| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Vascular Medicine and Atherosclerosis Unit, Cardiovascular Division, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA 02115
 |
Abstract |
|---|
 Top Abstract IntroductionMaterials and MethodsResultsDiscussionReferences |
|---|
. The present study
indicates a biphasic regulation of IL-1ß activity by MMPs: a
caspase-1-independent pathway of IL-1ß activation and inhibition of
IL-1ß activity by degrading the mature cytokine. The balance of the
respective MMPs and pIL-1ß might regulate the long term appearance of
IL-1ß activity at sites of acute or chronic
inflammation. |
Introduction |
|---|
|
TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
|---|
, biologic activity of IL-1ß requires processing
into the mature 18-kDa protein (3, 6, 7). This processing involves
proteolytic removal of the N-terminal portion of the precursor protein
(8, 9, 10) and is associated with IL-1ß-converting enzyme (ICE; or
caspase-1), an intracellular cysteine protease that cleaves the
precursor at position Asp116-Ala117 (11, 12, 13, 14).
The function of caspase-1 in the release of mature IL-1ß
(mIL-1ß)3 is well
established, and several in vitro as well as in vivo studies have shown
that cells that do not express caspase-1, such as fibroblasts and
keratinocytes (15, 16, 17), as well as caspase-1-deficient mice (18, 19),
lack the capacity to release mIL-1ß. However, recent in vivo studies
of local inflammation in caspase-1-deficient mice as well as in human
keratinocytes suggest caspase-1-independent mechanisms of IL-1ß
activation (20, 21). Aside from caspase-1, other proteases capable of
cleaving the IL-1ß precursor (pIL-1ß) include bacterial enzymes
(22), trypsin, or chymotrypsin (5, 6, 23), as well as the
physiologically more relevant enzymes, leukocyte elastase (6) and
granzyme A (24). Except for granzyme A, all of these proteases cleave
the pIL-1ß N terminal of the caspase-1 cleavage site, resulting in
fragments of >18 kDa. IL-1ß is an autoregulated protein, inducing its own expression (25, 26). Despite a decade of study on the mechanism(s) of activation and catabolism of the IL-1ß protein, surprisingly little is known about the fate of active IL-1ß. However, regulation of the local level of this potent and pleiotropic mediator (1, 27, 28) would seem crucial to avoid a self-perpetrating positive feedback loop of this autoinducible mediator.
Overexpression of IL-1ß occurs in various inflammatory diseases, including rheumatoid arthritis and atherosclerosis (1), conditions that also involve induction of matrix metalloproteinases (MMPs) (29, 30, 31, 32, 33). Different members of the MMP family contribute to the matrix degradation, including collagenases (such as interstitial collagenase, MMP-1), gelatinases (such as gelatinase A (MMP-2) and B (MMP-9)), or stromelysins (such as stromelysin-1, MMP-3) (34, 35). Cells associated with the diseases mentioned above, such as macrophages and vascular endothelial and smooth muscle cells, overexpress these MMPs at the sites of inflammation (30, 36, 37). Indeed, cytokines such as IL-1ß regulate the expression and activation of MMPs, a scenario that sets the stage for cross-regulation among these two classes of effectors of inflammation.
Since active MMPs as well as active IL-1ß colocalize at sites of inflammation and since the activation of IL-1ß does not necessarily depend on the presence of caspase-1, the current study tested the hypothesis that MMPs can modulate IL-1ß activity. We report here that the matrix metalloproteinases stromelysin-1, gelatinase A, and gelatinase B, but not interstitial collagenase, convert the inactive pIL-1ß into biologically active forms. Upon prolonged exposure, MMP-3 further degrades IL-1ß, yielding loss of biologic activity. These results suggest a novel role for these enzymes in the regulation of IL-1ß activity, e.g., at sites of acute or chronic inflammation.
|
Materials and Methods |
|---|
|
TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
|---|
Recombinant human MMP-2 and MMP-9 as well as the tissue
inhibitor of MMP-1 (TIMP-1) were purchased from Calbiochem (San Diego,
CA). The gelatinases were obtained as p-aminophenylmercuric
acetate (APMA)-activated, truncated enzymes (Calbiochem cat. No. PF023
and PF024). MMP-1 and MMP-3 were obtained as zymogens from Merck
Research Laboratories (Rahway, NJ) and were activated by incubation
with APMA (10 µM) for 3 h at 37°C. The APMA treatment
presumably produces active MMP-1 by cleavage of the
Val82-Leu83 (38) and active MMP-3 by cleavage
of the His82-Phe83 bond (39, 40). APMA was
removed by G-25 column chromatography. Activation of the enzymes
was confirmed by Western blotting as well as in hydrolysis assays
employing the fluorogenic substrate
MocAc-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 for
MMP-1; NFF-2
(MocAc-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys(Dnp)-NH2)
for MMP-2/-9; and NFF-3
(MocAc-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2)
(all from Peptide Institute, Osaka, Japan) for MMP-3. The
substrate (1 µM) and the respective rMMP (200 ng) were incubated for
3 h at 37°C and fluorescence intensity determined in a
fluorescence spectrometer (Perkin-Elmer, Norwalk, CT). All MMPs
employed in the present study were activated via APMA treatment and
share similar levels of enzymatic activity as determined by cleavage of
the respective fluorogenic substrate. Polyclonal rabbit
anti-IL-1ß and anti-IL-1 Ab were obtained from Upstate
Biotechnology (Lake Placid, NY). Recombinant human caspase-1 was
prepared as described previously (41). The secondary goat
anti-rabbit Ab was purchased from Jackson Immunoresearch (West
Grove, PA). The nucleotide [3H]thymidine was obtained
from Dupont-NEN (Boston, MA).
Processing assay
To study processing, recombinant human pIL-1ß or mIL-1 (both
at 50 ng) was incubated with the indicated concentrations of the
respective rMMP for the indicated times. Specificity of pIL-1ß
processing by MMPs was analyzed in processing assays performed in the
absence or presence of TIMP-1 (1 µg/ml). All processing assays were
performed in a final volume of 50 µl. For Western blot analysis,
processing was stopped by heating the samples (10 min, 95°C) in 10
µl SDS-PAGE (5x) sample buffer (0.2 M Tris, 5% glycerol, 0.1% SDS,
3% ß-mercaptoethanol, 0.1 mg/ml bromophenol blue, final
concentrations). For detection of IL-1ß activity, the processing
assay was stopped by adding excess rTIMP-1 (1 µg/ml) and freezing the
samples. The presence of TIMP-1 did not affect the assay (see also Fig. 1
).
|
The preparations of the processing assays were separated by standard SDS-PAGE under reducing conditions and transferred to polyvinylidene fluoride (PVDF) membranes using a semidry blotting apparatus (3.0 mA/cm2, 30 min; Bio-Rad, Hercules, CA). Blots were blocked for 2 h, and first and second Abs were diluted in 5% defatted dry milk/PBS/0.1% Tween 20. After 1 h of incubation with the respective primary Ab (1:1000), blots were washed four times for 15 min in PBS/0.1% Tween 20, and the secondary peroxidase-conjugated goat anti-rabbit Ab (1:10,000) was added for another hour. Finally, after four washings (20 min, PBS/0.1% Tween 20), detection of the Ag was conducted using the enhanced chemiluminescent detection method according to the manufacturer’s recommendations (Dupont-NEN), and subsequent exposure of the membranes to x-ray film.
IL-1ß activity assay
The IL-1-dependent murine thymocyte cell line D10.G4.1 (kindly provided by Dr. Andrew Lichtman, Brigham and Women’s Hospital) was cultured in RPMI 1640 (BioWhittaker, Walkersville, MD) supplemented with 1% L-glutamine, 1% penicillin/streptomycin, 20 µM 2-ME, 25 mM HEPES, and 10% FBS. For detection of IL-1ß activity, D10.G4.1 cells were washed twice (400 x g, 10 min, 4°C), and 50-µl aliquots of the cell suspension (100,000 cells/ml) were plated in 96-well flat-bottom microtiter plates (Falcon, Lincoln Park, NJ). For the assay, 50 µl of the samples were added in the absence or presence of the neutralizing IL-1ß Ab (1 µg/ml; Endogen, Woburn, MA) to triplicate cultures for 72 h. Finally, cells were exposed to tritiated thymidine ([3H]thymidine, 5 µCi/well) during the final 24 h, then harvested on glass fiber filter strips (Cambridge Technology, Watertown, MA), and [3H]thymidine incorporation (dpm per culture ± SD) was analyzed in a liquid scintillation counter (Beckman, Fullerton, CA). The mean of triplicate cultures was determined. For quantification of IL-1ß activity, [3H]thymidine incorporation was calibrated to a standard of recombinant human mIL-1ß (10 fg/ml–10 ng/ml) added to D10.G4.1 indicator cells.
|
Results |
|---|
|
TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
|---|
To explore the capability of matrix metalloproteinases to process
the inactive 33-kDa pIL-1ß, representatives of three classes of MMPs,
interstitial collagenase (MMP-1), stromelysin-1 (MMP-3), and the
gelatinases A (MMP-2) and B (MMP-9), were incubated with pIL-1ß, and
processing was followed by Western blot analysis. Active
stromelysin as well as the gelatinases A and B, but not interstitial
collagenase, processed pIL-1ß (Fig. 1).
However, preincubation of stromelysin-1, gelatinase A, and gelatinase B
with TIMP-1, a specific inhibitor of matrix metalloproteinases, before
coincubation with the cytokine, blocked pIL-1ß processing. The
specificity of the TIMP-1-mediated inhibition was demonstrated in
processing assays employing chymotrypsin or caspase-1. TIMP-1 inhibited
neither chymotrypsin- nor caspase-1-mediated cleavage of pIL-1ß (Fig. 1
).
Processing of the inactive pIL-1ß into biologically active IL-1ß by stromelysin-1 depended on concentration and time
Processing of the inactive pIL-1ß does not necessarily produce
the biologically active cytokine, a property of only certain
C-terminal fragments. The Ab used here for Western blot analysis was
raised against the mature form of IL-1ß, indicating generation of
C-terminal fragments by stromelysin-1, gelatinase A, and gelatinase B.
To determine whether these fragments possess biologic activity,
pIL-1ß was incubated with various concentrations of the respective
MMP for up to 72 h, and the preparations were analyzed by
immunoblotting as well as by an IL-1 activity assay. Incubation of
pIL-1ß with interstitial collagenase did not produce detectable
fragments or IL-1ß activity even after 72 h (Fig. 2, A and C) and use
of up to 10 µg/ml of the enzyme (Fig. 3, A and C). The
pIL-1ß itself showed no autodegradation for the times tested.
Processing of pIL-1ß by stromelysin-1 required at least 1 h of
incubation, as demonstrated by Western blot analysis (Fig. 2B). The processed bands detected had a m.w. of 
28 and 14
kDa. The 28-kDa band was detected before the lower m.w. cleavage
product. The precursor band became fainter after 3 h and
disappeared after 24 h of coincubation, concurrently with the
processed bands. IL-1ß activity was detected after 1 h of
incubation with stromelysin-1 and declined after 24 h, in parallel
with the 14-kDa band detected by immunoblotting. The inhibitory
IL-1ß Ab abrogated this biologic activity. In addition to its
dependence on the amount of time elapsed, processing of pIL-1ß
also depended on the concentration of stromelysin-1. Detection of both
processed bands in Western blot analysis and IL-1ß activity required
the incubation of the precursor with at least 1 µg/ml of
stromelysin-1 (Fig. 3, B and C). In contrast,
interstitial collagenase did not process pIL-1ß in any of the
concentrations tested.
|
|
A) for at least 24 h to
48 h of coincubation (Fig. 5A). In contrast, pIL-1ß
processing by gelatinase B required an 1000-fold lower concentration
of the enzyme (0.1 µg/ml MMP-9; Fig. 4B) and occurred
within minutes (Fig. 5B). Gelatinase B converted the
precursor into a prominent 17-kDa form and a minor 26-kDa band. Studies
in which equal amounts of rMMP-9 (1 µg/ml) were added every 8 h
to the processing assay (for a total time of 24 h, data not shown)
revealed extended cleavage of pIL-1ß into the 17-kDa immunoreactive
form, indicating a limited capacity of the rMMP-9 enzyme employed to
extend processing activity for more than 8 to 12 h. The
concentration dependence of the generation of biologic IL-1ß activity
by gelatinase A and gelatinase B paralleled that of the protein
processing (Fig. 4C).
|
|
In view of the disappearance of the precursor, as well as
processed IL-1ß protein and activity, after several hours of
incubation of the precursor with stromelysin-1, we further explored
whether MMPs can affect the presence and activity of human mature
IL-1ß. Incubation of recombinant mIL-1ß with stromelysin-1, but not
with interstitial collagenase, resulted in degradation of the mature
18-kDa protein in Western blot analysis (Fig. 6, A and B). Almost
no intermediate bands were detected during this degradation.
Corresponding to the Western blot analysis, IL-1ß activity declined
after 1 h of coincubation and disappeared after 3 h to 8 h
of incubation with stromelysin-1. Detection of IL-1ß activity after
coincubation with interstitial collagenase (Fig. 6, A and
C) resembled the kinetics obtained with mIL-1ß alone.
Gelatinase A as well as gelatinase B also demonstrated some mIL-1ß
processing capacity, resulting in 14, 10, and 5 kDa fragments, as
well as a 13-kDa fragment, respectively (Fig. 6, D and
E). However, complete degradation of the cytokine did not
occur even when the enzymes were applied for 72 h or were
repeatedly applied (every 8 h for 24 h) to the processing
assay (data not shown). Neither interstitial collagenase and
stromelysin-1 (Fig. 6C, right) nor gelatinase A and
gelatinase B (Fig. 6F, right) affected the appearance of the
second isoform of IL-1, IL-1.
|
|
Discussion |
|---|
|
TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
|---|
28-kDa fragments obtained with stromelysin-1 and gelatinase B,
have been shown by others to lack substantial activity (3, 6, 7, 8, 9, 10).
Aside from granzyme A-mediated processing (24), the products shown in
this report are the only reported fragments smaller than the products
obtained by caspase-1-mediated conversion. Other proteases such as
trypsin, chymotrypsin, cathepsin G, or elastase process the pIL-1ß
N-terminal of the Asp116-Ala117 site (5, 6, 22, 23). Similar to these proteases, the MMP-generated IL-1ß products
possessed less activity than mature, caspase-derived IL-1ß. However,
production of active IL-1ß by MMPs might occur at sites of local
inflammatory reactions. Recent studies by Fantuzzi et al. (20)
demonstrated that under pathologic conditions displaying inflammatory
aspects, caspase-1-deficient mice can mediate IL-1ß-dependent
reactions. Furthermore, production of biologically active IL-1ß in
these mice occurred at the same level as found in wild-type mice.
Although the mediator of this caspase-1-independent pIL-1ß processing
in the inflammatory model was unknown, the authors postulated a
conversion in the vicinity of the Asp116-Ala117
site and invoked the involvement of leukocyte-derived serin
proteases, such as chymase, elastase, or granzyme A. The induction of
IL-1ß activity in a caspase-1-deficient mice was unexpected, since
these mice have major defects in the production of mIL-1ß, even under
endotoxin activated conditions (18, 19). Conceivably, distinct
pathologic conditions, probably displaying inflammatory aspects and/or
tissue alterations, are required for induction of caspase-1-independent
mechanisms of IL-1ß processing. In addition to participating in normal homeostasis and developmental remodeling of connective tissues, MMPs appear to contribute, by their proteolytic activity, to the tissue damage seen in inflammatory diseases, such as rheumatoid arthritis, osteoarthritis, and atherosclerosis, as well as tumor metastasis (29, 30, 42, 43). Overexpression of interstitial collagenase, stromelysin-1, gelatinase A, and gelatinase B, as well as of cytokines such as IL-1ß, characterizes sites of inflammation (30, 34, 36, 44, 45, 46, 47, 48, 49). Within these diseases, the concentrations of MMPs as well as cytokine correlates with those used in the present study. Between 0.5 and 350 µg/ml MMP-1, MMP-2, MMP-3, and MMP-9 have been detected in the serum or at sites of chronic inflammation such as rheumatoid arthritis or atherosclerosis, describing MMP-3 > MMP-2/-9 >> MMP-1 as the most prominent MMP (50, 51, 52, 53, 54, 55). Furthermore, patients with chronic inflammatory diseases bear 0.1 to 10 ng/ml of IL-1ß in serum, but up to the µg/ml range at the inflammatory site (56, 57, 58). Cells associated with these diseases include fibroblasts and smooth muscle cells. Both cell types express but do not process pIL-1ß, due to the lack of caspase-1 (15, 16) or the expression of a caspase-1 inhibitory activity (41), respectively. Thus, caspase-1-independent activation of pIL-1ß via MMPs may be of major importance in these cell types. Keratinocytes of the human plantar stratum corneum process IL-1ß by a caspase-1-independent pathway. These caspase-1-deficient cells produce IL-1ß activity in the normal epidermis in vivo (21). Keratinocytes, like fibroblasts, can express MMPs (59, 60, 61), particularly at sites of inflammation. The presence of pro-IL-1ß in the cytoplasm and the predominantly extracellular presence of active forms of MMPs does not render irrelevant the findings reported herein. Sites of chronic inflammation are generally characterized by substantial cell turn-over and apoptotic and necrotic cell death. Such processes likely permit interaction between active MMPs and the pIL-1ß. In addition, both activation of MMPs and processing of the pIL-1ß can occur within the cytoplasm, indicating their possible intracellular interaction.
In addition to the generation of IL-1ß activity, the present study also provides evidence for participation of MMPs in IL-1ß degradation. IL-1ß has diverse and potent actions, including the ability to induce its own gene expression (25, 26). Thus, the presence of active IL-1ß might trigger a positive feedback loop, requiring an inhibitory limb to avoid excessive propagation. IL-1ß is one of the classical inducers of MMPs, including interstitial collagenase, stromelysin-1, and the gelatinases A and B, in various cell types (46, 62, 63). The presence of active IL-1ß might thus promote the expression of MMPs, which could govern IL-1ß action by catabolizing the mature cytokine.
In our study, different MMPs expressed different potentials for
processing the IL-1ß protein. Gelatinase B very effectively processed
pIL-1ß, yielding stable products and biologic activity. Stromelysin-1
required higher concentrations and several hours of coincubation to
convert the precursor, but was the only MMP tested that was capable of
completely degrading biologically active forms of IL-1ß. The present
data suggest operation of a novel pathway of IL-1ß regulation,
independent of caspase-1. We propose (Fig. 7) that at sites of acute and chronic
inflammation, the presence of MMP-9 yields biologic IL-1ß activity,
whereas MMP-3 can degrade the active form of the mediator, leading to
its inactivation. These alternative routes of IL-1ß activation and
catabolism illustrate 1) the redundancy of regulation of the biologic
effects of this multipotent cytokine, 2) the importance of inhibitory
as well as stimulatory control, and 3) that therapeutic strategies
targeting caspase-1 or MMPs must take these complexities into
consideration.
|
|
Acknowledgments |
|---|
|
Footnotes |
|---|
2 Address correspondence and reprint requests to Dr. Peter Libby, Vascular Medicine and Atherosclerosis Unit, Cardiovascular Division, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, 221 Longwood Avenue, LMRC 307, Boston, MA 02115. E-mail address:
3 Abbreviations used in this paper: mIL-1ß, recombinant mature human IL-1ß (18 kDa); MMP, matrix metalloproteinase; pIL-1ß, recombinant human IL-1ß precursor (33 kDa); APMA, p-aminophenylmercuric acetate; TIMP-1, tissue inhibitor of matrix metalloproteinases 1.
Received for publication November 25, 1997. Accepted for publication June 1, 1998.
|
References |
|---|
|
TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
|---|
and 1ß. Proc. Natl. Acad. Sci. USA 84:4572.. J. Immunol. 147:2964.[Abstract]
and IL-1ß by arterial cells in atherosclerosis. Am. J. Pathol. 138:951.[Abstract]
and IL-1ß selectively induce expression of 92-kDa gelatinase by human macrophages. J. Immunol. 157:4159.[Abstract]
This article has been cited by other articles:
|
|
 |
|
  K. L. Hailey, S. Li, M. D. Andersen, M. Roy, V. L. Woods Jr, and P. A. Jennings Pro-interleukin (IL)-1{beta} Shares a Core Region of Stability as Compared with Mature IL-1{beta} While Maintaining a Distinctly Different Configurational Landscape: A COMPARATIVE HYDROGEN/DEUTERIUM EXCHANGE MASS SPECTROMETRY STUDY J. Biol. Chem., September 18, 2009; 284(38): 26137 - 26148. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Page, J. R. Ledford, P. Zhou, and M. Wills-Karp A TLR2 Agonist in German Cockroach Frass Activates MMP-9 Release and Is Protective against Allergic Inflammation in Mice J. Immunol., September 1, 2009; 183(5): 3400 - 3408. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. J. Heilpern, W. Wertheim, J. He, G. Perides, R. T. Bronson, and L. T. Hu Matrix Metalloproteinase 9 Plays a Key Role in Lyme Arthritis but Not in Dissemination of Borrelia burgdorferi Infect. Immun., July 1, 2009; 77(7): 2643 - 2649. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Chotikavanich, C. S. de Paiva, D. Q. Li, J. J. Chen, F. Bian, W. J. Farley, and S. C. Pflugfelder Production and Activity of Matrix Metalloproteinase-9 on the Ocular Surface Increase in Dysfunctional Tear Syndrome Invest. Ophthalmol. Vis. Sci., July 1, 2009; 50(7): 3203 - 3209. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Kanayama, D. Kurotaki, J. Morimoto, T. Asano, Y. Matsui, Y. Nakayama, Y. Saito, K. Ito, C. Kimura, N. Iwasaki, et al. {alpha}9 Integrin and Its Ligands Constitute Critical Joint Microenvironments for Development of Autoimmune Arthritis J. Immunol., June 15, 2009; 182(12): 8015 - 8025. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Beeghly-Fadiel, W. Lu, J.-R. Long, X.-o. Shu, Y. Zheng, Q. Cai, Y.-T. Gao, and W. Zheng Matrix Metalloproteinase-2 Polymorphisms and Breast Cancer Susceptibility Cancer Epidemiol. Biomarkers Prev., June 1, 2009; 18(6): 1770 - 1776. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 I. Vanlaere and C. Libert Matrix Metalloproteinases as Drug Targets in Infections Caused by Gram-Negative Bacteria and in Septic Shock Clin. Microbiol. Rev., April 1, 2009; 22(2): 224 - 239. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. MacLauchlan, E. A. Skokos, N. Meznarich, D. H. Zhu, S. Raoof, J. M. Shipley, R. M. Senior, P. Bornstein, and T. R. Kyriakides Macrophage fusion, giant cell formation, and the foreign body response require matrix metalloproteinase 9 J. Leukoc. Biol., April 1, 2009; 85(4): 617 - 626. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. M. Manicone, T. P. Birkland, M. Lin, T. Betsuyaku, N. van Rooijen, J. Lohi, J. Keski-Oja, Y. Wang, S. J. Skerrett, and W. C. Parks Epilysin (MMP-28) Restrains Early Macrophage Recruitment in Pseudomonas aeruginosa Pneumonia J. Immunol., March 15, 2009; 182(6): 3866 - 3876. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. Sheen, C. M. O'Kane, K. Chaudhary, M. Tovar, C. Santillan, J. Sosa, L. Caviedes, R. H. Gilman, G. Stamp, and J. S. Friedland High MMP-9 activity characterises pleural tuberculosis correlating with granuloma formation Eur. Respir. J., January 1, 2009; 33(1): 134 - 141. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. E. Lackey, S. L. Ashley, A. L. Davis, and K. A. Hoag Retinoic Acid Decreases Adherence of Murine Myeloid Dendritic Cells and Increases Production of Matrix Metalloproteinase-9 J. Nutr., August 1, 2008; 138(8): 1512 - 1519. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Lin, P. Jackson, A. M. Tester, E. Diaconu, C. M. Overall, J. E. Blalock, and E. Pearlman Matrix Metalloproteinase-8 Facilitates Neutrophil Migration through the Corneal Stromal Matrix by Collagen Degradation and Production of the Chemotactic Peptide Pro-Gly-Pro Am. J. Pathol., July 1, 2008; 173(1): 144 - 153. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Foronjy, T. Nkyimbeng, A. Wallace, J. Thankachen, Y. Okada, V. Lemaitre, and J. D'Armiento Transgenic expression of matrix metalloproteinase-9 causes adult-onset emphysema in mice associated with the loss of alveolar elastin Am J Physiol Lung Cell Mol Physiol, June 1, 2008; 294(6): L1149 - L1157. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Cheung, D. Marchant, E. K.-Y. Walker, Z. Luo, J. Zhang, B. Yanagawa, M. Rahmani, J. Cox, C. Overall, R. M. Senior, et al. Ablation of Matrix Metalloproteinase-9 Increases Severity of Viral Myocarditis in Mice Circulation, March 25, 2008; 117(12): 1574 - 1582. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Charrier-Hisamuddin, C. L. Laboisse, and D. Merlin ADAM-15: a metalloprotease that mediates inflammation FASEB J, March 1, 2008; 22(3): 641 - 653. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. Van Lint and C. Libert Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation J. Leukoc. Biol., December 1, 2007; 82(6): 1375 - 1381. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Sariahmetoglu, B. D. Crawford, H. Leon, J. Sawicka, L. Li, B. J. Ballermann, C. Holmes, L. G. Berthiaume, A. Holt, G. Sawicki, et al. Regulation of matrix metalloproteinase-2 (MMP-2) activity by phosphorylation FASEB J, August 1, 2007; 21(10): 2486 - 2495. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. A. Mosig, O. Dowling, A. DiFeo, M. C. M. Ramirez, I. C. Parker, E. Abe, J. Diouri, A. A. Aqeel, J. D. Wylie, S. A. Oblander, et al. Loss of MMP-2 disrupts skeletal and craniofacial development and results in decreased bone mineralization, joint erosion and defects in osteoblast and osteoclast growth Hum. Mol. Genet., May 1, 2007; 16(9): 1113 - 1123. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Westermann, S. Rutschow, S. Jager, A. Linderer, S. Anker, A. Riad, T. Unger, H.-P. Schultheiss, M. Pauschinger, and C. Tschope Contributions of Inflammation and Cardiac Matrix Metalloproteinase Activity to Cardiac Failure in Diabetic Cardiomyopathy: The Role of Angiotensin Type 1 Receptor Antagonism Diabetes, March 1, 2007; 56(3): 641 - 646. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. Svedin, H. Hagberg, K. Savman, C. Zhu, and C. Mallard Matrix Metalloproteinase-9 Gene Knock-out Protects the Immature Brain after Cerebral Hypoxia-Ischemia J. Neurosci., February 14, 2007; 27(7): 1511 - 1518. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. J. Greenlee, Z. Werb, and F. Kheradmand Matrix Metalloproteinases in Lung: Multiple, Multifarious, and Multifaceted Physiol Rev, January 1, 2007; 87(1): 69 - 98. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Bry, J. A. Whitsett, and U. Lappalainen IL-1beta Disrupts Postnatal Lung Morphogenesis in the Mouse Am. J. Respir. Cell Mol. Biol., January 1, 2007; 36(1): 32 - 42. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
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]
|
|
|
|
 |
|
 M. A. Birrell, S. Wong, A. Dekkak, J. De Alba, S. Haj-Yahia, and M. G. Belvisi Role of Matrix Metalloproteinases in the Inflammatory Response in Human Airway Cell-Based Assays and in Rodent Models of Airway Disease J. Pharmacol. Exp. Ther., August 1, 2006; 318(2): 741 - 750. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J.-o Deguchi, M. Aikawa, C.-H. Tung, E. Aikawa, D.-E. Kim, V. Ntziachristos, R. Weissleder, and P. Libby Inflammation in Atherosclerosis: Visualizing Matrix Metalloproteinase Action in Macrophages In Vivo Circulation, July 4, 2006; 114(1): 55 - 62. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Khandoga, J. S. Kessler, M. Hanschen, A. G. Khandoga, D. Burggraf, C. Reichel, G. F. Hamann, G. Enders, and F. Krombach Matrix metalloproteinase-9 promotes neutrophil and T cell recruitment and migration in the postischemic liver J. Leukoc. Biol., June 1, 2006; 79(6): 1295 - 1305. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Hu and L. B. Ivashkiv Costimulation of Chemokine Receptor Signaling by Matrix Metalloproteinase-9 Mediates Enhanced Migration of IFN-{alpha} Dendritic Cells J. Immunol., May 15, 2006; 176(10): 6022 - 6033. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Tedgui and Z. Mallat Cytokines in Atherosclerosis: Pathogenic and Regulatory Pathways Physiol Rev, April 1, 2006; 86(2): 515 - 581. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. C. Frake, H. E. Smith, L.-F. Chen, and W. L. Biffl Prestorage Leukoreduction Prevents Accumulation of Matrix Metalloproteinase 9 in Stored Blood Arch Surg, April 1, 2006; 141(4): 396 - 400. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P T G Elkington and J S Friedland Matrix metalloproteinases in destructive pulmonary pathology Thorax, March 1, 2006; 61(3): 259 - 266. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. Dimitriadis, C.A. White, R.L. Jones, and L.A. Salamonsen Cytokines, chemokines and growth factors in endometrium related to implantation Hum. Reprod. Update, November 1, 2005; 11(6): 613 - 630. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. S. Ikonomidis, J. R. Barbour, Z. Amani, R. E. Stroud, A. R. Herron, D. M. McClister Jr, S. E. Camens, M. L. Lindsey, R. Mukherjee, and F. G. Spinale Effects of Deletion of the Matrix Metalloproteinase 9 Gene on Development of Murine Thoracic Aortic Aneurysms Circulation, August 30, 2005; 112(9_suppl): I-242 - I-248. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Garcia-Touchard, T. D. Henry, G. Sangiorgi, L. G. Spagnoli, A. Mauriello, C. Conover, and R. S. Schwartz Extracellular Proteases in Atherosclerosis and Restenosis Arterioscler Thromb Vasc Biol, June 1, 2005; 25(6): 1119 - 1127. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. C. Taggart, C. M. Greene, T. P. Carroll, S. J. O'Neill, and N. G. McElvaney Elastolytic Proteases: Inflammation Resolution and Dysregulation in Chronic Infective Lung Disease Am. J. Respir. Crit. Care Med., May 15, 2005; 171(10): 1070 - 1076. [Full Text] [PDF]
|
|
|
|
|
|
U. Lappalainen, J. A. Whitsett, S. E. Wert, J. W. Tichelaar, and K. Bry Interleukin-1{beta} Causes Pulmonary Inflammation, Emphysema, and Airway Remodeling in the Adult Murine Lung Am. J. Respir. Cell Mol. Biol., April 1, 2005; 32(4): 311 - 318. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Sakamoto, H. Mukae, T. Fujii, H. Ishii, S. Yoshioka, T. Kakugawa, K. Sugiyama, Y. Mizuta, J.-i. Kadota, M. Nakazato, et al. Differential effects of {alpha}- and {beta}-defensin on cytokine production by cultured human bronchial epithelial cells Am J Physiol Lung Cell Mol Physiol, March 1, 2005; 288(3): L508 - L513. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. J. Scotton, F. O. Martinez, M. J. Smelt, M. Sironi, M. Locati, A. Mantovani, and S. Sozzani Transcriptional Profiling Reveals Complex Regulation of the Monocyte IL-1{beta} System by IL-13 J. Immunol., January 15, 2005; 174(2): 834 - 845. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Odaka, M. Tanioka, and T. Itoh Matrix Metalloproteinase-9 in Macrophages Induces Thymic Neovascularization following Thymocyte Apoptosis J. Immunol., January 15, 2005; 174(2): 846 - 853. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. J. Burton, R. L. Bailey, D. Jeffries, D. C. W. Mabey, and M. J. Holland Cytokine and Fibrogenic Gene Expression in the Conjunctivas of Subjects from a Gambian Community Where Trachoma Is Endemic Infect. Immun., December 1, 2004; 72(12): 7352 - 7356. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Luo, D.-Q. Li, A. Doshi, W. Farley, R. M. Corrales, and S. C. Pflugfelder Experimental Dry Eye Stimulates Production of Inflammatory Cytokines and MMP-9 and Activates MAPK Signaling Pathways on the Ocular Surface Invest. Ophthalmol. Vis. Sci., December 1, 2004; 45(12): 4293 - 4301. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Gendron, P. Plamondon, and D. Grenier Binding of Pro-Matrix Metalloproteinase 9 by Fusobacterium nucleatum subsp. nucleatum as a Mechanism To Promote the Invasion of a Reconstituted Basement Membrane Infect. Immun., October 1, 2004; 72(10): 6160 - 6163. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Q. Rao, G.-G. Zheng, G. Li, Y.-M. Lin, and K.-F. Wu Membrane-Bound Macrophage Colony-Stimulating Factor Mediated Auto-Juxtacrine Downregulates Matrix Metalloproteinase-9 Release on J6-1 Leukemic Cell Experimental Biology and Medicine, October 1, 2004; 229(9): 946 - 953. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. J. McCawley, H. C. Crawford, L. E. King Jr., J. Mudgett, and L. M. Matrisian A Protective Role for Matrix Metalloproteinase-3 in Squamous Cell Carcinoma Cancer Res., October 1, 2004; 64(19): 6965 - 6972. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. A.B. Joosten, R. L. Smeets, M. I. Koenders, L. A.M. van den Bersselaar, M. M.A. Helsen, B. Oppers-Walgreen, E. Lubberts, Y. Iwakura, F. A.J. van de Loo, and W. B. van den Berg Interleukin-18 Promotes Joint Inflammation and Induces Interleukin-1-Driven Cartilage Destruction Am. J. Pathol., September 1, 2004; 165(3): 959 - 967. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. E. Stearns, G. Kim, F. Garcia, and M. Wang Interleukin-10 Induced Activating Transcription Factor 3 Transcriptional Suppression of Matrix Metalloproteinase-2 Gene Expression in Human Prostate CPTX-1532 Cells Mol. Cancer Res., July 1, 2004; 2(7): 403 - 416. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K Joronen, R Ala-aho, M-L Majuri, H Alenius, V-M Kahari, and E Vuorio Adenovirus mediated intra-articular expression of collagenase-3 (MMP-13) induces inflammatory arthritis in mice Ann Rheum Dis, June 1, 2004; 63(6): 656 - 664. [Abstract] [Full Text]
|
|
|
|
|
|
J. H. M. van Bilsen, J. P. A. Wagenaar-Hilbers, M. C. J. T. Grosfeld-Stulemeijer, M. J. F. van der Cammen, M. E. A. van Dijk, W. van Eden, and M. H. M. Wauben Matrix Metalloproteinases as Targets for the Immune System during Experimental Arthritis J. Immunol., April 15, 2004; 172(8): 5063 - 5068. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. M. Stuart, F. Pan, X. Yin, Z. Haskova, S. Plambeck, and T. A. Ferguson Effect of Metalloprotease Inhibitors on Corneal Allograft Survival Invest. Ophthalmol. Vis. Sci., April 1, 2004; 45(4): 1169 - 1173. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Conant, C. St. Hillaire, H. Nagase, R. Visse, D. Gary, N. Haughey, C. Anderson, J. Turchan, and A. Nath Matrix Metalloproteinase 1 Interacts with Neuronal Integrins and Stimulates Dephosphorylation of Akt J. Biol. Chem., February 27, 2004; 279(9): 8056 - 8062. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 F. Gilli, A. Bertolotto, A. Sala, F. Hoffmann, M. Capobianco, S. Malucchi, T. Glass, L. Kappos, R. L.P. Lindberg, and D. Leppert Neutralizing antibodies against IFN-{beta} in multiple sclerosis: antagonization of IFN-{beta} mediated suppression of MMPs Brain, February 1, 2004; 127(2): 259 - 268. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Fieber, P. Baumann, R. Vallon, C. Termeer, J. C. Simon, M. Hofmann, P. Angel, P. Herrlich, and J. P. Sleeman Hyaluronan-oligosaccharide-induced transcription of metalloproteases J. Cell Sci., January 15, 2004; 117(2): 359 - 367. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Nonaka, T. Kuwabara, H. Mimuro, A. Kuwae, and S. Imajoh-Ohmi Shigella-induced necrosis and apoptosis of U937 cells and J774 macrophages Microbiology, September 1, 2003; 149(9): 2513 - 2527. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. A. Owen, Z. Hu, B. Barrick, and S. D. Shapiro Inducible Expression of Tissue Inhibitor of Metalloproteinases-Resistant Matrix Metalloproteinase-9 on the Cell Surface of Neutrophils Am. J. Respir. Cell Mol. Biol., September 1, 2003; 29(3): 283 - 294. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. L. Lindsey, J. Yoshioka, C. MacGillivray, S. Muangman, J. Gannon, A. Verghese, M. Aikawa, P. Libby, S. M. Krane, and R. T. Lee Effect of a Cleavage-Resistant Collagen Mutation on Left Ventricular Remodeling Circ. Res., August 8, 2003; 93(3): 238 - 245. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Leonardi, P. Brun, G. Abatangelo, M. Plebani, and A. G. Secchi Tear Levels and Activity of Matrix Metalloproteinase (MMP)-1 and MMP-9 in Vernal Keratoconjunctivitis Invest. Ophthalmol. Vis. Sci., July 1, 2003; 44(7): 3052 - 3058. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 O. R.F. Mook, C. Van Overbeek, E. G. Ackema, F. Van Maldegem, and W. M. Frederiks In Situ Localization of Gelatinolytic Activity in the Extracellular Matrix of Metastases of Colon Cancer in Rat Liver Using Quenched Fluorogenic DQ-gelatin J. Histochem. Cytochem., June 1, 2003; 51(6): 821 - 829. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
I. Nelissen, E. Martens, P. E. Van Den Steen, P. Proost, I. Ronsse, and G. Opdenakker Gelatinase B/matrix metalloproteinase-9 cleaves interferon-{beta} and is a target for immunotherapy Brain, June 1, 2003; 126(6): 1371 - 1381. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Visse and H. Nagase Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases: Structure, Function, and Biochemistry Circ. Res., May 2, 2003; 92(8): 827 - 839. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Chen, D. Li, T. Saldeen, and J. L. Mehta TGF-beta 1 attenuates myocardial ischemia-reperfusion injury via inhibition of upregulation of MMP-1 Am J Physiol Heart Circ Physiol, May 1, 2003; 284(5): H1612 - H1617. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
W. Li, K. Tanaka, Y. Chiba, T. Kimura, K. Morioka, T. Uesaka, A. Ihaya, M. Sasaki, T. Tsuda, and N. Yamada Role of MMPs and plasminogen activators in angiogenesis after transmyocardial laser revascularization in dogs Am J Physiol Heart Circ Physiol, January 1, 2003; 284(1): H23 - H30. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. Roeb, K. Schleinkofer, T. Kernebeck, S. Potsch, B. Jansen, I. Behrmann, S. Matern, and J. Grotzinger The Matrix Metalloproteinase 9 (MMP-9) Hemopexin Domain Is a Novel Gelatin Binding Domain and Acts as an Antagonist J. Biol. Chem., December 20, 2002; 277(52): 50326 - 50332. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. S.-T. Kai, G. S. Butler, C. J. Morrison, A. E. King, G. R. Pelman, and C. M. Overall Utilization of a Novel Recombinant Myoglobin Fusion Protein Expression System to Characterize the Tissue Inhibitor of Metalloproteinase (TIMP)-4 and TIMP-2 C-terminal Domain and Tails by Mutagenesis. THE IMPORTANCE OF ACIDIC RESIDUES IN BINDING THE MMP-2 HEMOPEXIN C DOMAIN J. Biol. Chem., December 6, 2002; 277(50): 48696 - 48707. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. J. Rowe, L. Allen, V. C. Ridger, P. G. Hellewell, and M. K. B. Whyte Caspase-1-Deficient Mice Have Delayed Neutrophil Apoptosis and a Prolonged Inflammatory Response to Lipopolysaccharide-Induced Acute Lung Injury J. Immunol., December 1, 2002; 169(11): 6401 - 6407. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Itoh, H. Matsuda, M. Tanioka, K. Kuwabara, S. Itohara, and R. Suzuki The Role of Matrix Metalloproteinase-2 and Matrix Metalloproteinase-9 in Antibody-Induced Arthritis J. Immunol., September 1, 2002; 169(5): 2643 - 2647. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Sartor, E. Pezzato, and S. Garbisa (-)Epigallocatechin-3-gallate inhibits leukocyte elastase: potential of the phyto-factor in hindering inflammation, emphysema, and invasion J. Leukoc. Biol., January 1, 2002; 71(1): 73 - 79. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Sugawara, A. Uehara, T. Nochi, T. Yamaguchi, H. Ueda, A. Sugiyama, K. Hanzawa, K. Kumagai, H. Okamura, and H. Takada Neutrophil Proteinase 3-Mediated Induction of Bioactive IL-18 Secretion by Human Oral Epithelial Cells J. Immunol., December 1, 2001; 167(11): 6568 - 6575. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z. Ma, H. Qin, and E. N. Benveniste Transcriptional Suppression of Matrix Metalloproteinase-9 Gene Expression by IFN-{gamma} and IFN-{beta}: Critical Role of STAT-1{alpha} J. Immunol., November 1, 2001; 167(9): 5150 - 5159. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B Isaksen and M K Fagerhol Calprotectin inhibits matrix metalloproteinases by sequestration of zinc Mol. Pathol., October 1, 2001; 54(5): 289 - 292. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Mack, K. Jungermann, O. Gotze, and H. L. Schieferdecker Anaphylatoxin C5a Actions in Rat Liver: Synergistic Enhancement by C5a of Lipopolysaccharide-Dependent {alpha}2-Macroglobulin Gene Expression in Hepatocytes Via IL-6 Release from Kupffer Cells J. Immunol., October 1, 2001; 167(7): 3972 - 3979. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Solomon, D. Dursun, Z. Liu, Y. Xie, A. Macri, and S. C. Pflugfelder Pro- and Anti-inflammatory Forms of Interleukin-1 in the Tear Fluid and Conjunctiva of Patients with Dry-Eye Disease Invest. Ophthalmol. Vis. Sci., September 1, 2001; 42(10): 2283 - 2292. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
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]
|
|
|
|
|
|
B. O. Evert, I. R. Vogt, C. Kindermann, L. Ozimek, R. A. I. de Vos, E. R. P. Brunt, I. Schmitt, T. Klockgether, and U. Wullner Inflammatory Genes Are Upregulated in Expanded Ataxin-3-Expressing Cell Lines and Spinocerebellar Ataxia Type 3 Brains J. Neurosci., August 1, 2001; 21(15): 5389 - 5396. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Opdenakker, P. E. Van den Steen, B. Dubois, I. Nelissen, E. Van Coillie, S. Masure, P. Proost, and J. Van Damme Gelatinase B functions as regulator and effector in leukocyte biology J. Leukoc. Biol., June 1, 2001; 69(6): 851 - 859. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Lindsey, K. Wedin, M. D. Brown, C. Keller, A. J. Evans, J. Smolen, A. R. Burns, R. D. Rossen, L. Michael, and M. Entman Matrix-Dependent Mechanism of Neutrophil-Mediated Release and Activation of Matrix Metalloproteinase 9 in Myocardial Ischemia/Reperfusion Circulation, May 1, 2001; 103(17): 2181 - 2187. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Boulday, S. Coupel, F. Coulon, J.-P. Soulillou, and B. Charreau Antigraft Antibody-Mediated Expression of Metalloproteinases on Endothelial Cells : Differential Expression of TIMP-1 and ADAM-10 Depends on Antibody Specificity and Isotype Circ. Res., March 2, 2001; 88(4): 430 - 437. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. E. Van den Steen, P. Proost, A. Wuyts, J. Van Damme, and G. Opdenakker Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact Blood, October 15, 2000; 96(8): 2673 - 2681. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. H. Vu and Z. Werb Matrix metalloproteinases: effectors of development and normal physiology Genes & Dev., September 1, 2000; 14(17): 2123 - 2133. [Full Text]
|
|
|
|
|
|
A. Solomon, M. Rosenblatt, D.-Q. Li, Z. Liu, D. Monroy, Z. Ji, B. L. Lokeshwar, and S. C. Pflugfelder Doxycycline Inhibition of Interleukin-1 in the Corneal Epithelium Invest. Ophthalmol. Vis. Sci., August 1, 2000; 41(9): 2544 - 2557. [Abstract] [Full Text]
|
|
|
|
|
|
M. Kawasaki, K. Kuwano, N. Hagimoto, T. Matsuba, R. Kunitake, T. Tanaka, T. Maeyama, and N. Hara Protection from Lethal Apoptosis in Lipopolysaccharide-Induced Acute Lung Injury in Mice by a Caspase Inhibitor Am. J. Pathol., August 1, 2000; 157(2): 597 - 603. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Pagenstecher, A. K. Stalder, C. L. Kincaid, B. Volk, and I. L. Campbell Regulation of Matrix Metalloproteinases and Their Inhibitor Genes in Lipopolysaccharide-Induced Endotoxemia in Mice Am. J. Pathol., July 1, 2000; 157(1): 197 - 210. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Gardella, C. Andrei, S. Costigliolo, L. Olcese, M. R. Zocchi, and A. Rubartelli Secretion of bioactive interleukin-1beta by dendritic cells is modulated by interaction with antigen specific T cells Blood, June 15, 2000; 95(12): 3809 - 3815. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Sobrin, Z. Liu, D. C. Monroy, A. Solomon, M. G. Selzer, B. L. Lokeshwar, and S. C. Pflugfelder Regulation of MMP-9 Activity in Human Tear Fluid and Corneal Epithelial Culture Supernatant Invest. Ophthalmol. Vis. Sci., June 1, 2000; 41(7): 1703 - 1709. [Abstract] [Full Text]
|
|
|
|
 |
|
 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]
|
|
|
|
 |
|
 M. P. Pereda, M. F. Ledda, V. Goldberg, A. Chervín, G. Carrizo, H. Molina, A. Müller, U. Renner, O. Podhajcer, E. Arzt, et al. High Levels of Matrix Metalloproteinases Regulate Proliferation and Hormone Secretion in Pituitary Cells J. Clin. Endocrinol. Metab., January 1, 2000; 85(1): 263 - 269. [Abstract] [Full Text]
|
|
|
|
 |
|
 C.-R. Roh, W.-J. Oh, B.-K. Yoon, and J.-H. Lee Up-regulation of matrix metalloproteinase-9 in human myometrium during labour: a cytokine-mediated process in uterine smooth muscle cells Mol. Hum. Reprod., January 1, 2000; 6(1): 96 - 102. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Zhang, A. L. Hampton, G. Nie, and L. A. Salamonsen Progesterone Inhibits Activation of Latent Matrix Metalloproteinase (MMP)-2 by Membrane-Type 1 MMP: Enzymes Coordinately Expressed in Human Endometrium Biol Reprod, January 1, 2000; 62(1): 85 - 94. [Abstract] [Full Text]
|
|
|
|
 |
|
 C. Coeshott, C. Ohnemus, A. Pilyavskaya, S. Ross, M. Wieczorek, H. Kroona, A. H. Leimer, and J. Cheronis Converting enzyme-independent release of tumor necrosis factor alpha and IL-1beta from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3 PNAS, May 25, 1999; 96(11): 6261 - 6266. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Mohan, S. K. Chintala, J. C. Jung, W. V. L. Villar, F. McCabe, L. A. Russo, Y. Lee, B. E. McCarthy, K. R. Wollenberg, J. V. Jester, et al. Matrix Metalloproteinase Gelatinase B (MMP-9) Coordinates and Effects Epithelial Regeneration J. Biol. Chem., January 11, 2002; 277(3): 2065 - 2072. [Abstract] [Full Text] [PDF]
|
|
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
