ArticleThe Biochemical journal1996
Proteinases are isoform-specific regulators of the binding of transforming growth factor beta to alpha 2-macroglobulin.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Agonists and Antagonists of TGF-β Family Ligands.Cold Spring Harbor perspectives in biology · 2016Review
- Gene regulation networks related to neural differentiation of hESC.Gene expression · 2007Article
- Modulation of extracellular matrix genes reflects the magnitude of physiological adaptation to aerobic exercise training in humans.BMC biology · 2005Article
- Increased Trypanosoma cruzi invasion and heart fibrosis associated with high transforming growth factor beta levels in mice deficient in alpha(2)-macroglobulin.Infection and immunity · 2002Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
alpha 2-Macroglobulin (alpha 2M) regulates growth and gene expression in many cell types by binding and neutralizing transforming growth factor beta (TGF-beta). In this study we characterized the effects of the serine proteinase, plasmin, on the interaction of alpha 2M with TGF-beta 1 and TGF-beta 2. Binding of both TGF-beta isoforms to purified alpha 2M-plasmin complex was primarily non-covalent and reversible. The binding affinity of alpha 2M for TGF-beta 1 was increased by plasmin; the Kd values were 320 and 84 nM for native alpha 2M and alpha 2M-plasmin respectively. In contrast the affinity of alpha 2M for TGF-beta 2 was decreased by plasmin; the Kd values were 14 and 80 nM for native alpha 2M and alpha 2M-plasmin respectively. Thrombin decreased the affinity of alpha 2M for TGF-beta 2 in a similar manner to plasmin. In assays of DNA synthesis in fetal bovine heart endothelial cells, native alpha 2M neutralized the activity of exogenously added TGF-beta 2, whereas alpha 2M-plasmin, at equivalent concentrations, had almost no effect. Native alpha 2M and methylamine-modified alpha 2M increased platelet-derived growth factor alpha-receptor expression in vascular smooth-muscle cells, an activity attributed to the neutralization of autocrine TGF-beta activity, whereas alpha 2M-plasmin was less effective at the same concentration. These studies demonstrate that the effects of proteinases on the cytokine-binding and cytokine-neutralizing activities of alpha 2M are cytokine-dependent. By reacting with alpha 2M, proteinases might regulate not only the availability of cytokines in the extracellular spaces but also the composition of the cytokine milieu.
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