In:
FEBS Letters, Wiley, Vol. 267, No. 1 ( 1990-07-02), p. 135-138
Abstract:
Magainins are a family of antimicrobial peptides present in the skin extracts of Xenopus laevis . Both magainin‐1 and ‐2 do not have any significant effect on the activity of protein kinase C (PKC). Magainin‐2 was found to be readily phosphorylated by PKC to 0.5 mol‐ 32 P/mol of peptide. Neither magainin‐1, which has a sequence of S 8 AGK and not S 8 AKK as in the case of magainin‐2, nor the magainin‐2 analogue with substitution of Ala for Ser 8 was phosphorylated by the kinase, suggesting that Ser 8 is the phosphorylation site of magainin‐2. One synthetic analogue of magainin, designated magainin B, which has a greater tendency for α‐helix formation in non‐aqueous environment than the parent peptide resulting from substitution of Ser 8 , Gly 13 , and Gly 18 with Ala in magainin‐2‐amide, is a potent inhibitor of PKC. This peptide inhibits all three PKC isozymes with IC 50 less than 20 μM. Magainin B also inhibits the binding of [ 3H ]phorbol 12,13‐dibutyrate to the kinase. These results suggest that magainin‐2 may be modified by PKC through phosphorylation and that certain synthetic analogues of magainins may be used as inhibitors of PKC.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(90)80307-5
Language:
English
Publisher:
Wiley
Publication Date:
1990
detail.hit.zdb_id:
1460391-3
SSG:
12
Permalink