[CANCER RESEARCH 57. 5505-5508. December 15. 1997]
Mitosin (a New Proliferation Marker) Correlates with Clinical Outcome in
Node-negative Breast Cancer1
Gary M. Clark,2 D. Craig Allred, Susan G. Hilsenbeck, Gary C. Chamness, C. Kent Osborne, Diane Jones, and
Wen-Hwa Lee
Department of Medicine, Division of Medical Oncology [G. M. C.. S. G. H.. G. C. C.. C. K. OJ. Department of Pathology /D. C. A.], and Department of Molecular Medicine,
Institute of Biotechnology ¡D.J., W.-H. L], University of Texas Health Science Center, San Antonio, Texas 78284
ABSTRACT
Tumor proliferation rate is an important prognostic factor in breast
cancer, and S-phase fraction (SPF), as measured by flow cytometry, is the
most clinically validated of several methods for measuring it. However,
flow cytometry is not well suited to evaluating the formalin-fixed, paraf
fin-embedded tumors that are routinely available or to the increasing
number of small breast cancers. These and other limitations have moti
vated research into alternative methods for measuring proliferation, in
cluding immunohistochemistry (IHC) against cell cycle-related antigens,
which are better suited for the evaluation of small archival tissue samples.
Mitosin is a recently described 350 kl) nuclear phosphoprotein that is
expressed in the late G,, S, G2, and M phases of the cell cycle but not in
G0. Using a new monoclonal antibody (14C10), this pilot study evaluated
mitosin expression by IHC in a series of 386 node-negative, formalin-fixed,
archival breast cancers and correlated the results with several prognostic
factors and clinical outcome (median follow-up, 78 months; range 3-214
months). The median and range of mitosin positive cells were 7% and
1-47%, respectively. There was a strong positive correlation between
mitosin and SPF (r = 0.57; /' = 0.0001), and there were significant
negative correlations with estrogen receptor, progesterone receptor, and
patient age. Mitosin was not related to overall survival in this pilot study.
However, in a univariate cutpoint analysis of disease-free survival (DFS),
patients with high levels of mitosin (>')'< positive cells) had significantly
worse DFS than did patients with lower levels (68% versus 84% at 5 years,
respectively). In a multivariate analysis of DFS, large tumor size (>2 cm)
and high mitosin were the only independently significant predictors of
recurrence (relative risks = 2.47 and 1.72, respectively) in a model con
taining the additional factors estrogen receptor, progesterone receptor,
patient age, and SPF. These preliminary results suggest that mitosin as
assessed by IHC may be superior to SPF as a prognostic factor in
node-negative breast cancer, but additional studies are necessary to vali
date these promising findings.
INTRODUCTION
Alterations in the control of cell proliferation are important in the
development and progression of many types of human cancer, and the
overall rate of proliferation is indirectly related to clinical outcome.
There are several techniques for estimating or measuring proliferation,
including light microscopic mitotic index, thymidine labeling index,
bromodeoxyuridine uptake, and DNA flow cytometry. Each of these
methods has strengths and weaknesses, but none are ideal for meas
uring proliferation in formalin-fixed, paraffin-embedded tissue, which
has become the standard method of processing and storing clinical
Received 2/19/97; accepted 10/14/97.
The costs of publication of this article were defrayed in part by the payment of page
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18 U.S.C. Section 1734 solely to indicate this fact.
1This work was supported by NIH Grants POI CA30195. P50 CA58I83. and P30
CA54174.
2 To whom requests for reprints should be addressed, at Department of Medicine.
Division of Medical Oncology. University of Texas Health Science Center. 7703 Floyd
Curl Drive. San Antonio. TX 78284-7884. Phone: (210) 567-4749: Fax: (210) 567-6687:
E-mail: gary@oncology.uthscsa.edu.
samples. IHC3 against cell cycle-related antigens is a more recent
method for measuring proliferation that is better suited for evaluating
routine archival tissue, and antibodies have been developed to a few
antigens, such as KÃOE67, which have been used in preliminary studies
with varying success. The ultimate success of IHC will depend on
how specific the antigens are for dividing cells and how sensitive the
antibodies against them are in archival tissue. So far, none of them is
optimal.
Mitosin is a recently identified 350 kD nuclear phosphoprotein that
is involved in cell division and, therefore, may be a suitable target for
evaluating proliferation by IHC. It was identified through its binding
to purified retinoblastoma protein, and it is expressed in the late G,,
S, G2, and M phases of the cell cycle but is absent in G0 (1). It
associates with the centromere, spindle, and midbody of the mitotic
apparatus during M and completely degrades following cytokinesis
(1). The carboxy terminus of the molecule has been shown to be
essential for the localization of mitosin in the nucleus (2).
We have developed several monoclonal antibodies to mitosin that
are suitable for IHC in archival tissue. This pilot study used one of
these antibodies (14C10) to measure mitosin expression by IHC in
386 archival node-negative human breast cancers. The results were
compared to SPF, as determined by flow cytometry, several other
clinical/pathological features, and patient outcome.
MATERIALS AND METHODS
Antibody Production and Characteristics. Balb/c mice were immunized
with bacterially expressed fusion protein GST lOBgl (containing amino acids
1759-2093 of mitosin). Injections of 100 /*g of protein were given s.c., the
first in Complete Freund's Adjuvant, followed by three boosts in Incomplete
Freund's Adjuvant at 4-6-week intervals. A final boost of GST lOBgl in
sterile PBS was given i.v. 3 days prior to the fusion.
Isolated immune splenocytes were fused with NSI mouse myeloma cells
using 50% polyethyleneglycol essentially as described by Oi and Herzenberg
(3). Successful hybridomas were initially screened by ELISA against GST and
GST lOBgl. Several clones that only reacted to GST lOBgl were expanded,
single-cell cloned, and retested by ELISA to confirm specificity. Five clones
(2G8, 13E7, 14C10, 16G6, and 18E1) with strong GST lOBgl activity were
then injected into the peritoneum of Balb/c mice to form ascites. IgG was
purified from the ascites using protein G Sepharose, dialyzed against PBS. and
stored long-term at -80°C.
In a previous study using normal mouse kidney CV1 cells synchronized by
different drugs to obtain uniform populations at different phases of the cell
cycle, mitosin was shown to be expressed in late G,, S, G2, and M but not in
G0 (1). The specificity of the mitosin antibody used in this study was con
firmed by immunoprecipitation against whole-cell lysates from the normal
human breast epithelial cell line HBL-IOO. To obtain sufficient quantity of
cells expressing mitosin, they were first arrested and synchronized at the G,-S
boundary for 24 h with hydroxyurea and released for 4 h prior to harvesting.
The lysates were precipitated with each of the five purified antibodies de
scribed above, the products were separated on a polyacrylamide gel. Western
blotted, and probed with antibody 14C10. Each antibody showed single-band
1The abbreviations used are: IHC, immunohistochemistry: SPF. S-phase fraction:
GST. glutathione 5-transferase; ER. estrogen receptor; PgR. progesterone receptor; DFS.
disease-free survival; OS. overall survival.
5505
Research.
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