A PENTACOSAPEPTIDE (CKS-25) HOMOLOGOUS TO RETROVIRAL ENVELOPE PROTEINS POSSESSES A TRANSFORMING-GROWTH-FACTOR-BETA ACTIVITY

Authors
Citation
Ss. Huang et Js. Huang, A PENTACOSAPEPTIDE (CKS-25) HOMOLOGOUS TO RETROVIRAL ENVELOPE PROTEINS POSSESSES A TRANSFORMING-GROWTH-FACTOR-BETA ACTIVITY, The Journal of biological chemistry, 273(9), 1998, pp. 4815-4818
Citations number
20
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology
ISSN journal
0021-9258
Volume
273
Issue
9
Year of publication
1998
Pages
4815 - 4818
Database
ISI
SICI code
0021-9258(1998)273:9<4815:AP(HTR>2.0.ZU;2-S
Abstract
CKS-17, a synthetic heptadecapeptide homologous to a conserved domain in retroviral envelope protein p15E, mimics the immunosuppressive prop erties of p15E in vitro and in vivo, but the mechanisms are not unders tood. Here we report that a synthetic pentacosapeptide designated CKS- 25, a longer version of CKS-17 that contains a functional transforming growth factor-beta(3) (TGF-beta(3)) active-site motif (RXXD), inhibit s I-125-labeled TGF-beta(1) (I-125-TGF-beta(1)) binding to cell-surfac e TGF-beta receptors in cultured epithelial cells. Multiple conjugatio n of CKS-25 to bovine serum albumin and carbonic anhydrase enhances th e I-125-TGF-beta(1) binding inhibitory activity and confers a partial TGF-beta agonist activity (growth inhibition but not transcriptional a ctivation). Since TGF-beta is a potent immunosuppressive factor, these results suggest that the immunosuppressive properties of CKS-17-bovin e serum albumin conjugate and p15E are mediated at least in part by th eir TGF-beta agonist activities.