Journal article
Tyrosine phosphorylation of maspin in normal mammary epithelia and breast cancer cells
Biochemical and biophysical research communications, Vol.295(4), pp.800-805
2002
DOI: 10.1016/S0006-291X(02)00764-7
PMID: 12127964
Abstract
Maspin is a 42
kDa tumor suppressor protein that belongs to the serine protease inhibitor (serpin) family. It inhibits cell motility and invasion in vitro, and tumor growth and metastasis in nude mice; however, maspin's molecular mechanism of action has remained elusive. Maspin contains several tyrosine residues and we hypothesized that phosphorylation of maspin could play a role in its biological function. Our study reveals that maspin is phosphorylated on tyrosine moiety(ies) in normal mammary epithelial cells endogenously expressing maspin. In addition, transfection of the maspin gene, using either a stable or inducible system into maspin-deficient breast cancer cell lines, yields a protein product that is phosphorylated on tyrosine residue(s). Furthermore, recombinant maspin protein can be tyrosine-phosphorylated by the kinase domain from the epidermal growth factor receptor in vitro. These novel observations suggest that maspin, which deviates from the classical serpin, may be an important signal transduction molecule in its phosphorylated form.
Details
- Title: Subtitle
- Tyrosine phosphorylation of maspin in normal mammary epithelia and breast cancer cells
- Creators
- Valerie A Odero-Marah - Department of Anatomy and Cell Biology, The Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA 52242, USAZhila Khalkhali-Ellis - Department of Anatomy and Cell Biology, The Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA 52242, USAGalen B Schneider - Holden Comprehensive Cancer Center at The University of Iowa, Iowa City, IA 52242, USAElisabeth A Seftor - Department of Anatomy and Cell Biology, The Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA 52242, USARichard E.B Seftor - Department of Anatomy and Cell Biology, The Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA 52242, USAJohn G Koland - Department of Pharmacology, The Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA 52242, USAMary J.C Hendrix - Department of Anatomy and Cell Biology, The Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA 52242, USA
- Resource Type
- Journal article
- Publication Details
- Biochemical and biophysical research communications, Vol.295(4), pp.800-805
- Publisher
- Elsevier Inc
- DOI
- 10.1016/S0006-291X(02)00764-7
- PMID
- 12127964
- ISSN
- 0006-291X
- eISSN
- 1090-2104
- Language
- English
- Date published
- 2002
- Academic Unit
- Dentistry Administration; Prosthodontics; Neuroscience and Pharmacology
- Record Identifier
- 9984065806302771
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