Journal ArticleDOI
Endothelial leukocyte adhesion molecule 1: an inducible receptor for neutrophils related to complement regulatory proteins and lectins
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TLDR
Endothelial leukocyte adhesion molecule-1 (ELAM-1), a cell surface glycoprotein expressed by cytokine-activated endothelium, mediates the adhesion of blood neutrophils and may be a member of a nascent gene family of cell surface molecules involved in the regulation of inflammatory and immunological events at the interface of vessel wall and blood.Abstract:
Focal adhesion of leukocytes to the blood vessel lining is a key step in inflammation and certain vascular disease processes. Endothelial leukocyte adhesion molecule-1 (ELAM-1), a cell surface glycoprotein expressed by cytokine-activated endothelium, mediates the adhesion of blood neutrophils. A full-length complementary DNA (cDNA) for ELAM-1 has now been isolated by transient expression in COS cells. Cells transfected with the ELAM-1 clone express a surface structure recognized by two ELAM-1 specific monoclonal antibodies (H4/18 and H18/7) and support the adhesion of isolated human neutrophils and the promyelocytic cell line HL-60. Expression of ELAM-1 transcripts in cultured human endothelial cells is induced by cytokines, reaching a maximum at 2 to 4 hours and decaying by 24 hours; cell surface expression of ELAM-1 protein parallels that of the mRNA. The primary sequence of ELAM-1 predicts an amino-terminal lectin-like domain, an EGF domain, and six tandem repetitive motifs (about 60 amino acids each) related to those found in complement regulatory proteins. A similar domain structure is also found in the MEL-14 lymphocyte cell surface homing receptor, and in granule-membrane protein 140, a membrane glycoprotein of platelet and endothelial secretory granules that can be rapidly mobilized (less than 5 minutes) to the cell surface by thrombin and other stimuli. Thus, ELAM-1 may be a member of a nascent gene family of cell surface molecules involved in the regulation of inflammatory and immunological events at the interface of vessel wall and blood.read more
Citations
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Journal ArticleDOI
Adhesion receptors of the immune system.
TL;DR: Three families of cell-surface molecules regulate the migration of lymphocytes and the interactions of activated cells during immune responses.
Journal ArticleDOI
Leukocytes roll on a selectin at physiologic flow rates: Distinction from and prerequisite for adhesion through integrins
TL;DR: Rolling of leukocytes on vascular endothelial cells, an early event in inflammation, can be reproduced in vitro on artificial lipid bilayers containing purified CD62, a selectin also named PADGEM and GMP-140 that is inducible on endothelial Cells.
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DNA Fragments in the Blood Plasma of Cancer Patients: Quantitations and Evidence for Their Origin from Apoptotic and Necrotic Cells
Sabine Jahr,Hannes Hentze,Sabine Englisch,Dieter Hardt,Frank O. Fackelmayer,Rolf-Dieter Hesch,Rolf Knippers +6 more
TL;DR: By quantitative methylation-specific PCR of the promoter region of the CDKN2A tumor suppressor gene, the fraction of plasma DNA derived from tumor cells is quantified and is consistent with the possibility that apoptotic and necrotic cells are a major source for plasma DNA in cancer patients.
Journal ArticleDOI
VCAM-1 on activated endothelium interacts with the leukocyte integrin VLA-4 at a site distinct from the VLA-4/Fibronectin binding site
Mariano J. Elices,Laurelee Osborn,Yoshikazu Takada,Carol Crouse,Stefan Luhowskyj,Martin E. Hemler,Roy R. Lobb +6 more
TL;DR: The VCAM-1/VLA-4 ligand-receptor pair may play a major role in the recruitment of mononuclear leukocytes to inflammatory sites in vivo.
Journal ArticleDOI
Direct expression cloning of vascular cell adhesion molecule 1, a cytokine-induced endothelial protein that binds to lymphocytes.
Laurelee Osborn,Catherine Hession,Richard Tizard,Cornelia Vassallo,Stefan Luhowskyj,Gloria Chi-Rosso,Roy R. Lobb +6 more
TL;DR: A previously undescribed adhesion molecule, VCAM-1, which is induced by cytokines on human endothelial cells and binds lymphocytes is cloned using a novel method requiring neither monoclonal antibodies nor purified protein.
References
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