Abstract:
:Using different binding assays we examined the interaction of the cytokine interleukin 4 (IL-4) with basement membrane. Equilibrium binding analysis revealed a high-affinity site characterized by a dissociation constant (Kd) of 0.3 nM. This interaction was confirmed by native polyacrylamide gel electrophoresis, which also indicated that the binding sites are composed of glycosaminoglycans (GAGs). In competition studies, N-sulfated GAGs (heparin and heparan sulfate) displayed a higher affinity than other GAGs for IL-4, and therefore may constitute the physiological ligand. Furthermore, the enzymatic and chemical cleavage of heparan sulfate demonstrated that only few peculiar domains (i.e. N-sulfated rich sequences) within heparan sulfate chains, displayed a significant affinity for IL-4. These data indicate a possible role of GAGs in storing IL-4 and modulating the cellular response to this cytokine.
journal_name
Cytokinejournal_title
Cytokineauthors
Lortat-Jacob H,Garrone P,Banchereau J,Grimaud JAdoi
10.1006/cyto.1996.0142subject
Has Abstractpub_date
1997-02-01 00:00:00pages
101-5issue
2eissn
1043-4666issn
1096-0023pii
S1043-4666(96)90142-8journal_volume
9pub_type
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