Literature DB >> 10402238

Expression of full length or truncated epidermal growth factor precursor transforms NIH3T3 fibroblasts.

R W Kwan1, R W Wong, S Y Chan.   

Abstract

Epidermal growth factor (EGF) is derived from a large precursor (EGFP) of unusual structure. As EGFP remains unprocessed in certain tissues, it is of biological relevance to study its activity. Activation of the EGF receptor by EGF is involved in transformation of NIH3T3 fibroblasts. We isolated clones of NIH3T3 expressing full length, cytoplasmic region deleted or EGF-repeats deleted EGFP. All clones formed colonies in soft agarose and tumors in nude mice. Two clones expressing EGF-repeats deleted EGFP formed more and larger colonies. To conclude, EGFP is biologically active. Deletion of the 8 EGF repeats may enhance anchorage independent growth in NIH3T3.

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Year:  1999        PMID: 10402238     DOI: 10.3892/ijo.15.2.281

Source DB:  PubMed          Journal:  Int J Oncol        ISSN: 1019-6439            Impact factor:   5.650


  3 in total

1.  Proprotein convertase PC7 enhances the activation of the EGF receptor pathway through processing of the EGF precursor.

Authors:  Estelle Rousselet; Suzanne Benjannet; Edwidge Marcinkiewicz; Marie-Claude Asselin; Claude Lazure; Nabil G Seidah
Journal:  J Biol Chem       Date:  2011-01-05       Impact factor: 5.157

2.  Semiquantitative immunoblots of membrane protein-epidermal growth factor.

Authors:  R W Wong; S Y Chan
Journal:  Mol Biotechnol       Date:  2000-05       Impact factor: 2.695

Review 3.  Epidermal growth factor, from gene organization to bedside.

Authors:  Fenghua Zeng; Raymond C Harris
Journal:  Semin Cell Dev Biol       Date:  2014-02-07       Impact factor: 7.727

  3 in total

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