to diabetes, ischemia/reperfusion, and atherosclerosis is also reviewed. Experimental data from the micro- and macrocirculation alludes at a vasculoprotective role for the glycocalyx. Assessing this possible role of the endothelial glycocalyx requires reliable visualization of this delicate layer, which is a great challenge. An overview is given of the various ways in which the endothelial glycocalyx has been visualized up to now, including first data from two-photon microscopic imaging.
1,481 citations