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The C‐terminal 26‐residue peptide of serpin A1 stimulates proliferation of breast and liver cancer cells: role of protein kinase C and CD47
Author(s) -
Congote Luis Fernando,
Temmel Nyssa
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.09.035
Subject(s) - cd47 , serpin , peptide , residue (chemistry) , chemistry , protein kinase a , breast cancer , biochemistry , kinase , cancer research , microbiology and biotechnology , biology , cancer , medicine , cell , gene
C26, the C‐terminal 26 residue peptide of serpin A1, significantly increased cell proliferation in cultures of hepatoma cells, but not in porcine kidney epithelial cells, human skin fibroblasts or keratinocytes. The mitogenic activity of C26 was preferentially inhibited with a protein kinase C (PKC) inhibitor, an antibody against CD47 and CD47 short interfering RNA. The mutant C26‐K19R,N22M, imitating a thrombospondin‐like cell adhesion motif, increased the mitogenic activity in both Hep G2 cells and MCF‐7 breast cancer cells. Phosphorylation of C26 at T24 (a putative PKC phosphorylation site) resulted in a 1.9–2.5 increase in mitogenic activity over C26 in MCF‐7 cells.