N-terminal peptide fragments of lipocortin-1 inhibit A549 cell growth and block EGF-induced stimulation of proliferation

• Published in: International journal of cancer Vol. 54; no. 1; p. 153
• Main Authors: Croxtall, J D, Waheed, S, Choudhury, Q, Anand, R, Flower, R J
• Format: Journal Article
• Language: English
• Published: United States 22.04.1993
• Subjects: Adenocarcinoma - pathology; Amino Acid Sequence; Annexin A1 - chemistry; Annexin A1 - pharmacology; Cell Division - drug effects; Dinoprostone - metabolism; Epidermal Growth Factor - antagonists & inhibitors; Humans; Lung Neoplasms - pathology; Molecular Sequence Data; Peptide Fragments - pharmacology; Tumor Cells, Cultured
• ISSN: 0020-7136
• DOI: 10.1002/ijc.2910540124

Lipocortin-1 mediates growth inhibition of glucocorticoids in A549 cells by suppressing the release of PGE2 necessary for their proliferation. We now show that 2 peptide fragments derived from the N-terminal portion of lipocortin-1 corresponding to amino-acids 13-25 and 21-33 also inhibited A549 cell growth and suppressed release of PGE2, whereas peptides 1-12 and 13-25 (Phe21; in which the tyrosine at position 21 was replaced by a phenylalanine residue) were inactive. Similarly, peptide 21-33 (Phe21) and a scrambled sequence of 13-25 failed to inhibit cell growth. Moreover, the EGF-induced stimulation of cell proliferation and PGE2 release in these cells was blocked by peptides 13-25 and 21-33, and also by peptides 1-12, 13-25 (Phe21) and 21-33 (Phe21), but not by a scrambled sequence of peptide 13-25.