Premium
Overexpression of the natural tetrapeptide acetyl‐ N ‐ser‐asp‐lys‐pro derived from thymosin β4 in neoplastic diseases
Author(s) -
Liu JianMiao,
GarciaAlvarez MariaConcepcion,
Big Jerome,
Kusinski Michal,
Kuzdak Krzysztof,
Riches Andrew,
WdzieczakBakala Joanna
Publication year - 2010
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2010.05488.x
Subject(s) - tetrapeptide , angiogenesis , cancer , cancer research , chemistry , oligopeptide , in vivo , biochemistry , biology , medicine , peptide , genetics
The natural tetrapeptide acetyl‐ser‐asp‐lys‐pro (AcSDKP) is formed in vivo by enzymatic cleavage of the N terminus of thymosin β4 by prolyl oligopeptidase (POP). Recently, AcSDKP was shown to promote angiogenesis. Because of the critical role of neovascularization in cancer development, the levels of AcSDKP and POP activity in a number of different malignant tissues were investigated. Our studies revealed that AcSDKP levels were markedly elevated in neoplastic diseases including hematologic malignancies and solid neoplasms. Consistent with this finding, the enhanced activity of POP was also detected in all analyzed specimens of cancer tissues. Both these novel findings are in concert with the previously reported overexpression of thymosin β4 in a large variety of malignant tumors and with its potential role in cancerogenesis. The physiological relevance of these findings awaits further studies; however, our first results strongly suggest a key role for AcSDKP in the pathogenesis of cancer.