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N‐terminal peptide fragments of lipocortin‐1 inhibit a549 cell growth and block EGF‐induced stimulation of proliferation
Author(s) -
Croxtall J. D.,
Waheed S.,
Choudhury Q.,
Anand R.,
Flower R. J.
Publication year - 1993
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910540124
Subject(s) - peptide , cell growth , stimulation , a549 cell , tyrosine , epidermal growth factor , peptide sequence , annexin , annexin a1 , biology , microbiology and biotechnology , chemistry , biochemistry , cell , endocrinology , receptor , gene
Lipocortin‐1 mediates growth inhibition of glucocorticoids in A549 cells by suppressing the release of PGE 2 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 PGE 2 , whereas peptides 1–12 and 13–25 (Phe 21 ; in which the tyrosine at position 21 was replaced by a phenylalanine residue) were inactive. Similarly, peptide 21–33 (Phe 21 ) and a scrambled sequence of 13–25 failed to inhibit cell growth. Moreover, the EGF‐induced stimulation of cell proliferation and PGE 2 release in these cells was blocked by peptides 13–25 and 21–33, and also by peptides 1–12, 13–25 (Phe 21 ) and 21–33 (Phe 21 ), but not by a scrambled sequence of peptide 13–25.