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J Biol Chem, Vol. 273, Issue 9, 4815-4818, February 27, 1998

COMMUNICATION
A Pentacosapeptide (CKS-25) Homologous to Retroviral Envelope Proteins Possesses a Transforming Growth Factor-beta Activity

Shuan Shian Huang and Jung San Huang

From the Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, St. Louis, Missouri 63104

CKS-17, a synthetic heptadecapeptide homologous to a conserved domain in retroviral envelope protein p15E, mimics the immunosuppressive properties of p15E in vitro and in vivo, but the mechanisms are not understood. 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), inhibits 125I-labeled TGF-beta 1 (125I-TGF-beta 1) binding to cell-surface TGF-beta receptors in cultured epithelial cells. Multiple conjugation of CKS-25 to bovine serum albumin and carbonic anhydrase enhances the 125I-TGF-beta 1 binding inhibitory activity and confers a partial TGF-beta agonist activity (growth inhibition but not transcriptional activation). Since TGF-beta is a potent immunosuppressive factor, these results suggest that the immunosuppressive properties of CKS-17-bovine serum albumin conjugate and p15E are mediated at least in part by their TGF-beta agonist activities.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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