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J. Biol. Chem., Vol. 276, Issue 28, 26099-26106, July 13, 2001
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From the The
Identification of a Novel Structural Variant of the
6 Integrin*
,,,
,, and**
Department of Radiation Oncology, University
of Arizona Cancer Center and the ** Department of Molecular and Cellular
Biology, University of Arizona, Tucson, Arizona 85724, the
§ Beth Israel Deaconess Medical Center and Harvard Medical
School, Boston, MA 02215, ¶ Deutsches Krebsforschungszentrum,
Heidelberg 69120, Germany, and the Department of Dermatology,
Oregon Health Sciences University, Portland, Oregon 97201
6 integrin
is a 140-kDa (nonreduced) laminin receptor. We have identified a novel
70-kDa (nonreduced) form of the 6 integrin called
6p for the latin word parvus, meaning small. The variant was immunoprecipitated from human cells using four different 6-specific monoclonal antibodies but not with
3 or 5 antibodies. The 6p
integrin contained identical amino acid sequences within exons 13-25,
corresponding to the extracellular "stalk region" and the
cytoplasmic tail of the 6 integrin. The light chains of
6 and 6p were identical as judged by
6A-specific antibodies and electrophoretic properties.
The 6p variant paired with either 
1 or
4 subunits and was retained on the cell surface three
times longer than 6. Reverse transcription/polymerase
chain reaction analysis revealed a single polymerase chain reaction product. The 6p variant was found in human prostate
(DU145H, LnCaP, PC3) and colon (SW480) cancer cell lines but not in
normal prostate (PrEC), breast cancer (MCF-7), or lung cancer (H69)
cell lines or a variant of a prostate carcinoma cell line (PC3-N). Protein levels of 6p increased 3-fold during
calcium-induced terminal differentiation in a normal mouse keratinocyte
model system. A novel form of the 6 integrin exists on
cell surfaces that contains a dramatically altered extracellular domain.
*
This work was supported by National Institutes of
Health Grants PO1-56666, CA23074, CA75152, CA31101, and ES06694.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Arizona
Cancer Center, University of Arizona, 1501 N. Campbell Ave., Tucson, AZ 85724. Tel.: 520-626-7553; Fax: 520-626-4979; E-mail:
cress@azcc.arizona.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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