Thrombin B-Loop Peptide (B-Lp) Has Specific Receptors On Macrophages View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1987-04

AUTHORS

Sherin Devaskar, Lynn Karycki, George Wilner, Arnold Kahn

ABSTRACT

α-Thrombin, a serine protease with potent procoagulant activity, has the capacity to stimulate the proliferation of fibroblasts, vascular endothelial cells and macrophages. However, for the latter cell type, esterolytically intact enzyme is not required and, in fact, the mitogenic potency of the molecule appears to reside in a limited unique region of thrombin termed the B-loop peptide (B-LP). In an attempt to determine the mechanism by which B-LP mediates mitogenesis, B-LP sensitive J774.1 macrophage cells were fixed in paraformaldehyde and incubated for 1 hr with 125I B-LP in the presence and absence of exogenous unlabeled ligand (10−10-10−7)(n=5). The data show that the J744.1 cells possess a specific, saturable B-LP receptor that exhibits a Kd of ∼1.12 nM; a value that coincides with the concentration of peptide necessary to optimally elicit a mitogenic response in these cells. Native α-thrombin, inactivated DIP-thrombin and unlabeled B-LP displace bound 125-labeled B-LP from J774 cells at equimolar concentrations suggesting that all the 3 peptides interact with a common receptor site on macrophages. Scatchard analysis indicates that ∼ 4000 such receptors are present per cell. We suggest that ligand activation of these receptors is responsible for triggering the biological response associated with thrombin-stimulated macrophages, and therefore, is likely pivotal in promoting the accumulation of these cells during the processes of inflammation and wound healing. More... »

PAGES

298-298

Identifiers

URI

http://scigraph.springernature.com/pub.10.1203/00006450-198704010-00783

DOI

http://dx.doi.org/10.1203/00006450-198704010-00783

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020916863


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