[CANCER
RESEARCH
45, 5643-5647,
November 1985]
Abundant Synthesis of the Transformation-induced Protein of Neoplastia
Human Fibroblasts, Plastin, in Normal Lymphocytes1
David Goldstein,2 Julie Djeu, Gerald Latter, Stephen Burbeck, and John Leavitt
Armand Hammer Cancer Research Center, Linus Pauling Institute of Science and Medicine, Palo Alto, California 94306 [D. G., G. L, S. B., J. L], and Department of
Medical Microbiology, University of South Florida School of Medicine, Tampa, Florida 33612 [J. D.]
ABSTRACT
The transformation-induced protein plastin (p219; M, 68,000,
pi 5.3) is a reliable cytosolic marker for neoplastia human fibroblasts. Fibroblasts transformed in vitro by chemical carcinogens
or SV40 virus and tumor-derived cancer cells of fibroblastoid or
epithelioid origin usually express plastin and p220, a minor
phosphorylated form of plastin. We report here that plastin is
expressed as one of the most abundant proteins of normal,
untransformed lymphocytes. The phosphorylated form of plastin
was detectable in adherent mpnocytes but not in purified T- or
sized in purified subpopulations of normal human lymphocytes,
we observed that plastin is one of the most abundant proteins
of all lymphocyte subpopulations. Furthermore we have discov
ered that a probable allelic variant of plastin exists in a human
subpopulation. The natural presence of plastin in normal lympho
cytes suggests an approach to studying the mechanism of
activation of this gene as well as a possible clue as to its function
in transformed human fibroblasts.
NK lymphocytes. We also demonstrate that an allelic variant or
mutated form of plastin exhibiting altered charge is found at a
reduced frequency in the human population. We discuss the
possible significance of these observations in terms of evaluating
the role of plastin induction in expression of the cancerous
phenotype of fibroblasts.
INTRODUCTION
Human cells neoplastically transformed by treatment with
chemical carcinogens provide a valuable model system for study
ing the macromolecular changes which lead to the development
of human cell tumorigenicity. Two sets of abundant cytoplasmic
transformation specific polypeptides, p788/p7893 and p219/
p220 (plastin), have been identified by comparison of two-dimen
sional protein profiles of in vitro transformed human fibroblasts
with the parental diploid fibroblast strains (1-4). One or both of
these transformation markers is usually expressed in human
tumor-derived cells of fibroblastoid or epithelioid origin, but these
markers are not expressed appreciably in normal fibroblasts (3,
4). The lower-molecular weight markers p788/p789 (pi 5.3-5.2;
M, 26,000-27,000) may be derived from an epidermal growth
factor or transforming growth factor precursor protein, since
these polypeptides exhibit similar amino acid composition (2).
The other polypeptide marker, plastin (p219/p220; pi 5.3, M,
68,000), is more enigmatic in that it exhibits no unusual proper
ties that would aid in the identification of its function. However,
it is known that plastin is phosphorylated (p220) and that it
exhibits partial lability in transformed human fibroblasts (5). The
induction of plastin synthesis upon neoplastic transformation is
independent of the type of activated oncogene and more fre
quently correlated with transformation than oncogene activation
(4)During our examination of the spectrum of proteins synthe1This work was supported in part by a grant from the National Cancer Institute
(Grant CA-34763) and funding from the Japan Shipbuilding Foundation to J. L.
2 To whom requests for reprints should be addressed. Supported by funds
MATERIALS AND METHODS
Cell Cultures. The KD strain of diploid human fibroblasts and the HuT12 cell line have been described previously (1, 4). The HT-1080 cell line
was purchased from the American Type Culture Collection (Rockville,
MD). The fibroblast cells were cultured in Dulbecco's modified Eagle's
medium, supplemented with 10% fetal calf serum (1).
Purification of Peripheral Blood Lymphocytes, T-Cells, and NK
Cells. Lymphocytes were obtained from three sources, all located at the
National Institutes of Health, Bethesda, MD. The lymphocyte concen
trates from the Platelet-Pheresis Center were diluted 1:5 in RPMI 1640
medium containing 10% fetal bovine serum, 100 ß<j/m\each of penicillin
and streptomycin, 2 HIM glutamine, 5 mw 4-{2-hydroxyethyl)-1-piperazineethanesulfonic acid, and 2 units/ml of preservative-free heparin. The
buffy coats from the blood bank and the leukopacks from the leukopheresis center were diluted 1:2 in phosphate-buffered
saline. PBL
mononuclear cells were obtained by Ficoll-Hypaque density gradient
centrifugation of the buffy coats obtained from the blood bank at the
National Institute of Health. For further purification of lymphocyte sub
sets, adherent cells were first removed by incubation on plastic tissue
culture dishes and subsequent incubation on nylon wool columns (6).
From the remaining non-adherent cells, NK and T-cells were purified
through a discontinuous Percoli density gradient centrifugation step
following the method of Djeu ef a/. (6). The adherent cells were rinsed
free of non-adherent cells by washing repeatedly with phosphate-buff
ered saline to obtain the mononuclear cell preparation.
Labeling of Cellular Proteins, Two-dimensional Polyacry lamide Gel
Electrophoresis, and Analysis by Computerized Microdensitometry.
All cell types in suspension cultures or in high-density subconfluent
monolayers were labeled for 4 h with [^SJmethionine (New England
Nuclear) exactly as described previously (1, 3). Radiolabeled cells in
monolayers or in suspension were washed three times with cold phos
phate-buffered saline, drained, and then lysed directly in O'Farrell's "lysis
buffer A" (1). Protein samples were stored at -76°C prior to electrophoresis. Replicate two-dimensional polyacrylamide electrophoresis gels
were made from each protein sample with the Iso-Dalt system from
Electro-Nucleonics (Oak Ridge, TN). However, the second-dimension
gels were thinner (1 mm as opposed to 1.5 mm). Kodak XAR-2 film was
donated to the Linus Pauling Institute by Robert Sabin.
'The abbreviations used are: p, polypeptide; PBL, peripheral blood lymphocyte;
used for autoradiography. Exposure time was 2 h for measurement of
actin synthesis and 2 to 4 days for measurement of total protein
synthesis. The film was developed in a Kodak X-Omat model 5 processor
and digitized on an Optronics P-1000 film scanner at a pixel size of 100
NK cell, natural killer cell.
Received 5/22/85; revised 8/1/85; accepted 8/6/85.
tim. We have described this method of computerized
previously (2-5,10) in greater detail.
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1985
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PLASTIN AS A MARKER
FOR NEOPLASTIC
RESULTS
Fibroblast Transformation-specific Plastin in Normal Lym
phocytes. Fig. 1 presents autoradiographs of the [35S]methionine-labeled total polypeptides of normal KD fibroblasts, in vitro
transformed HuT-12 fibroblasts, and normal monocytes. The
transformation-induced
plastin polypeptides (p219/p220) ex
pressed by neoplastic human fibroblasts (3, 4) are indicated in
the HuT-12 polypeptide pattern (Fig. 10). The total (unfractionated) polypeptide separation patterns for KD and HuT-12 fibro
blasts have been shown previously to be virtually the same both
qualitatively and quantitatively, with the exception of transfor
mation-induced plastin polypeptides (p219/p220) and one addi
tional set of neoplasia-specific epidermal growth factor-related
polypeptides, p788/p789 (1, 3, 4). Fig. 1C shows the most
abundant acidic polypeptides of normal monocytes derived from
human PBL by selection of cells in the PBL preparation that
adhere to a plastic substratum (6). Two abundant polypeptides
that are electrophoretically identical to the plastin polypeptides
in HuT-12 fibroblasts are found in monocytes (Fig. 1C) as well
as in total peripheral blood lymphocytes, purified T-lymphocytes,
and NK lymphocytes (Fig. 2, Table 1). The relative rates of
expression of plastin in monocytes, T-cells, NK cells, and unfractionated PBLs did not vary greatly (Table 1), which suggests that
plastin is constitutively expressed at high levels in all major
subpopulations of lymphocytes. Furthermore, plastin appears to
be more abundant in monocytes and NK lymphocytes than in
transformed or human tumor-derived fibroblasts (Table 1). Microdensitometry analysis performed on two-dimensional total acidic
protein patterns of monocytes and T-cells indicates that plastin
2).
We established that the plastin-like polypeptides of monocytes
fibroblasts co-migrated with the labeled plastin-like polypeptides
from monocytes or PBLs so that they each resolved as one
electrophoretic "spot" in two-dimensional gel autoradiographs
when total proteins from the two cell types were mixed together
prior to electrophoresis (not shown). Their co-migration was also
established by mixing excess unlabeled monocyte proteins with
radioactive neoplastic fibroblast proteins, followed by observa
tion that radioactively labeled plastin in the autoradiogram was
superimposed upon silver-stained plastin-like polypeptides,
which for the most part were monocyte derived (not shown).
These results indicate that these electrophoretically identical
proteins of transformed fibroblasts and lymphocytes are the
same proteins.
To determine if plastin expression is modulated in leukemogenesis as it is accompanying fibroblast transformation, we
compared the rates of plastin synthesis in freshly isolated normal
NK cells and in the Molt-4 (8) and CCRF-CEM (ATCC-CCL-119)
cell lines, each derived from a T-cell leukemia. Fig. 3 compares
the patterns of [35S]methionine-labeled protein synthesis be
lymphocytes exhibited two distinct electrophoretic isoforms of
plastin (Fig. 4). In this individual's monocytes the rate of synthesis
identical to plastin in trans
210
formed fibroblasts first by overlapping autoradiographs of the
respective protein patterns. As expected, we found that many
of the surrounding abundant polypeptides in the patterns such
as fi-, 7-actin, intermediate filament protein, p222, and p210
were also in superimposable positions (Figs. 1 and 2). These
other major proteins were found to be common among all
lymphocytes, normal and transformed fibroblasts, and tumorderived cells of fibroblastoid, epithelioid, and lymphoid origin.
Also, [35S]methionine-labeled plastin from transformed human
tween NK cells and Molt-4 cells. Microdensitometry measure
ments of the rates of plastin synthesis in both of these two cell
types revealed no significant difference (Table 1). The rate of
synthesis of plastin in the other leukemic T-cell line, CCRF-CEM,
also appeared unaffected (not shown).
Expression of a Variant Isoform of Plastin in Lymphocytes
of One Individual. We have examined protein synthesis in
lymphocyte preparations from nine different donors. One donor's
is one of the 15 most abundant proteins of these cell types. In
in vitro transformed human fibroblasts, plastin is among the 50
to 100 most abundant proteins (3, 4). The minor phosphorylated
form of plastin, p220 (5), was found in monocytes (Fig. 1) but
not in any of the non-adherent lymphocyte cell populations (Fig.
and PBLs are electrophoretically
FIBROBLASTS
• 220/T
*
222
•
210
220
219
\
ß
**•
Fig. 1. Comparison of the two-dimensional polypeptide patterns between normal and transformed [^Slmethionine-labeled human fibroblasts and [^Slmethioninelabeled human monocytes in the electrophoretic regions of plastin (p219/220) and ¡i-and vactin. The positions of the fibroblast neoplasia-specificplastin polypeptides
(p219/p220) are identified in the gels representing transformed fibroblasts and normal monocytes. Polypeptides common to normal fibroblasts, transformed fibroblasts,
and monocytes are p222, p210, ,i-actin (¿),vactin (•>),
and vimentin (v: see Refs. 1, 3. and 8). A, KD, normal human fibroblasts, 106dpm in protein per gel; B, HuT-12,
transformed human fibroblasts. 10" dpm in protein per gel; C. normal human monocytes. 2 x 105dpm in protein per gel.
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PLASTIN
AS A MARKER
FOR
NEOPLASTIC
FIBROBLASTS
Fig. 2. Computerized images from autoradiographs of twodimensional polypeptide patterns of "non-adherent" lympho
cytes (6), in the electrophoretic regions of plastin (p219), p222,
and ii- and 7-actin. A, NK cells (6); B. PBL (6); C, T-cells (6).
\ 'I-
ßs
between p219 and p219x is the same as the shift in /S-actin
Table 1
Relative amount of [xS]methionine-labeled
plastin (p219/p220) compared
to total [xS]methionine-labeled
/J- and t-actin
resulting from one charge altering mutation (1,9).
As a further test of the relatedness of these plastin variants
and
(p219/p220 and p219x/p220x), we labeled these proteins with
7-actin0.030.100.040.130.070.030.020.040.003Not
originNormal
typePBLNKT-cellMonocyteMolt-4Sarcoma-2HuT-12HuT-14HT1080Diploid
Cell
ten different 14C-amino acids and examined the distribution of
lymphocyteNormal
lymphocyteNormal
lymphocyteNormal
lymphocyteT-cell
leukemiaLeiomyosarcomaIn
each amino acid between the two isoforms. The ratio of p219/
p220 to p219x/p220x remained virtually constant regardless of
the type of labeled amino acid used (Fig. 4, Table 2), although
the other neighboring but unrelated polypeptides p220 and p210
were at variance in their incorporation of each amino acid label
(Fig. 4). The constancy of the ratio between p219/p220 and
p219x/p220" with ten different amino acid labels suggests that
transformedfibroblastsIn
vitro
transformedfibroblastsFibrosarcomaNormal
vitro
humanfibroblastsCell
diploidPlastin/rf-
the two putative plastin variants are nearly identical in amino
acid composition (7, 10).
Amino Acid Composition Analysis of Plastin. The predicted
amino acid composition for plastin is shown in Table 3. Monocytes were labeled individually with 20 radioactive amino acids
(all 14Cexcept for methionine, which was labeled with 35S),and
detectable
N K Cells
Inter
mediate
Filament
Protein
ß-Tubulin'
separate two-dimensional polyacrylamide gels of total proteins
were produced for each independent amino acid label. Autoradiography and microdensitometry were performed to determine
the relative incorporation of each amino acid label into total
plastin polypeptide (p219/p220) and the standard ß-,7-actin for
which the amino acid composition is known (2, 9). For each
amino acid label the relative amount of radioactivity in plastin
was computed using the measured radioactivity simultaneously
incorporated into the reference protein ß-,7-actin. The amino
iOLT-4 Cells
Inter
mediate
Filament
Protein
ß-Tubulin'
o-Tubulin
Fig. 3. Comparison of [Å“S]methionine-labeled
erized images of NK cells and Molt-4 cells.
acid composition of plastin was then predicted according to the
method described previously by Latter ef al. (7,10). Using 68,000
as the molecular weight of plastin, the number of amino acid
residues was estimated to be 460. The calculated compositions
indicate that threonine is the most abundant amino acid (about
57 residues), followed by glutamic acid (about 51 residues).
Histidine appears to be the least abundant (about 3 residues),
followed by tryptophan (about 5 residues).
ß.y-Actin
polypeptide patterns in comput
of the usual electrophoretic form of plastin (p219) is reduced by
about one-half when compared to the rate of synthesis of ß-and
7-actin or p222, and the variant plastin (p219x) is expressed at
nearly the same rate. The similarity in the shape and phenotype
of these two sets of resolved spots indicates that they are highly
related proteins. The variant plastin polypeptides (p219x/p220x)
have shifted in the gel pattern as though they had acquired one
additional positive net charge resulting from an amino acid ex
change. The distance in the equilibrium isoelectric focusing plane
CANCER
RESEARCH
DISCUSSION
Although it is a soluble protein, the high abundance of plastin
in lymphocytes and monocytes strongly suggests that it may
have a structural role in these cell types. For example, plastin is
expressed at the same level of abundance as intermediate
filament protein and appears to be stable (see Figs. 1 and 2). By
contrast, plastin exhibits a biphasic decay kinetics indicative of
the presence of both stable and labile elements in transformed
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PLASTIN AS A MARKER
FOR NEOPLASTIC
219
FIBROBLASTS
219
il
219
Fig. 4. Comparison of '4C-labeledamino acids from human monocytes, showing the electrophoretic position and phenotype of invariant plastin (p219/p220) and the
variant plastin (p219"/p220x)using four different [14C]amino acid labels. The downward arrows indicate the positions of invariant plastin (p219/p220), and the upward
arrows indicate the positions of the variant plastin (p219"/p220x)isoform. The smaller arrows always identify the position of phosphorylated plastin (p220). 14C-Amino
acid labels:A, [14C]arginine;B, [14C]tryptophan;C, [14C]glutamicacid; and D, [14C]isoleucine.
Table 2
Ratio of variant plastin (p219'/p220") to invariant plastin
(p219/220) with different "C-amino acid labels
such as the HuT strains (3-5) and tumor-derived fibroblasts like
the fibrosarcoma-derived cell line HT1080 and leiomyosarcomaderived cell line Sarcoma-2 (4) have more contracted cytoskeletons (5)4 and less anchorage dependence for growth (12)4 like
Mean = 0.77 ±0.1
(SE).14C-Amino
4
acidAlanine
p219"/p220"0.60
monocytes and lymphocytes. Thus a tentative working hypoth
esis is that plastin may either regulate cytoarchitectural rear
Arginine
0.65
rangement or anchorage independence, two general phenotypes
Aspartic acid
0.83
common to both lymphocytes and transformed fibroblasts.
Glutamic acid
0.77
Lack of synthesis of plastin in normal fibroblasts and the high
Glycine
0.74
Isoleucine
0.76
level constitutive expression of plastin in monocytes and lympho
Phenylalanine
1.0
cytes suggest either that the plastin gene in normal fibroblasts
Proline
0.72
Serine
0.82
is under negative regulation or that a positive control mechanism
Tryptophanp219/p220:
0.85
is in effect in monocytes and lymphocytes. Elucidation of the
nature of this regulatory control mechanism could reveal a key
regulatory step in the induction of cancerous fibroblasts, since
Table 3
Predicted amino acid composition for the monocyte plastin polypeptides
plastin is usually induced accompanying fibroblast transforma
tion.
Construction of cell hybrids between normal fibroblasts and
of
no. of
residues3261322336145121330352381317235751742
eachresidue0.060.030.050.070.010.030.110.050.010.070.080.050.020.030.040.050.120.010.040.09Estimated
lymphocytes or monocytes may lead to up- or down-regulation
AlanineArginineAsparagineAspartic
of either the lymphocyte or the fibroblast alÃ-eles,depending on
whether a positive or negative control process governs the
expression of the plastin gene in these two cell types. Fortu
acidCysteineGlutamineGlutamic
nately, charge variants of plastin exist like the variant described
in this study. The existence of such variants should permit
acidGlycineHistidineIsoleucineLeucineLysineMethioninePhenylalanineProlineSerineThreonineTryptophanTyrosineValinePercentage
simultaneous assessment of expression from both allelic genes
donated by the fibroblasts and the lymphocyte within hybrid cell
populations.
The finding that plastin is polymorphic in the human population
raises a number of questions related to the possible participation
of plastin mutations in human health and predisposition to dis
ease that could be addressed through epidemiology. Goldman
and Merril (13) have also reported that the plastin polypeptide is
polymorphic in peripheral blood lymphocytes and have demon
strated that the same polymorphism we describe here is quite
a Total number of residues is 460.
frequently observed. Furthermore, they demonstrate the exist
ence of individuals who exhibit only the variant electrophoretic
isoforms of plastin (p219x/p220x) (13) and thus are homozygous
fibroblasts (5). Vimentin and ß-and 7-actin are the principal
for a germ line-transmitted mutated form of plastin. Two addi
cytoskeletal proteins of lymphocytes, monocytes, and fibroblasts
tional observations suggest that the variant plastin may have
(1, 5, 8, 11), yet lymphocytes and monocytes have relatively
contracted cytoskeletons compared to normal fibroblasts. Trans
4D. Goldstein, J. Djeu, G. Latter, S. Burbeck, and J. Leavitt, unpublished
formed fibroblasts which express abundant amounts of plastin
observations.
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PLASTIN AS A MARKER
FOR NEOPLASTIC
altered properties as a consequence of this mutation. First, the
migration rate of these variant plastin polypeptides in sodium
dodecyl sulfate is slightly increased when compared with invar
iant plastin, which thus suggests that a conformational change
or deletion has occurred in the protein. In this regard single amino
acid exchanges will sometimes alter the migration rate of a
protein in sodium dodecyl sulfate gels (3, 9). Also, the steady
state concentration of variant plastin appears to be slightly higher
than invariant plastin in hétérozygotes,since the mean ratio
between these two isoforms is 0.77 (Table 2) with the less
common plastin variant (p219x/p220x) in excess. Individuals car
rying one or both mutated alÃ-elescould be classified by protein
profiling of their lymphocytes. Then the three groups could be
analyzed for any benefits or risks that might be associated with
this mutation. These studies might be useful for evaluating the
role of mutant plastin genes in either suppression or predisposi
tion of the afflicted subpopulations to the individual forms of
cancer if, as speculated, plastin plays a role in tumorigenesis or
metastasis. Alterations in the normal differentiated functions of
monocytes and lymphocytes might also be explored through
epidemiology.
REFERENCES
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CANCER
RESEARCH
FIBROBLASTS
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Abundant Synthesis of the Transformation-induced Protein of
Neoplastic Human Fibroblasts, Plastin, in Normal Lymphocytes
David Goldstein, Julie Djeu, Gerald Latter, et al.
Cancer Res 1985;45:5643-5647.
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