Eric B. Lynam
University of New Mexico
11 Papers
237 Citations
Eric B. Lynam is an academic researcher from University of New Mexico. The author has contributed to research in topics: Neutrophil aggregation & L-selectin. The author has an hindex of 9, co-authored 11 publications.
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Papers
•Journal Article
Hydroxamate-based metalloprotease inhibitor blocks shedding of L-selectin adhesion molecule from leukocytes: functional consequences for neutrophil aggregation.
TL;DR: It is shown that a hydroxamate-based metalloprotease inhibitor, N-(D,L-[2-(hydroxyaminocarbonyl)- methyl]-4-methylpentano)-L-3-(tert-butyl)-alanyl-L-alanine, 2-aminoethyl amide, also inhibits L-selectin shedding from neutrophils, eosinophils, and lymphocytes.
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β2-Integrin and L-Selectin Are Obligatory Receptors in Neutrophil Aggregation
TL;DR: The minimum requirement for adhesion between two mixed populations of neutrophils was that one population expressed the beta 2-integrin and the other expressed the L- selectin adhesive epitope, which resulted in an approximately 50% reduction in two-color aggregation as compared with that in unblocked samples.
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•Journal Article
A role for lectin interactions during human neutrophil aggregation.
TL;DR: The results implicate a lectinlike contribution to neutrophil aggregation, and suggest that L-selectin is the molecule that mediates the carbohydrate-dependent adhesive event, as well as suggesting that carbohydrate interactions play a role in aggregation.
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Beta2-integrins mediate stable adhesion in collisional interactions between neutrophils and ICAM-1-expressing cells.
Eric B. Lynam,Larry A. Sklar,A.D. Taylor,Sriram Neelamegham,Bruce S. Edwards,C. W. Smith,Scott I. Simon +6 more
TL;DR: Application of defined shear in a cone and plate viscometer showed that adhesion to the ICAM‐1 cells decreased from a maximum level to baseline as shear rate increased up to 400 s‐1 in a manner typical of integrin adhesion alone, in contrast, homotypic aggregation supported by the transition from selectin to integrin binding exhibited an increase in efficiency up to 800 s-1.
41
Lipopolysaccharide enhances CD11b/CD18 function but inhibits neutrophil aggregation
TL;DR: The data suggest that inhibition of neutrophil aggregation by LPS/LBP is related to the expression of L-selectin via CD14 rather than LPS inhibition of CD11b/CD18 function during cellular stimulation.
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