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PHAGOCYTES
From the Department of Biochemistry, The Holland
Laboratory, American Red Cross, Rockville, MD; and Department of
Biochemistry and Molecular Biology, George Washington University,
Washington, DC.
Expression of tissue transglutaminase (transglutaminase II, tTG)
was shown to increase drastically during monocyte differentiation into
macrophages; however, its role in monocytic cells remains largely
unknown. This study describes a novel function of cell surface tTG as
an adhesion and migration receptor for fibronectin (Fn). Two
structurally related transglutaminases, tTG and the A subunit of factor
XIII (FXIIIA), are expressed on the surface of monocytic cells, whereas
only surface tTG is associated with multiple integrins of the
Monocytic cells are involved in a variety of immune
and inflammatory processes. A number of proinflammatory cytokines can trigger extravasation of monocytes and stimulate their invasion into
inflamed tissues where these cells play a key role in a local immune
response.1-5 Several subsets of adhesion molecules on the
surface of monocytes are involved in different stages of this multistep
process. This involves rolling of monocytic cells along vascular
endothelium, arrest and initial adhesion to endothelium and subsequent
strong adhesion, and spreading and transmigration of monocytes across
the endothelial monolayer as well as invasion into underlying
tissues.6-8 As adhesion receptors, integrins participate
in multiple aspects of monocyte adhesion and transmigration across the
endothelial monolayer. The Tissue transglutaminase (tTG) is a member of transglutaminase family of
enzymes that covalently cross-link proteins in a
Ca++-dependent manner.19 In addition, tTG has
a guanosine triphosphatase (GTPase) activity20 and is
involved in intracellular signaling via agonist-mediated interactions
with tTG accumulates rapidly to very high levels, up to 0.1% to 1% of
total cellular protein, due to a strong increase in its biosynthesis, following induction of monocyte differentiation by adhesion to a
substrate,34 various cytokines, and serum
retinoids35,36 or lipopolysaccharide.34,37
Similarly, an approximate 50-fold up-regulation of tTG was observed in
the human monocytic leukemia cell line THP-1 after stimulation with
12-O-tetradecanoyl-phorbol-13-acetate (TPA).38 The
induction of tTG protein is a specific response of monocytic cells that
strictly correlates with the extent of their morphologic and functional
differentiation.34,38 Transglutaminase activity in
macrophages was suggested to participate in Fc receptor-mediated phagocytosis.39-41 Yet, there is a lack of information
regarding the role of tTG in monocytic cell functions. Another member
of transglutaminase family, the A (catalytic) subunit of coagulation protein factor XIII (FXIIIA) is also expressed by
monocytes42-44; however, its functions in this cell type
remain unknown. Here we demonstrate that monocyte differentiation into
macrophages is accompanied by a sharp increase in the level of
integrin-associated surface tTG. Cell surface tTG is colocalized with
Complementary DNA, antibodies, ECM proteins, and Fn
fragments
Cell isolation, culture, and transfection
Metabolic labeling and cell surface biotinylation Untreated THP-1 cells in suspension and TPA-treated THP-1 cells adherent on Fn were incubated for 12 hours in methionine, cysteine-minus Dulbecco modified Eagle medium (DMEM) with 100 µCi/mL 35S-Translabel (ICN Biologicals, Irvine, CA). The 35S-labeled cells were washed several times with PBS before immunoprecipitation. Untreated or EDTA-detached TPA-treated THP-1 cells were surface biotinylated in suspension by incubating for 15 minutes with 0.2 mg/mL Sulfo-NHS-Biotin (Pierce, Rockford, IL) in PBS. The reaction was stopped by addition of 20 mM TrisCl, pH 7.5, and washing of cells with PBS from excess biotin.Analysis of integrins, tTG, and FXIIIA by immunoprecipitation and immunoblotting Adherent or suspended 35S-labeled or surface-biotinylated THP-1 cells were washed in PBS and lysed in ice-cold RIPA buffer, containing 1% Triton X-100, 0.5% Na-deoxycholate, 0.1% sodium dodecyl sulfate (SDS), 150 mM NaCl, 50 mM TrisCl, pH 7.5, with 0.5 mM phenylmethylsulfonyl fluoride (PMSF), 0.5 mM benzamidine, 10 µg/mL leupeptin, and 10 µg/mL aprotinin. Cell lysates were precleared by centrifugation (14 000 rpm for 30 minutes at 4°C). Then 3 × 108 cpm of protein-incorporated radioactivity (for 35S-labeled cells) or 1 mg total cell protein (for surface-biotinylated cells) was taken for each immunoprecipitation sample with antibodies (4-8 µg/sample) against integrins, tTG, or FXIIIA, followed by protein G-Sepharose.To visualize 35S-labeled proteins, SDS-polyacrylamide gel electrophoresis (SDS-PAGE) in 10% acrylamide/0.25% bis-acrylamide gels was followed by treatment of gels with Autofluor (Amersham Pharmacia) and fluorography. To detect biotinylated proteins, proteins separated by SDS-PAGE were transferred to polyvinylidene difluoride (PVDF) membrane. After blocking the membrane with 5% BSA in TBS/0.05%Tween-20, it was developed with avidin-peroxidase (Pierce). To prove the identity of tTG and FXIIIA in the samples, the same blots were probed with mAb TG100 against tTG or polyclonal antibody to the FXIIIA, respectively. To determine the amounts of tTG and integrin-tTG complexes in
THP-vector and THP-antisense cell populations, Quantitation of the number of tTG molecules on the surface of monocytes and THP-1 cells To determine the number of tTG molecules on the cell surface, THP-1 cells were kept in suspension without any treatment or treated with 150 ng/mL TPA and plated for indicated periods on Fn-coated dishes. Human monocytes were used as untreated cells or cells treated with 5 ng/mL macrophage colony-stimulating factor (M-CSF) and plated on Fn-coated dishes for indicated periods. Adherent cells were detached with EDTA and washed in DMEM/2% BSA before incubation with the label. Then 2 × 105 cells were incubated in suspension for 45 minutes at 4°C with 10 µg/mL 125I-labeled mAb 4G3 against tTG (specific activity 3 × 106 cpm/µg) in DMEM containing 2% BSA. To separate from unbound label, cells were centrifuged (10 000 rpm, 5 minutes, 4°C) through 400 µL 20% sucrose in DMEM. Cell-bound radioactivity was counted in a gamma counter. Incubation with 10-fold excess unlabeled mAb 4G3 was used to determine and subtract nonspecific binding. Three independent experiments were performed with duplicate samples. The number of surface tTG molecules was determined based on 1:1 stoichiometry for mAb 4G3 binding to tTG in the presence of excess 125I-labeled mAb 4G3.Flow cytometry For flow cytometry, live nonpermeabilized untreated or TPA-stimulated THP-1 cells plated on Fn for indicated periods and detached by EDTA were incubated for 1 hour at 4°C with 10 µg/mL polyclonal anti-tTG antibody, polyclonal anti-FXIIIA antibody, or mAbs against human 1-, 2-, or
3-integrins. After washing with PBS, cells were fixed
with 3% paraformaldehyde in PBS, washed, and then incubated with
secondary fluorescein-labeled IgG. The cells were analyzed in FACScan
flow cytometer (Becton Dickinson, Franklin Lakes, NJ). Similarly, untreated and TPA-treated THP-vector and THP-antisense cell
populations plated on Fn for 72 hours were analyzed for surface tTG
expression by incubation for 1 hour at 4°C with 10 µg/mL polyclonal anti-tTG antibody, followed by fluorescein-labeled IgG. Three independent determinations were performed for each cell surface protein, cell type, and treatment.
Immunofluorescence To induce differentiation, THP-1 cells were treated with 150 ng/mL TPA and plated in RPMI containing 10% FBS on Fn-coated glass coverslips for 72 hours. Live nonpermeabilzed cells were double-stained with 10 µg/mL polyclonal anti-tTG antibody and 10 µg/mL mouse mAb JB1A against human1-integrin, mAb B3A to human
3-integrin, or mAb 10.1 against Fc RI receptor.
Following incubation with primary antibodies, cells were fixed with 3%
paraformaldehyde in PBS. After several washes with PBS, cells were
stained with a combination of fluorescein-labeled goat anti-rabbit IgG
and rhodamine-conjugated goat anti-mouse IgG (Chemicon). To
simultaneously visualize cell surface tTG and cytoskeletal proteins
localized at podosomes, live nonpermeabilized cells were stained with
10 µg/mL polyclonal anti-tTG antibody and fluorescein-labeled goat anti-rabbit IgG. Then cells were washed, fixed with paraformaldehyde, permeabilized with 0.1% Triton X-100 in PBS, and costained with rhodamine-phalloidin or antivinculin mAb 7F9 followed by
rhodamine-labeled goat anti-mouse IgG. Stained cells were analyzed and
photographed using Eclipse E800 epifluorescence microscope (Nikon,
Tokyo, Japan) and Spot RT digital camera (Diagnostic Instruments,
Sterling Heights, MI).
Cell adhesion and spreading assays The 24-well tissue culture plates (Costar, Cambridge, MA) were coated with 10 µg/mL laminin, collagen, BSA, Fn, and Fn fragments and then blocked with 0.5% BSA. For adhesion studies, 35S-labeled THP-1 cells or human peripheral blood monocytes in serum-free AIM-V medium (Gibco BRL) containing 0.5% BSA were used. Cells were used either without stimulation or were pretreated for 1 hour with 150 ng/mL TPA (THP-1 cells) or for 4 hours with 5 ng/mL M-CSF (human monocytes). Some cell samples were preincubated for 1 hour at 4°C with 20 µg/mL blocking polyclonal anti-tTG antibody, mAbs 4G3 or CUB7402 against tTG, polyclonal antibody to FXIIIA, function-blocking mAbs against1-, 2-,
and 3-integrins or control nonimmune mouse IgG (all
antibodies were purified IgG). Then 2 × 104 cells were
plated on protein-coated wells for 1 hour at 37°C in serum-free
AIM-V/0.5% BSA supplemented with either 150 ng/mL TPA (THP-1 cells) or
5 ng/mL M-CSF (monocytes) and respective antibodies. Adherent cells
were washed 3 times with PBS and lysed in 100 µL hot 1% SDS. Bound
radioactivity was counted in a scintillation counter and converted into
cell numbers by referring to the levels of
35S-radioactivity incorporated per 103 cells.
Three independent experiments with duplicate determinations were
performed for each cell type and treatment.
For analysis of cell spreading, unlabeled THP-1 cells were treated as indicated above and following plating in serum-free AIM-V/0.5% BSA on protein-coated wells were allowed to spread for 12 hours at 37°C. Cells were washed 3 times with PBS, fixed with 3% paraformaldehyde in PBS, and then stained with Coomassie brilliant blue, destained, and photographed. Migration assays Directional migration of 35S-labeled cells (5 × 104 cells/insert) in Transwells (Costar) with 5-µm pores and the membrane undersurface coated with collagen I, laminin, Fn, the 42-kd and 110-kd Fn fragments, and BSA (10 µg/mL each) was analyzed under serum-free conditions using AIM-V medium with 0.5% BSA. To stimulate chemotactic migration of cells, 125 ng/mL monocyte chemoattractant protein-1 (MCP-1) was added to lower chambers of the Transwells. THP-1 cells were used either without stimulation or were treated with 150 ng/mL TPA immediately before the assay. Human monocytes were treated with 5 ng/mL M-CSF 4 hours before the assay. Some cell samples were preincubated for 1 hour at 4°C with 20 µg/mL blocking polyclonal anti-tTG antibody, mAbs 4G3 or CUB7402 against tTG, polyclonal antibody to FXIIIA, function-blocking mAbs against1-, 2-, and 3-integrins or
control nonimmune mouse IgG. All antibodies were used as purified IgG.
Differentiation agents (TPA or M-CSF) and the respective antibodies
were kept in the medium during the assay. Following incubation for 4 hours at 37°C, cells transmigrated from the upper chambers to the
membrane undersurface. To remove cells from the upper chambers, they
were washed twice with 0.25% trypsin. Transmigrated cells were
harvested from the undersurface of the inserts, the medium, and the
bottom surface of the wells. The number of transmigrated cells in each
sample was determined by cell lysis in 100 µL hot 1% SDS and
counting 35S-radioactivity in a scintillation counter. The
35S-radioactivity was converted into the number of cells by
referring to the levels of 35S-radioactivity incorporated
per 103 cells. Three independent experiments with
duplicated measurements were performed for each cell type, protein
substrate, and treatment.
Monocyte differentiation is accompanied by up-regulation of integrin-associated cell surface tTG Earlier work demonstrated a drastic increase in tTG content and transglutaminase activity concomitant with monocyte conversion into macrophages.34,37-39,49 We recently showed that tTG can serve as an integrin-binding adhesion coreceptor for Fn on fibroblastic cells.33 Thus, using metabolic labeling and immunoprecipitation, we analyzed biosynthesis of tTG and association of tTG with integrins in untreated THP-1 cells in suspension and TPA-treated THP-1 cells plated on Fn for 3 days (Figure 1A). Biosynthesis of tTG strongly increased, whereas the amounts of synthesized FXIIIA diminished following differentiation of THP-1 cells. We also detected an enhancement in biosynthesis of1-, 2-,
and 3-integrins in differentiated THP-1 macrophages.
Notably, the amounts of tTG associated with 1- and
3-integrins were significantly elevated in TPA-treated adherent THP-1 cells (Figure 1A, arrow). In agreement with our previous
data, we were unable to detect complexes of 2-integrins with tTG.33 These results were corroborated using
biotinylation of cell surface proteins and immunoprecipitation of
integrins, tTG, and FXIIIA from untreated and TPA-treated THP-1 cells
(Figure 1B). Differentiation of THP-1 cells raised the expression
levels of cell surface tTG (Figure 1B,C, arrows). In parallel, the
amounts of cell surface tTG complexed with 1- and
3-integrins increased markedly in adherent TPA-treated
THP-1 macrophages (Figure 1B,C, arrow). In contrast, a lack of
association of FXIIIA with integrins and down-regulation of surface
expression of FXIIIA were detected during differentiation of THP-1
cells (Figure 1B,D, arrowhead). Flow cytometry analysis of
1-, 2-, and 3-integrins,
tTG, and FXIIIA on undifferentiated and TPA-differentiated THP-1 cells confirmed a strong approximate 8- to 10-fold increase in the amounts of
surface tTG and down-regulation of surface FXIIIA (Table
1).
Next, using binding of 125I-labeled anti-tTG mAb 4G3
to cells in suspension, we determined a time course of tTG cell surface expression in THP-1 cells during differentiation (Figure
2A). The number of tTG molecules on the
surface of THP-1 cells progressively increased from
6.7 ± 1.3 × 104 for unstimulated cells to
61.1 ± 12 × 104 for TPA-stimulated cells adherent to
Fn. We also observed a biphasic effect of TPA on the expression of
surface tTG. A first rapid phase resulted in an approximate 6-fold
increase in surface tTG within 2 hours after stimulation (Figure 2A)
and was not inhibited by treatment of cells with cycloheximide (data
not shown). In contrast, a second phase of the increase of surface tTG
entirely depended on de novo protein synthesis, started about 12 hours after cell stimulation with TPA and reached a plateau on day 3 of
differentiation. We also determined the number of tTG molecules on the
surface of human monocytes that were induced to differentiate with
M-CSF (Figure 2B). Similarly, the number of surface tTG molecules on
monocytes increased about 2-fold after 2 hours and about 5-fold after
72 hours of M-CSF treatment. Together, our data indicate that monocytic
cells sharply up-regulate the amounts of integrin-associated cell
surface tTG during differentiation.
tTG is codistributed with 1- or
3-integrins revealed their precise and extensive
colocalization at podosomes. These specialized adhesive structures of
macrophages are involved in adhesion, migration, and
diapedesis.50-52 This localization was specific for cell
surface adhesion receptors, because FcRI receptor was not
accumulated at macrophage podosomes (Figure 3C). Several cytoskeletal
proteins such as actin and vinculin, which are concentrated at the
cytoplasmic face of macrophage podosomes,50 also appeared
codistributed with surface tTG in differentiated THP-1 cells, though to
a somewhat lesser extent than integrins (Figure 3D,E, arrows,
arrowheads). The mAb 4G3 also detected tTG in podosomes (Figure 3F),
whereas no staining of these structures could be seen without primary antibody (Figure 3G). Thus, cell surface tTG is localized at podosomes, which serve as specialized cell-ECM adhesive contacts of
macrophages.
Expression of antisense tTG construct in THP-1 cells reduces the level of cell surface tTG Following transfection of antisense tTG construct into THP-1 cells and selection of stable transfectants, we analyzed the expression levels of tTG and the amounts of tTG associated with integrins in the transfectants by immunoprecipitation and immunoblotting (Figure 4A). We observed a strong decrease in the total tTG content in THP-1 antisense transfectants differentiated for 72 hours in the presence of TPA, compared with vector-transfected THP-1 cells. This corresponded to significantly reduced amounts of tTG complexed with1- and 3-integrins in the
THP-antisense transfectants (Figure 4A, arrow). Analysis of surface tTG
by immunostaining with polyclonal anti-tTG antibody and flow cytometry
with live transfectants demonstrated an approximate 2- to 2.5-fold
decrease on unstimulated and 4-fold decrease on TPA-induced
THP-antisense transfectants compared with vector-transfected
counterparts (Figure 4B). Thus, we generated THP-1 transfectants that
express significantly reduced levels of surface tTG.
Down-regulation or inhibition of cell surface tTG specifically decreases adhesion of monocytic cells on Fn and its 42-kd gelatin-binding fragment To define the role of surface tTG in adhesion of THP-1 monocytic cells, we performed quantitative adhesion assays with TPA- induced cells and several ECM proteins and Fn fragments (Figure 5, A,B).
Preincubation with function-blocking antibody against tTG did not
change adhesion of THP-vector cells on collagen type I, laminin, and
the 110-kd cell-binding fragment of Fn (Figure 5A). In contrast,
adhesion of THP-vector cells on Fn and, in particular on the 42-kd
gelatin-binding fragment of Fn,29,33 was significantly reduced by blocking anti-tTG antibody. In agreement, adhesion on
collagen I, laminin, and the 110-kd Fn fragment was not altered by
expression of antisense tTG construct. However, adhesion on Fn and even
more so, on the 42-kd fragment of Fn, was reduced for THP-antisense
transfectants compared to THP-vector control cells. Adhesion of both
THP-1 vector and THP-antisense cells to Fn was induced about 6- to
7-fold by treatment with TPA, whereas it was twice lower for the
antisense transfectants (Figure 5B). Treatment of uninduced THP-1 cells
with antibodies against integrins or tTG had little effect on adhesion
to Fn (data not shown). Function-blocking mAbs against
Then, we examined the role of
Antisense inhibition or blocking cell surface tTG selectively reduces migration of monocytic cells on Fn and the 42-kd fragment of Fn To analyze the potential involvement of surface tTG in migration of TPA-stimulated THP-1 monocytic cells, we used transmigration assays with Transwells (Costar) where the undersurface was coated with ECM proteins and Fn fragments. To ensure an efficient directional migration, MCP-1 was added to lower chambers. Only very few THP-1 cells transmigrated onto protein-coated membranes in the absence of TPA stimulation (data not shown). Treatment with blocking antibody against tTG did not change migration of TPA-induced THP-vector cells on collagen type I, laminin, and the 110-kd cell-binding fragment of Fn (Figure 7). On the contrary, blocking anti-tTG antibody significantly reduced migration of THP-vector cells on Fn and its 42-kd fragment. Likewise, migration on collagen I, laminin, and the 110-kd Fn fragment was not altered by expression of THP-antisense construct, whereas migration on Fn and the 42-kd fragment of Fn was decreased for TPA-induced THP-antisense transfectants compared to their THP-vector counterparts.
Further, we tested several antibodies against tTG, integrins, and
FXIIIA in migration assays with TPA-stimulated THP-1 cells and
membranes precoated with Fn and the 110-kd and 42-kd Fn fragments (Figure 8). Polyclonal antibody and mAb
4G3 against the NH2-terminal Fn-binding domain of tTG had
the most striking inhibitory effects on migration of THP-1 cell on Fn.
Another mAb CUB7402 against the tTG fragment
(331-478), which also interferes with the interaction of
surface tTG with Fn,33 decreased the migration of THP-1
cells on Fn to a lesser extent. Because the monovalent Fab fragment of
anti-tTG mAb 4G3 also inhibited THP-1 cell migration on Fn (data not
shown), interfering with tTG-Fn interaction rather than mere clustering
of tTG on the cell surface reduced monocyte migration. Function-blocking antibodies to either
Similarly, analysis of M-CSF-treated human monocytes revealed a key
role of surface tTG in MCP-1-induced transmigration on Fn and its
42-kd fragment (Figure 9). Again, a
pretreatment with anti-tTG antibodies caused a strong inhibitory effect
on cell migration on Fn and, even more so, on the 42-kd fragment,
whereas antibodies against
Previous work showed that tTG content is drastically increased in
monocytic cells undergoing differentiation34,37-39,49; however, the functional significance of this up-regulation of tTG
remained unknown. Here we show that monocyte maturation into macrophages is accompanied by a sharp elevation of cell surface tTG.
This occurs in response to inducers of monocyte differentiation (adhesion to Fn, treatment with M-CSF or other cytokines that promote
macrophage phenotype) or as a result of treatment of THP-1 monocytic
leukemia cells with nonspecific activators of protein kinase C (TPA).
Importantly, we found that the first phase of up-regulation of surface
tTG occurs rapidly within 2 hours after stimulation and does not
require protein synthesis. This suggests that monocytes can elevate
promptly the amounts of surface tTG in response to various activation
stimuli. Mechanisms underlying this rapid up-regulation of surface tTG
remain unknown. Yet, recently we reported that complexes of tTG with
We recently reported colocalization of surface tTG with
The results presented in this work highlight a novel function of
cell surface tTG as an adhesion and migration receptor on macrophages.
We observed a significant decrease in adhesion and migration of
monocytic cells on Fn due to down-regulation of cell surface tTG by
expression of antisense construct or inhibition of tTG-Fn interaction
with blocking antibodies. Notably, the magnitude of these effects
exceeded those of blocking antibodies against either Our data also point to dissimilar roles of 2 structurally related
transglutaminases, tTG and FXIIIA, in monocytic cell functions. In
contrast to a sharp increase in the tTG biosynthesis and content, we
found a down-regulation of FXIIIA expression during monocyte differentiation. Then, as in the case of its exogenous expression in
fibroblasts,33 FXIIIA failed to interact with
Where may the interaction of cell surface tTG on monocytic cells with the surrounding Fn-containing matrices occur in vivo? This can take place during migration of monocytic cells beneath the endothelial monolayer into underlying tissues that contain large amounts of Fn in the ECM. Yet, a rapid up-regulation of cell surface tTG on monocytic cells in response to activation stimuli suggests that tTG interaction with Fn and, possibly other tTG-binding ECM proteins or endothelial receptors, may also occur during earlier stages of monocyte extravasation. Further work is required to address a potential role of integrin-associated cell surface tTG in monocyte-endothelial interactions. Notably, certain types of acute monocytic leukemia are characterized by 2 subpopulations of monocytes.53,54 One of these displays an increased extravasation and accumulation in various tissues due to elevated adhesive and migratory capacity. In future work it will be important to determine whether the abnormal adhesive and migratory properties of monocytic leukemia cells involve a deranged expression of cell surface tTG.
The authors thank Dr Peter Davies (University of Texas, Houston, TX) for providing tTG cDNA. We wish to thank Dr Kenneth Ingham (Department of Biochemistry, American Red Cross) for providing purified Fn fragments used in this study. We are grateful to Liubov Zaritskaya (Department of Immunology, American Red Cross) for expert technical assistance with monocyte isolation and flow cytometry analysis.
Submitted February 22, 2001; accepted May 9, 2001.
Supported by grant CA77697 from the National Institutes of Health.
The publication costs of this article were defrayed in part by page charge payment. Therefore, and solely to indicate this fact, this article is hereby marked "advertisement" in accordance with 18 U.S.C. section 1734.
Reprints: Alexey M. Belkin, Department of Biochemistry, The Holland Laboratory, American Red Cross, 15601 Crabbs Branch Way, Rockville, MD 20855; e-mail: belkina{at}usa.redcross.org.
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S. G. Priglinger, C. S. Alge, T. C. Kreutzer, A. S. Neubauer, C. Haritoglou, A. Kampik, and U. Welge-Luessen Keratinocyte Transglutaminase in Proliferative Vitreoretinopathy Invest. Ophthalmol. Vis. Sci., November 1, 2006; 47(11): 4990 - 4997. [Abstract] [Full Text] [PDF]
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S. G. Priglinger, C. S. Alge, A. S. Neubauer, N. Kristin, C. Hirneiss, K. Eibl, A. Kampik, and U. Welge-Lussen TGF-{beta}2-Induced Cell Surface Tissue Transglutaminase Increases Adhesion and Migration of RPE Cells on Fibronectin through the Gelatin-Binding Domain Invest. Ophthalmol. Vis. Sci., March 1, 2004; 45(3): 955 - 963. [Abstract] [Full Text] [PDF]
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S. Orru, I. Caputo, A. D'Amato, M. Ruoppolo, and C. Esposito Proteomics Identification of Acyl-acceptor and Acyl-donor Substrates for Transglutaminase in a Human Intestinal Epithelial Cell Line: IMPLICATIONS FOR CELIAC DISEASE J. Biol. Chem., August 22, 2003; 278(34): 31766 - 31773. [Abstract] [Full Text] [PDF]
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E. S. Roberts, M. A. Zandonatti, D. D. Watry, L. J. Madden, S. J. Henriksen, M. A. Taffe, and H. S. Fox Induction of Pathogenic Sets of Genes in Macrophages and Neurons in NeuroAIDS Am. J. Pathol., June 1, 2003; 162(6): 2041 - 2057. [Abstract] [Full Text] [PDF]
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S. N. P. Murthy, S. Iismaa, G. Begg, D. M. Freymann, R. M. Graham, and L. Lorand Conserved tryptophan in the core domain of transglutaminase is essential for catalytic activity PNAS, March 5, 2002; 99(5): 2738 - 2742. [Abstract] [Full Text] [PDF]
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Top
Abstract
Introduction
4
1.
TPA) and THP-1 cells induced to differentiate
by plating on Fn for 72 hours in the presence of 150 ng/mL TPA (+TPA)
were analyzed. The 
, THP-vector; 
, THP-antisense.
Shown are the means of triplicate determinations.
) cells were
stimulated for 1 hour with 150 ng/mL TPA and then allowed to adhere to
wells coated with collagen type I (Col I), laminin (Ln), Fn, 110-kd or
42-kd Fn fragments, or BSA. Some samples of THP-vector cells were
pretreated for 1 hour with function-blocking polyclonal anti-tTG
antibody (
), either untreated or pretreated for 1 hour with 150 ng/mL
TPA (
). Monocyte samples were preincubated
for 1 hour with control nonimmune IgG, function-blocking polyclonal
anti-tTG antibody, mAb 4G3 against tTG, or blocking mAbs against
