Cloning and sequence analysis of a cDNA for rat transforming growth factor-α

@article{Lee1985CloningAS,
  title={Cloning and sequence analysis of a cDNA for rat transforming growth factor-$\alpha$},
  author={David C. Lee and Timothy M. Rose and Nancy R. Webb and George J. Todaro},
  journal={Nature},
  year={1985},
  volume={313},
  pages={489-491}
}
Transforming growth factors (TGFs) are mitogenic polypeptides produced most conspicuously by transformed cells and conferring on normal cells several phenotypic alterations associated with transformation1,2. TGFs comprise two distinct sets of molecules: TGF-αs are structurally similar to epidermal growth factor (EGF), binding to and inducing the tyrosine phosphorylation of the EGF receptor in a manner indistinguishable from that of EGF3. In addition, the 50-amino acid rat TGF-α4 has 33 and 44… 
Expression and characterization of transforming growth factor alpha precursor protein in transfected mammalian cells.
TLDR
Cell fractionation studies indicate that the Mr 13,000 to 17,000 species expressed in induced 5:2 cells is membrane associated, consistent with predictions based on the cDNA sequence of the TGF alpha precursor.
Expression and characterization of transforming growth factor alpha precursor protein in transfected mammalian cells
TLDR
Cell fractionation studies indicate that the Mr 13,000 to 17,000 species expressed in induced 5:2 cells is membrane associated, consistent with predictions based on the cDNA sequence of the TGF alpha precursor.
Synthesis of biologically active transforming growth factor alpha.
  • J. Tam
  • Biology, Chemistry
    International journal of peptide and protein research
  • 1987
TLDR
The chemical synthesis of TGF alpha provided convincing evidence that TGFalpha is functionally related to EGF and is one of the active principles required for cellular transformation.
Isolation of Genomic Sequence Encoding a Biologically Active Bovine TGF- α Protein
TLDR
Bovine TGF-α may be a normal regulator of cell growth in the bovine animal and its mitogenic activity is comparable to that of human EGF in causing proliferation of bovines mammary epithelial cells.
Proteolytic maturation of transforming growth factor-α
TLDR
Elastase-like enzymes, purified from transformed Schwann or liver epithelial cells, are inhibited in a time- and concentration-dependent fashion with three differently substituted monocyclic β-lactam-based compounds originally developed as specific inhibitors of polymorphonuclear leukocyte elastase, thus further supporting the elast enzyme-like character of the putative pro-TGF-α processing enzymes.
A truncated, secreted form of the epidermal growth factor receptor is encoded by an alternatively spliced transcript in normal rat tissue
TLDR
Southern blot analysis of rat genomic DNA indicated that the 3'-terminal sequence of this transcript is derived from the EGF-R gene, and Northern (RNA blot) analysis established that the truncated receptor is encoded by a 2.7-kb mRNA which codes for a truncated form of the receptor.
Characterization of high molecular weight transforming growth factor alpha produced by rat hepatocellular carcinoma cells.
TLDR
The size and soluble nature of this polypeptide suggest that it represents the extracellular domain of the transmembrane TGF alpha precursor.
Retroviral expression of transforming growth factor-alpha does not transform fibroblasts or keratinocytes.
TLDR
It is suggested that overexpression of TGF alpha does not, by itself, transform rodent fibroblasts or keratinocytes and exogenously added TGFalpha is an extremely potent mitogen for BALB/MK cells.
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TLDR
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