CG&D
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Davis, T. L.
Right arrow Articles by Cress, A. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Davis, T. L.
Right arrow Articles by Cress, A. E.
Cell Growth & Differentiation Vol. 13, 107-113, March 2002
© 2002 American Association for Cancer Research

Differential Regulation of a Novel Variant of the {alpha}6 Integrin, {alpha}6p1

Tracy L. Davis, Friederike Buerger and Anne E. Cress2

Department of Radiation Oncology, Arizona Cancer Center [T. L. D., F. B., A. E. C.], and the Department of Molecular and Cellular Biology [A. E. C.], University of Arizona, Tucson, Arizona 85724-5024

We have reported previously the existence of an Mr 70,000 form of the {alpha}6 integrin called {alpha}6p in a variety of human epithelial cell lines. Four different experimental conditions were used to examine the regulation of {alpha}6 and {alpha}6p integrin. The production of the {alpha}6 integrin was decreased by 45% using a protein translation inhibitor (2.25 µM puromycin), whereas production of the {alpha}6p variant was unaffected. The {alpha}6p variant was decreased 60% by actin depolymerization (10 µM cytochalasin D) corresponding to a decrease in its surface expression, whereas {alpha}6 integrin production was unaffected. The {alpha}6p variant was resistant to endoglycosidase H treatment, whereas the {alpha}6 integrin was both sensitive and resistant to endoglycosidase H treatment, indicating retention in the endoplasmic reticulum and processing through the Golgi apparatus. Additionally, digestion by endoglycosidase F demonstrated both {alpha}6p and {alpha}6 integrin contained NH2-linked glycosylations and both shifted Mr ~10,000 on enzymatic digestion. Finally, inhibition of serine/threonine phosphatases by either calyculin A (15 nM) or okadaic acid (62 µM) did not affect {alpha}6p, whereas the production of {alpha}6 integrin was decreased by 50%. These data suggest that the production of the {alpha}6p variant is distinct from {alpha}6 integrin and may involve a post-translational processing event at the cell surface.




This article has been cited by other articles:


Home page
J Biol ChemHome page
J. Liu, P. B. Gurpur, and S. J. Kaufman
Genetically Determined Proteolytic Cleavage Modulates {alpha}7{beta}1 Integrin Function
J. Biol. Chem., December 19, 2008; 283(51): 35668 - 35678.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation
Copyright © 2002 by the American Association of Cancer Research.