Open AccessEfficient synthesis of human type alpha transforming growth factor: its physical and biological characterization.
Author(s) -
James P. Tam,
Maqsood A. Sheikh,
David Solomon,
Liliana Ossowski
Publication year - 1986
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.83.21.8082
Subject(s) - tgf alpha , epidermal growth factor , transforming growth factor , edman degradation , growth factor , amino acid , biology , transforming growth factor, beta 3 , plasminogen activator , stimulation , alpha (finance) , peptide sequence , cell culture , microbiology and biotechnology , biochemistry , chemistry , receptor , endocrinology , gene , medicine , construct validity , genetics , nursing , patient satisfaction
Human transforming growth factor type alpha (TGF-alpha) was synthesized by a stepwise solid-phase method with an overall yield of 26%. Synthetic TGF-alpha, consisting of 50 amino acid residues deduced from a cDNA precursor sequence, was purified in a single HPLC step. The homogeneity and primary structure were confirmed by several criteria including Edman degradation and mass spectrometry. Synthetic TGF-alpha was as active as murine epidermal growth factor in binding to the epidermal growth factor receptor and in stimulation of anchorage-dependent and of anchorage-independent growth of normal indicator cells in culture. Synthetic TGF-alpha stimulated plasminogen activator production in A 431 and HeLa cells; the stimulation was similar to that induced by epidermal growth factor. Furthermore, synthetic human TGF-alpha showed similar immunoreactivity when compared with rat TGF-alpha. Thus, the 50-amino acid TGF-alpha is likely to be the bioactive principle produced and secreted by tumor cell lines.