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, Granulocyte-Macrophage CSF, and IL-1ß Through Prostaglandin-Dependent and -Independent Mechanisms
Immunopathology Section, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892
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Abstract |
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 Top Abstract IntroductionMaterials and MethodsResultsDiscussionReferences |
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,
granulocyte-macrophage-CSF (GM-CSF), or IL-1ß when added individually
enhanced the endogenous levels of 92-kDa gelatinase (MMP-9) and TIMP-1
but failed to induce interstitial collagenase (MMP-1). However, GM-CSF,
when added with either TNF- or IL-1ß, induced MMP-1 and
synergistically enhanced MMP-9 and TIMP-1. Th2 cytokines, such as IL-4,
inhibited the induction of MMPs and TIMP-1 by TNF-, GM-CSF, and
IL-1. Cytokine stimulation of MMP-1 was due, at least in part, to an
increase in the release of arachidonic acid and PG E2
(PGE2), because inhibition of MMP-1 by indomethacin could
be reversed by exogenous PGE2. In contrast to MMP-1,
cytokine stimulation of MMP-9 and TIMP-1 was unaffected by
indomethacin. The PGE2-independent induction of monocyte
MMP-9 and TIMP-1 by these cytokines differed from stimulation of MMP-9
and TIMP-1 by LPS, which is in large part PG-dependent. In addition,
LPS stimulated higher levels of MMP-1 whereas cytokines induced higher
levels of MMP-9 and TIMP-1. This is the first demonstration that
monocyte MMP-1 can be induced by cytokines and that MMP-1, MMP-9, and
TIMP-1 are differentially regulated by cytokines through PG-dependent
and -independent mechanisms. |
Introduction |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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The degree of connective tissue degradation by MMPs is also influenced by tissue inhibitors of MMPs (TIMPs). Four members of the TIMP family have been identified (3, 4). While all the TIMPs inhibit the active forms of metalloproteinases, TIMP-1 binds pro-gelatinase B (MMP-9) whereas TIMP-2 forms a complex with pro-gelatinase A (MMP-2). Monocytes/macrophages have been shown to produce TIMP-1 and TIMP-2, with the inducible TIMP-1 being produced in larger amounts, whereas TIMP-2 is synthesized constitutively and actually may be decreased by stimulants which activate these cells (5).
Previous studies have demonstrated that the induction of monocyte MMP
production by Con A, LPS, or extracellular matrix components such as
collagen and SPARC or osteonectin is regulated in large part by
a PG E2 (PGE2)-cAMP dependent mechanism
(6, 7, 8, 9, 10). This mechanism has been demonstrated through the
inhibition of monocyte MMP induction by indomethacin and the reversal
of suppression by exogenous agents, such as PGE2 or
dibutyryl cAMP (Bt2cAMP), which elevate intracellular
levels of cAMP. Similarly, the production of TIMP-1 by macrophages has
also been shown to be regulated by PGs (9). We have previously shown
that cytokine modulation of monocyte PGE2 also regulates
MMP production. For example, the Th2 cytokines, IL-4 and IL-10, inhibit
monocyte MMP production, in large part, as a result of their
suppression of PG synthesis (11, 12). Additional cytokines encountered
by the monocyte during entry into and at an inflammatory site that may
also influence the production of MMP by monocytes include TNF-,
IL-1ß, and the CSFs (granulocyte-macrophage CSF (GM-CSF),
macrophage-CSF, and IL-3). The proinflammatory cytokines TNF- and
IL-1ß have been shown to induce interstitial collagenase (MMP-1) and
stromelysin production by fibroblasts (1). In contrast, these MMPs were
not induced in macrophages exposed to these cytokines (13). However,
recently TNF- and IL-1ß have been shown to enhance the production
of MMP-9 by monocytes while having no effect on MMP-1 (14). Athough we
have previously reported that Ag-activated spleen cells are capable of
inducing MMP-1 production by macrophages (15), the potential cytokines
involved in the induction of MMP-1 by monocytes or macrophages are
unknown. Here we report that while TNF-, GM-CSF, or IL-1ß when
added individually stimulated only MMP-9 and TIMP-1 but not MMP-1, the
combination of GM-CSF with TNF- or IL-1ß or all three cytokines
induced the synthesis of MMP-1 and caused a further enhancement of
MMP-9 and TIMP-1. Moreover, the stimulation of MMP-1 occurs through a
PG-dependent mechanism, whereas the induction of MMP-9 and TIMP-1 by
these cytokines is PG-independent.
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Materials and Methods |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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Human peripheral blood cells were obtained by leukapheresis of normal volunteers at the Department of Transfusion Medicine at the National Institutes of Health. These cells were diluted in endotoxin-free PBS without Ca2+ and Mg2+ (BioWhittaker, Walkersville, MD) and layered over 20 ml of endotoxin-free lymphocyte sedimentation medium (Organon Teknika, Durham, NC) in 50 ml tubes (Falcon, Becton Dickinson, Oxnard, CA). After density sedimentation at 400 x g for 30 min, the monocytes in the mononuclear cell layer were purified by counterflow centrifugal elutriation on a Beckman (Torrence, CA) elutriation system as previously described (16, 17), except that pyrogen-free PBS was used in the elutriation procedure. Monocytes were enriched to >90% as determined by morphology, nonspecific esterase staining, and flow cytometry. Moreover, the purification procedure did not activate the monocytes as shown by the fact that following overnight incubation at 37°C in suspension less than 4% of these cells were IL-2R positive, a sensitive marker of monocyte activation (18).
Culture conditions
Purified monocytes were cultured in DMEM (BioWhittaker)
supplemented with 2 mM L-glutamine (Mediatech, Washington,
DC) and 10 µg/ml gentamicin sulfate (BioWhittaker). TNF- (1
x 107 U/mg) and GM-CSF (1 x 107 U/mg)
were obtained from PeproTech (Rocky Hill, NJ), and IL-1ß (1.9 x
107 U/mg) was obtained from DuPont (Wilmington, DE). LPS
(Escherichia coli O55:B5; Difco, Detroit, MI),
Bt2cAMP, PGE2, and/or indomethacin (Sigma, St.
Louis, MO) were also added to some of the cultures. Unless otherwise
stated, following purification the monocytes were adhered for 30 min
before the addition of reagents. Each experiment was repeated a minimum
of three times with different donors.
Phospholipase activity assay
Purified monocytes (2 x 106/0.5 ml of DMEM) were plated in 24-well plates for 30 min at 37°C. Then autologous or AB serum (final concentration, 10%) and 1 µCi/well of [5,6,8,9,11,12,14,15-3H]arachidonic acid were added. After 18 h of incubation the cultures were washed three times in DMEM containing 0.02% fatty-acid-free human serum albumin (Sigma) to remove the unincorporated arachidonic acid and cultured in the same medium for varying times after the addition of cytokines. Aliquots of culture medium were assayed for the release of [3H]arachidonic acid by liquid scintillation counting.
PGE2 assay
PGE2 levels in the media supernatants from monocyte cultures were determined by RIA as described (19) using rabbit anti-PGE2 antiserum (Upstate Biotechnology, Lake Placid, NY). In general, PGE2 levels were measured 24 h after stimulation to allow for maximal accumulation of this PG in the medium.
Detection of MMP-1 and TIMP-1 by Western blot analysis
For determination of MMP-1 and TIMP-1, proteins in the conditioned medium from monocyte cultures were precipitated 36 to 48 h after the addition of cytokines or LPS with cold ethanol (final concentration, 60%) at -70°C for at least 30 min. Pelleted proteins (12,000 x g for 20 min) were washed with 1 ml of ethanol and subsequently lyophilized by rotary evaporation. The lyophilized proteins for MMP-1 or TIMP-1 determination were resuspended in SDS-Laemmli loading buffer (500 mM Tris-HCl, pH 6.8/10% SDS/0.01% bromophenol-blue/20% glycerol), reduced with 1% 2-ME, heated for 2 min at 95°C, loaded, and electrophoresed on a 8–16% (MMP) Tris-glycine gradient polyacrylamide gel (Novex, San Diego, CA) in SDS running buffer (25 mM Tris-HCl, pH 8.3/192 mM glycine/10% SDS). After electrophoresis, the proteins from membranes or conditioned supernatants were transferred onto 0.45-µm nitrocellulose in a buffer containing 25 mM Tris-HCl, pH 8.3/192 mM glycine/20% methanol and blocked with 50 mM Tris-HCl, pH 7.5/150 mM NaCl/0.3% Tween-20 (TBST) containing 5% nonfat dry milk for at least 1 h. The blots were washed three times with TBST and then incubated for 1 h or overnight with primary Ab. For the detection of MMP-1 or TIMP-1, the blots were incubated with a peptide specific MMP-1 or TIMP-1 Ab (generously provided by Dr. Henning Birkedal-Hansen, National Institute of Dental Research, National Institutes of Health) followed by protein A-horseradish peroxidase (Amersham, Arlington Heights; 1:3000 dilution in TBST containing 5% nonfat dry milk) and developed with the enhanced chemiluminescence (ECL) detection system (Amersham). The Ab against MMP-1 recognized the active (ACL) and pro-collagenase (PCL) forms.
Detection of MMP-9 by zymography
MMP-9 was analyzed by zymography which involves the determination of the ability of culture supernatants to digest gelatin in polyacrylamide gels. Culture supernatants (10 µl) were added to loading buffer (10 µl) as described above for Western blot analysis except that the samples were not heated or reduced. The samples were loaded on 10% polyacrylamide gels (Novex) containing 0.1% gelatin. Following electrophoresis the gels were incubated in 0.05 M Tris-HCl, pH 7.5, containing 0.2 M NaCl, 5 mM CaCl2, and 2.5% Triton X-100 for 30 to 60 min and subsequently incubated for 2 to 4 h at room temperature in the same buffer without Triton X-100. The gels were then stained with Coomassie blue (0.25% Coomassie blue/45.4% methanol/9.2% glacial acetic acid) and destained (75% ethanol/25% glacial acetic acid).
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Results |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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Previous studies have identified cytokines, IFN-
, IL-4, and
IL-10, which inhibit the production of MMPs by monocytes (11, 12, 20, 21, 22). Here we examined cytokines that may enhance or induce MMP
production by monocytes with the potential implications this may have
at an inflammatory site. Addition of TNF-, GM-CSF, or IL-1ß alone
significantly enhanced MMP-9 production in a dose-dependent manner
(Fig. 1
, A–C). The
individual cytokines, particularly TNF- and GM-CSF, were very potent
at inducing MMP-9, with many of the experiments demonstrating that a
maximal stimulation was reached by 10 ng/ml. Thus, as shown in Figure 1B, as little as 1 ng/ml of TNF- or GM-CSF enhanced MMP-9
production and a maximal stimulation occurred by 5 to 10 ng/ml of
TNF- or GM-CSF. Moreover, when GM-CSF was added with either TNF-
or IL-1ß there was a synergistic increase in MMP-9 (Fig. 1, A and C). In contrast to MMP-9, MMP-1 was not
induced by the individual cytokines. However of considerable interest
was the ability of the combination of TNF- and GM-CSF to induce
significant levels of MMP-1 (Fig. 1A). Similar results were
also obtained with TNF-ß (data not shown). In addition, the
combination of IL-1ß with TNF- or GM-CSF also induced MMP-1, but
generally at lower levels than TNF- plus GM-CSF (Fig. 1C). The degree of MMP-1 conversion from the PCL form to the
ACL form varied between experiments, which may be dependent on the
extent of activation and/or the length of incubation. An example of
this is shown in Figure 1A in which only the ACL form was
observed whereas both PCL and ACL were detected in the experiment shown
in Figure 1C. The PCL forms had molecule weights of
approximately 57 and 55 kDa and the ACL forms were 45 and 43 kDa.
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The signal transduction pathway leading to the induction of
monocyte MMPs by activators such as Con A has been shown to involve an
increase in phospholipase activity with the subsequent release of
arachidonic acid (20). To determine whether this early step in
activation accounted for the differential regulation of MMPs by
cytokines, we examined the effect of TNF-, GM-CSF, or IL-1ß
individually or in combination on the release of arachidonic acid by
monocytes (Fig. 2). TNF-, GM-CSF, or
IL-1ß when added individually at the indicated concentrations, or at
higher concentrations (data not shown), did not significantly increase
the release of arachidonic acid above control levels. However, the
addition of these cytokines in combination induced a substantial
increase in arachidonic acid release.
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The arachidonic acid released following stimulation of the
monocytes is metabolized into various metabolites including the
eicosanoids. Of particular importance is PGE2 which has
been shown to regulate the production of monocyte MMPs (6). Therefore,
we also determined the levels of PGE2 in cytokine-treated
monocyte cultures, because this more accurately reflects the effect on
MMPs than does arachidonic acid release, which is metabolized into many
products. The combination of cytokines caused a substantial increase in
PGE2, with the combination of GM-CSF and TNF- inducing
the greatest increase, whereas cultures treated with a single cytokine
had levels of PGE2 similar to that of control cultures
(Fig. 3).
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The finding that the individual cytokines did not increase
arachidonic acid or PGE2 whereas the combination of
cytokines did suggested that this may account for the differential
regulation of MMP-1 and MMP-9. To determine whether this was the case,
indomethacin was added to some of the cultures. As shown in Figure 4A, the induction of MMP-1 by
GM-CSF plus TNF- or IL-1ß or all three cytokines was significantly
inhibited by indomethacin. The data used in Figure 4A were
from a donor whose monocytes, unlike the monocytes from the majority of
donors, were partially activated since very low levels of MMP-1 were
stimulated by GM-CSF or IL-1ß treatment alone, which were also
inhibited by indomethacin. The lack of complete inhibition by
indomethacin of MMP-1 induced by the combination of cytokines is also
most likely related to prior partial activation in vivo. This differed
from the majority of experiments, as represented by Figure 4B, in which indomethacin caused a complete inhibition of
MMP-1. In contrast to MMP-1, the enhancement of MMP-9 by TNF-,
GM-CSF, or IL-1ß alone or in combination was not inhibited by
indomethacin. Thus the induction of MMP-1 by cytokines occurs through a
PG-dependent mechanism whereas the enhancement of MMP-9 is
PG-independent.
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B, PGE2 or
Bt2cAMP reversed the inhibition by indomethacin of cytokine
induced MMP-1 production. Moreover, the addition of PGE2 or
Bt2cAMP with TNF- and GM-CSF, in the absence of
indomethacin, resulted in a significant enhancement of MMP-1 over that
induced by the cytokines (Fig. 4C). Thus, exogenous
PGE2 or Bt2cAMP can increase MMP-1 production
beyond the maximum stimulation by the combination of cytokines,
indicating that the exogenous levels of PGE2 at an
inflammatory site may potentiate the induction of MMP-1 by cytokines.
This was in contrast to cytokine induction of MMP-9, which was not
enhanced by PGE2 or Bt2cAMP (data not shown).
Effect of TNF- and GM-CSF on TIMP-1
In addition to the contribution of MMPs, the degree of connective
tissue destruction is also influenced by TIMPs. Of the family of TIMPs,
TIMP-1 and TIMP-2 have been reported to be produced by
monocytes/macrophages (5). Because TIMP-1 is inducible as compared with
TIMP-2 which is constitutively expressed, we focused on the effect of
cytokines on TIMP-1. As shown in Figure 5, TIMP-1, like MMP-9, was enhanced by
TNF- or GM-CSF with a further increase when these cytokines were
added together. Also similar to MMP-9, TIMP-1 induction by these
cytokines was not inhibited by indomethacin. These findings were in
contrast to the stimulation of TIMP-1 by LPS, which could be decreased
by indomethacin (Fig. 5). In addition, the stimulation of TIMP-1
production by cytokines was unaffected by the addition of
PGE2 or Bt2cAMP (data not shown).
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and GM-CSF-induced MMPs and TIMP-1
We have shown previously that theTh2 derived cytokine IL-4
inhibits Con A or LPS induced MMP production by monocytes, suggesting
that the ratio of cell types, particularly that of T cell subsets, may
determine the outcome of an inflammatory lesion. Therefore, we examined
the effect of IL-4 on the induction of monocyte MMP-1, MMP-9, and
TIMP-1 by the combination of TNF- and GM-CSF. IL-4 caused a
significant inhibition of TNF- and GM-CSF induced MMP-1 and MMP-9
production when added 60 to 30 min before these cytokines or even at
the same time as the cytokines (Fig. 6).
The inhibitory effect of IL-4 on MMP-1 or MMP-9 was still observed when
IL-4 was added 30 to 60 min after TNF- and GM-CSF, indicating IL-4
inhibits cytokine-mediated MMP production at a relatively late stage in
the induction or processing of these enzymes. Similar results were
observed with TIMP-1 (data not shown).
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LPS is a known potent activator of monocytes/macrophages and
therefore we compared the degree of induction of monocyte MMPs by LPS
with that of cytokines. As demonstrated in Figure 7, LPS induced substantially higher
levels of MMP-1 than a combination of TNF- and GM-CSF. The degree to
which LPS increased MMP-1 above that stimulated with the cytokines
varied between experiments, with the data in Figure 7 demonstrating an
example of the maximal differential observed. In contrast to MMP-1, but
similar to TIMP-1 induction (Fig. 5), the combination of TNF- and
GM-CSF stimulated monocytes to produce significantly higher levels of
MMP-9 than LPS. These findings demonstrate that there is a differential
expression of MMPs and TIMP-1 by monocytes depending on whether the
monocytes are exposed to LPS or cytokines.
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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, IL-4, and IL-10 to
inhibit the production of these enzymes (11, 12, 13, 20, 21, 22). Recently,
monocyte/macrophage MMPs have been shown to be selectively up-regulated
by cytokines with the demonstration that MMP-9 but not MMP-1 or TIMP-1
can be enhanced by IL-1 or TNF- (14). Our findings confirm the
ability of IL-1 or TNF- to enhance MMP-9 but not MMP-1 and, in
addition, show for the first time that monocyte MMP-1 production can be
induced by cytokines when the combination of TNF- and GM-CSF or
GM-CSF and IL-1 are added simultaneously. In contrast to the findings
of Saren et al. (14), TIMP-1 was increased by these cytokines.
The different culture times before exposure of the
monocytes/macrophages to cytokines may account for this discrepancy. In
general, the combination of TNF- and GM-CSF was significantly more
effective in the induction of MMP-1 and in the enhancement of MMP-9 and
TIMP-1 than if IL-1 was combined with GM-CSF.
Previous studies have demonstrated that monocytes stimulated with Con
A, LPS, zymosan, type I and type III collagen, laminin peptides, and
SPARC produce MMPs through a PG-dependent pathway (6, 7, 8, 9, 10). The findings
in the present study demonstrate that the induction of MMP-1 by the
combination of cytokines is also PG-dependent. Evidence for this was
shown by the ability of indomethacin to inhibit the production of MMP-1
which could be restored by PGE2 or Bt2cAMP.
Further support for this was the stimulation of the release of
arachidonic acid and PGE2 by the combination of cytokines,
which was not the case for the individual cytokines. Other CSFs, such
as IL-3 or macrophage-CSF, in combination with TNF- also induced
MMP-1 production, but not when added alone (data not shown). Although
macrophage-CSF has been reported to increase the release of low levels
of arachidonic acid and PGE2 from monocytes (23), these
amounts may be below that needed for the induction of MMP-1 and/or an
additional signal event is required. This latter possibility is
suggested by the failure to induce MMP-1 when Bt2cAMP or
PGE2 was added to monocytes treated with either TNF- or
GM-CSF, but did enhance MMP-1 production when added to the combination
of cytokines. As we have previously shown (6), the addition of cAMP
elevating agents to monocytes in the absence of a primary stimulus
fails to increase MMP-1 production by monocytes. An appropriate primary
stimulus is likely required to cause alterations in the cytoskeletal
framework and/or activation of additional transcription factors
necessary for the PGE2-mediated induction of MMP-1.
In contrast to MMP-1, regulation of MMP-9 and TIMP-1 by cytokines
differed in several aspects. First, unlike MMP-1, MMP-9 and TIMP-1 were
enhanced by the individual addition of TNF-, GM-CSF or IL-1. Second,
the cytokine-induced increase in MMP-9 and TIMP-1 was not inhibited by
indomethacin. This differs from previous findings with stimulants such
as Con A, LPS, zymosan, denatured collagen, and SPARC, in which the
enhancement of the basal levels of 92-kDa gelatinase could be
substantially inhibited by indomethacin (9, 10, 11). Similarly, the
stimulation of TIMP-1 by LPS, zymosan, or denatured collagen has also
been shown to be inhibited by indomethacin (9). Thus, the signal
transduction pathway(s) utilized by the cytokines individually or in
combination for the enhancement of MMP-9 and TIMP-1 are PG-independent.
It is unclear at this time as to how cytokines differ in their
regulation of monocyte MMP-9 from other agonists; however, TNF-,
GM-CSF, and IL-1 are known to influence or act through several signal
transduction pathways (24, 25, 26, 27). Depending on the signal transduction
pathways invoked by the individual or combined cytokines, differing
sets or levels of transactivating factors may be affected. The
cytokine-mediated signal transduction pathways and promoter elements
leading to MMP production by monocytes appear to differ, at least in
part, from other cell types. For example, in contrast to monocytes,
TNF- or IL-1 alone have been shown to directly induce MMP-1 in cells
such as fibroblasts and synovial adherent cells (1). In addition,
studies with U937 cells, a human monocytic cell line, have demonstrated
that the upstream promoter elements such as the polyoma enhancer
A-binding protein-3 site (PEA-3) and TTCA sequence
involved in the induction of MMP-1 in fibroblasts do not play a major
role, if any, in the activation of the collagenase gene in monocytic
cells (28). The critical sequences in the collagenase promoter for
MMP-1 production by LPS stimulated U937 cells were from -72 to the
transcription start site which included AP-1. The sequence of events
initiated by the combination of cytokines leading to the production of
MMP-1 by primary monocytes may involve upstream events in multiple
pathways that converge on a specific combination of transactivating
factors.
From this and previous studies it is clear that the types and amounts
of cytokines present at an inflammatory site may determine the extent
of connective tissue degradation. For example, the Th2 cytokines, IL-10
and IL-4, have been shown to suppress monocyte MMPs (11, 12, 21, 22).
As shown here, Th2 cytokines, as represented by IL-4, can also
effectively suppress the induction of MMP-1 and the enhancement of
MMP-9 and TIMP-1 by TNF- and GM-CSF. Thus, the balance between
cytokines such as TNF-, GM-CSF, and IL-1 and the Th2 cytokines may
be important in the outcome of an inflammatory response. This is
further indicated by the paucity of Th2-derived cytokines in many
inflammatory lesions (29, 30), which may allow unabated production of
MMPs.
The findings presented here demonstrate that the cytokines present at the tissue site may have a dramatic impact on the degree and specificity of the MMPs produced by monocytes/macrophages. The initial exposure of monocytes to low levels of a single or a combination of cytokines emanating from the vascular wall at an inflammation site may induce MMP-9, which would facilitate their migration through the basement membrane. Once at the site of inflammation the higher levels of a combination of cytokines would induce MMP-1 and initiate the destruction of fibrillar collagen. The stimulation of monocyte MMPs by cytokines through PG-independent (MMP-9) and PG-dependent (MMP-1) mechanisms provide insight into the therapeutic considerations aimed at regulating these MMPs.
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Acknowledgments |
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Footnotes |
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2 Abbreviations used in this paper: MMPs, matrix metalloproteinases; TIMPs, tissue inhibitor of matrix metalloproteinases; MMP-1, interstitial collagenase; MMP-9, 92-kDa gelatinase; PGE2, PG E2; Bt2cAMP, dibutyryl cAMP; GM-CSF, granulocyte-macrophage CSF; PCL, pro-collagenase; ACL, active collagenase; SPARC, secreted protein, acidic and rich in cysteine.
Received for publication January 9, 1998. Accepted for publication May 8, 1998.
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References |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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. J. Clin. Invest. 86:1204.
blocks endogenous prostaglandin E2-dependent collagenase production. J. Immunol. 144:3518.[Abstract]
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 N. L. Webster and S. M. Crowe Matrix metalloproteinases, their production by monocytes and macrophages and their potential role in HIV-related diseases J. Leukoc. Biol., November 1, 2006; 80(5): 1052 - 1066. [Abstract] [Full Text] [PDF]
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B. J. Gu and J. S. Wiley Rapid ATP-induced release of matrix metalloproteinase 9 is mediated by the P2X7 receptor Blood, June 15, 2006; 107(12): 4946 - 4953. [Abstract] [Full Text] [PDF]
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 M. Illemann, N. Bird, A. Majeed, M. Sehested, O. D. Laerum, L. R. Lund, K. Dano, and B. S. Nielsen MMP-9 Is Differentially Expressed in Primary Human Colorectal Adenocarcinomas and Their Metastases Mol. Cancer Res., May 1, 2006; 4(5): 293 - 302. [Abstract] [Full Text] [PDF]
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 C.-H. Chen, K.-C. Lin, D. T. Y. Yu, C. Yang, F. Huang, H.-A. Chen, T.-H. Liang, H.-T. Liao, C.-Y. Tsai, J. C. C. Wei, et al. Serum matrix metalloproteinases and tissue inhibitors of metalloproteinases in ankylosing spondylitis: MMP-3 is a reproducibly sensitive and specific biomarker of disease activity Rheumatology, April 1, 2006; 45(4): 414 - 420. [Abstract] [Full Text] [PDF]
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 S. Rosch, R. Ramer, K. Brune, and B. Hinz R(+)-Methanandamide and Other Cannabinoids Induce the Expression of Cyclooxygenase-2 and Matrix Metalloproteinases in Human Nonpigmented Ciliary Epithelial Cells J. Pharmacol. Exp. Ther., March 1, 2006; 316(3): 1219 - 1228. [Abstract] [Full Text] [PDF]
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 H. N. Jabbour, R. W. Kelly, H. M. Fraser, and H. O. D. Critchley Endocrine Regulation of Menstruation Endocr. Rev., February 1, 2006; 27(1): 17 - 46. [Abstract] [Full Text] [PDF]
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 K. Fredriksson, X. D. Liu, J. Lundahl, J. Klominek, S. I. Rennard, and C. M. Skold Red blood cells increase secretion of matrix metalloproteinases from human lung fibroblasts in vitro Am J Physiol Lung Cell Mol Physiol, February 1, 2006; 290(2): L326 - L333. [Abstract] [Full Text] [PDF]
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Y. Zhang and L. M. Wahl Synergistic enhancement of cytokine-induced human monocyte matrix metalloproteinase-1 by C-reactive protein and oxidized LDL through differential regulation of monocyte chemotactic protein-1 and prostaglandin E2 J. Leukoc. Biol., January 1, 2006; 79(1): 105 - 113. [Abstract] [Full Text] [PDF]
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P. T. G. Elkington, R. K. Nuttall, J. J. Boyle, C. M. O'Kane, D. E. Horncastle, D. R. Edwards, and J. S. Friedland Mycobacterium tuberculosis, but Not Vaccine BCG, Specifically Upregulates Matrix Metalloproteinase-1 Am. J. Respir. Crit. Care Med., December 15, 2005; 172(12): 1596 - 1604. [Abstract] [Full Text] [PDF]
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 E. Elass, L. Aubry, M. Masson, A. Denys, Y. Guerardel, E. Maes, D. Legrand, J. Mazurier, and L. Kremer Mycobacterial Lipomannan Induces Matrix Metalloproteinase-9 Expression in Human Macrophagic Cells through a Toll-Like Receptor 1 (TLR1)/TLR2- and CD14-Dependent Mechanism Infect. Immun., October 1, 2005; 73(10): 7064 - 7068. [Abstract] [Full Text] [PDF]
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 A. Daugherty, N. R. Webb, D. L. Rateri, and V. L. King Thematic review series: The Immune System and Atherogenesis. Cytokine regulation of macrophage functions in atherogenesis J. Lipid Res., September 1, 2005; 46(9): 1812 - 1822. [Abstract] [Full Text] [PDF]
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M. P. Kim, M. Zhou, and L. M. Wahl Angiotensin II increases human monocyte matrix metalloproteinase-1 through the AT2 receptor and prostaglandin E2: implications for atherosclerotic plaque rupture J. Leukoc. Biol., July 1, 2005; 78(1): 195 - 201. [Abstract] [Full Text] [PDF]
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Y. Lu and L. M. Wahl Production of matrix metalloproteinase-9 by activated human monocytes involves a phosphatidylinositol-3 kinase/Akt/IKK{alpha}/NF-{kappa}B pathway J. Leukoc. Biol., July 1, 2005; 78(1): 259 - 265. [Abstract] [Full Text] [PDF]
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R. Han and T. J. Smith Induction by IL-1{beta} of Tissue Inhibitor of Metalloproteinase-1 in Human Orbital Fibroblasts: Modulation of Gene Promoter Activity by IL-4 and IFN-{gamma} J. Immunol., March 1, 2005; 174(5): 3072 - 3079. [Abstract] [Full Text] [PDF]
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M. P. Kim, C. A. Gaydos, B. J. Wood, J. P. Hardick, Y. Zhang, and L. M. Wahl Chlamydia pneumoniae Enhances Cytokine-Stimulated Human Monocyte Matrix Metalloproteinases through a Prostaglandin E2-Dependent Mechanism Infect. Immun., January 1, 2005; 73(1): 632 - 634. [Abstract] [Full Text] [PDF]
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F. E. Baratelli, N. Heuze-Vourc'h, K. Krysan, M. Dohadwala, K. Riedl, S. Sharma, and S. M. Dubinett Prostaglandin E2-Dependent Enhancement of Tissue Inhibitors of Metalloproteinases-1 Production Limits Dendritic Cell Migration through Extracellular Matrix J. Immunol., November 1, 2004; 173(9): 5458 - 5466. [Abstract] [Full Text] [PDF]
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B Safieh-Garabedian, G M Mouneimne, W El-Jouni, M Khattar, and R Talhouk The effect of endotoxin on functional parameters of mammary CID-9 cells Reproduction, March 1, 2004; 127(3): 397 - 406. [Abstract] [Full Text] [PDF]
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Y. Nakamura, S. Esnault, T. Maeda, E. A. B. Kelly, J. S. Malter, and N. N. Jarjour Ets-1 Regulates TNF-{alpha}-Induced Matrix Metalloproteinase-9 and Tenascin Expression in Primary Bronchial Fibroblasts J. Immunol., February 1, 2004; 172(3): 1945 - 1952. [Abstract] [Full Text] [PDF]
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N. M. Price, R. H. Gilman, J. Uddin, S. Recavarren, and J. S. Friedland Unopposed Matrix Metalloproteinase-9 Expression in Human Tuberculous Granuloma and the Role of TNF-{alpha}-Dependent Monocyte Networks J. Immunol., November 15, 2003; 171(10): 5579 - 5586. [Abstract] [Full Text] [PDF]
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M. Zhou, Y. Zhang, J. A. Ardans, and L. M. Wahl Interferon-{gamma} Differentially Regulates Monocyte Matrix Metalloproteinase-1 and -9 through Tumor Necrosis Factor-{alpha} and Caspase 8 J. Biol. Chem., November 14, 2003; 278(46): 45406 - 45413. [Abstract] [Full Text] [PDF]
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 S. S. Barbieri, S. Eligini, M. Brambilla, E. Tremoli, and S. Colli Reactive oxygen species mediate cyclooxygenase-2 induction during monocyte to macrophage differentiation: critical role of NADPH oxidase Cardiovasc Res, October 15, 2003; 60(1): 187 - 197. [Abstract] [Full Text] [PDF]
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 G. PLENZ, H. ESCHERT, S. BEISSERT, V. ARPS, J. R. SINDERMANN, H. ROBENEK, and W. VOLKER Alterations in the vascular extracellular matrix of granulocyte macrophage colony-stimulating factor (GM-CSF) -deficient mice FASEB J, August 1, 2003; 17(11): 1451 - 1457. [Abstract] [Full Text] [PDF]
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H Tsuboi, Y Matsui, K Hayashida, S Yamane, M Maeda-Tanimura, A Nampei, J Hashimoto, R Suzuki, H Yoshikawa, and T Ochi Tartrate resistant acid phosphatase (TRAP) positive cells in rheumatoid synovium may induce the destruction of articular cartilage Ann Rheum Dis, March 1, 2003; 62(3): 196 - 203. [Abstract] [Full Text] [PDF]
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 D Reinhardt, H H Sigusch, J Hensse, S C Tyagi, R Korfer, and H R Figulla Cardiac remodelling in end stage heart failure: upregulation of matrix metalloproteinase (MMP) irrespective of the underlying disease, and evidence for a direct inhibitory effect of ACE inhibitors on MMP Heart, December 1, 2002; 88(5): 525 - 530. [Abstract] [Full Text] [PDF]
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 M. Abraham, S. Shapiro, N. Lahat, and A. Miller The role of IL-18 and IL-12 in the modulation of matrix metalloproteinases and their tissue inhibitors in monocytic cells Int. Immunol., December 1, 2002; 14(12): 1449 - 1457. [Abstract] [Full Text] [PDF]
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 W. Mattos, S. Lim, R. Russell, A. Jatakanon, K. F. Chung, and P. J. Barnes Matrix Metalloproteinase-9 Expression in Asthma: Effect of Asthma Severity, Allergen Challenge, and Inhaled Corticosteroids Chest, November 1, 2002; 122(5): 1543 - 1552. [Abstract] [Full Text] [PDF]
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 P. Spessotto, F. M. Rossi, M. Degan, R. Di Francia, R. Perris, A. Colombatti, and V. Gattei Hyaluronan-CD44 interaction hampers migration of osteoclast-like cells by down-regulating MMP-9 J. Cell Biol., September 16, 2002; 158(6): 1133 - 1144. [Abstract] [Full Text] [PDF]
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 C.-M. Liu, C.-Y. Hong, C.-T. Shun, T.-Y. Hsiao, C.-C. Wang, J.-S. Wang, M. Hsiao, and S.-K. Lin Inducible Cyclooxygenase and Interleukin 6 Gene Expressions in Nasal Polyp Fibroblasts: Possible Implication in the Pathogenesis of Nasal Polyposis Arch Otolaryngol Head Neck Surg, August 1, 2002; 128(8): 945 - 951. [Abstract] [Full Text] [PDF]
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E. Scandella, Y. Men, S. Gillessen, R. Forster, and M. Groettrup Prostaglandin E2 is a key factor for CCR7 surface expression and migration of monocyte-derived dendritic cells Blood, July 30, 2002; 100(4): 1354 - 1361. [Abstract] [Full Text] [PDF]
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J. A. Ardans, A. P. Economou, J. M. Martinson Jr., M. Zhou, and L. M. Wahl Oxidized low-density and high-density lipoproteins regulate the production of matrix metalloproteinase-1 and -9 by activated monocytes J. Leukoc. Biol., June 1, 2002; 71(6): 1012 - 1018. [Abstract] [Full Text] [PDF]
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 R. H. Eckel, M. Wassef, A. Chait, B. Sobel, E. Barrett, G. King, M. Lopes-Virella, J. Reusch, N. Ruderman, G. Steiner, et al. Prevention Conference VI: Diabetes and Cardiovascular Disease: Writing Group II: Pathogenesis of Atherosclerosis in Diabetes Circulation, May 7, 2002; 105 (18): e138 - e143. [Full Text] [PDF]
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 G. A. Limb, J. T. Daniels, R. Pleass, D. G. Charteris, P. J. Luthert, and P. T. Khaw Differential Expression of Matrix Metalloproteinases 2 and 9 by Glial Muller Cells : Response to Soluble and Extracellular Matrix-Bound Tumor Necrosis Factor-{alpha} Am. J. Pathol., May 1, 2002; 160(5): 1847 - 1855. [Abstract] [Full Text] [PDF]
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 F. Reno, P. Grazianetti, M. Stella, G. Magliacani, C. Pezzuto, and M. Cannas Release and Activation of Matrix Metalloproteinase-9 During In Vitro Mechanical Compression in Hypertrophic Scars Arch Dermatol, April 1, 2002; 138(4): 475 - 478. [Abstract] [Full Text] [PDF]
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Y. K. Zhu, X. Liu, R. F. Ertl, T. Kohyama, F. Q. Wen, H. Wang, J. R. Spurzem, D. J. Romberger, and S. I. Rennard Retinoic Acid Attenuates Cytokine-Driven Fibroblast Degradation of Extracellular Matrix in Three-Dimensional Culture Am. J. Respir. Cell Mol. Biol., November 1, 2001; 25(5): 620 - 627. [Abstract] [Full Text] [PDF]
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Y. K. Zhu, X. D. Liu, C. M. Skold, T. Umino, H. J. Wang, J. R. Spurzem, T. Kohyama, R. F. Ertl, and S. I. Rennard Synergistic neutrophil elastase-cytokine interaction degrades collagen in three-dimensional culture Am J Physiol Lung Cell Mol Physiol, October 1, 2001; 281(4): L868 - L878. [Abstract] [Full Text] [PDF]
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D. Baram, G. G. Vaday, P. Salamon, I. Drucker, R. Hershkoviz, and Y. A. Mekori Human Mast Cells Release Metalloproteinase-9 on Contact with Activated T Cells: Juxtacrine Regulation by TNF-{alpha} J. Immunol., October 1, 2001; 167(7): 4008 - 4016. [Abstract] [Full Text] [PDF]
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M. Quiding-Jarbrink, D. A. Smith, and G. J. Bancroft Production of Matrix Metalloproteinases in Response to Mycobacterial Infection Infect. Immun., September 1, 2001; 69(9): 5661 - 5670. [Abstract] [Full Text] [PDF]
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 E. E.J.M. Creemers, J. P.M. Cleutjens, J. F.M. Smits, and M. J.A.P. Daemen Matrix Metalloproteinase Inhibition After Myocardial Infarction: A New Approach to Prevent Heart Failure? Circ. Res., August 3, 2001; 89(3): 201 - 210. [Abstract] [Full Text] [PDF]
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 J. A. Ardans, A. Blum, P. R. Mangan, S. Wientroub, R. O. Cannon III, and L. M. Wahl Raloxifene-Mediated Increase in Matrix Metalloproteinase-1 Production by Activated Monocytes Arterioscler Thromb Vasc Biol, August 1, 2001; 21(8): 1265 - 1268. [Abstract] [Full Text] [PDF]
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G. G. Vaday, S. Franitza, H. Schor, I. Hecht, A. Brill, L. Cahalon, R. Hershkoviz, and O. Lider Combinatorial signals by inflammatory cytokines and chemokines mediate leukocyte interactions with extracellular matrix J. Leukoc. Biol., June 1, 2001; 69(6): 885 - 892. [Abstract] [Full Text] [PDF]
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D. K. Madtes, A. L. Elston, L. A. Kaback, and J. G. Clark Selective Induction of Tissue Inhibitor of Metalloproteinase-1 in Bleomycin-Induced Pulmonary Fibrosis Am. J. Respir. Cell Mol. Biol., May 1, 2001; 24(5): 599 - 607. [Abstract] [Full Text]
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G. G. Vaday, H. Schor, M. A. Rahat, N. Lahat, and O. Lider Transforming growth factor-{beta} suppresses tumor necrosis factor {alpha}-induced matrix metalloproteinase-9 expression in monocytes J. Leukoc. Biol., April 1, 2001; 69(4): 613 - 621. [Abstract] [Full Text]
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 B. C. Kieseier, C. Schneider, J. M. Clements, A. J. H. Gearing, R. Gold, K. V. Toyka, and H.-P. Hartung Expression of specific matrix metalloproteinases in inflammatory myopathies Brain, February 1, 2001; 124(2): 341 - 351. [Abstract] [Full Text] [PDF]
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 D. Zanger, B. K. Yang, J. Ardans, M. A. Waclawiw, G. Csako, L. M. Wahl, and R. O. Cannon III Divergent effects of hormone therapy on serum markers of inflammation in postmenopausal women with coronary artery disease on appropriate medical management J. Am. Coll. Cardiol., November 15, 2000; 36(6): 1797 - 1802. [Abstract] [Full Text] [PDF]
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G. G. Vaday, R. Hershkoviz, M. A. Rahat, N. Lahat, L. Cahalon, and O. Lider Fibronectin-bound TNF-{alpha} stimulates monocyte matrix metalloproteinase-9 expression and regulates chemotaxis J. Leukoc. Biol., November 1, 2000; 68(5): 737 - 747. [Abstract] [Full Text]
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 Z. Kadri, E. Petitfrère, C. Boudot, J.-M. Freyssinier, S. Fichelson, P. Mayeux, H. Emonard, W. Hornebeck, B. Haye, and C. Billat Erythropoietin Induction of Tissue Inhibitors of Metalloproteinase-1 Expression and Secretion Is Mediated by Mitogen-activated Protein Kinase and Phosphatidylinositol 3-kinase Pathways Cell Growth Differ., November 1, 2000; 11(11): 573 - 580. [Abstract] [Full Text]
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C. Chizzolini, R. Rezzonico, C. De Luca, D. Burger, and J.-M. Dayer Th2 Cell Membrane Factors in Association with IL-4 Enhance Matrix Metalloproteinase-1 (MMP-1) While Decreasing MMP-9 Production by Granulocyte-Macrophage Colony-Stimulating Factor-Differentiated Human Monocytes J. Immunol., June 1, 2000; 164(11): 5952 - 5960. [Abstract] [Full Text] [PDF]
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 C S SETHI, T A BAILEY, P J LUTHERT, and N H V CHONG Matrix metalloproteinase biology applied to vitreoretinal disorders Br J Ophthalmol, June 1, 2000; 84(6): 654 - 666. [Full Text]
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 R. Lichtinghagen, O. Huegel, T. Seifert, C. I. Haberkorn, D. Michels, P. Flemming, M. Bahr, and K. H.W. Boeker Expression of Matrix Metalloproteinase-2 and -9 and Their Inhibitors in Peripheral Blood Cells of Patients with Chronic Hepatitis C Clin. Chem., February 1, 2000; 46(2): 183 - 192. [Abstract] [Full Text] [PDF]
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A. Schmid-Kotsas, H.-J. Gross, A. Menke, H. Weidenbach, G. Adler, M. Siech, H. Beger, A. Grunert, and M. G. Bachem Lipopolysaccharide-Activated Macrophages Stimulate the Synthesis of Collagen Type I and C-Fibronectin in Cultured Pancreatic Stellate Cells Am. J. Pathol., November 1, 1999; 155(5): 1749 - 1758. [Abstract] [Full Text] [PDF]
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 S. Kimmins and L. A. MacLaren Cyclic Modulation of Integrin Expression in Bovine Endometrium Biol Reprod, November 1, 1999; 61(5): 1267 - 1274. [Abstract] [Full Text]
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S. Saito, N. Yamaji, K. Yasunaga, T. Saito, S.-i. Matsumoto, M. Katoh, S. Kobayashi, and Y. Masuho The Fibronectin Extra Domain A Activates Matrix Metalloproteinase Gene Expression by an Interleukin-1-dependent Mechanism J. Biol. Chem., October 22, 1999; 274(43): 30756 - 30763. [Abstract] [Full Text] [PDF]
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 A. Cox, N. J. Camp, C. Cannings, F. S. d. Giovine, M. Dale, J. Worthington, S. John, W. E. R. Ollier, A. J. Silman, and G. W. Duff Combined sib-TDT and TDT provide evidence for linkage of the interleukin-1 gene cluster to erosive rheumatoid arthritis Hum. Mol. Genet., September 1, 1999; 8(9): 1707 - 1713. [Abstract] [Full Text] [PDF]
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U. T. Shankavaram, W.-C. Lai, S. Netzel-Arnett, P. R. Mangan, J. A. Ardans, N. Caterina, W. G. Stetler-Stevenson, H. Birkedal-Hansen, and L. M. Wahl Monocyte Membrane Type 1-Matrix Metalloproteinase. PROSTAGLANDIN-DEPENDENT REGULATION AND ROLE IN METALLOPROTEINASE-2 ACTIVATION J. Biol. Chem., May 25, 2001; 276(22): 19027 - 19032. [Abstract] [Full Text] [PDF]
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