INT108628

Context Info Confidence 0.60 First Reported 2003 Last Reported 2011 Negated 2 Speculated 1 Reported most in Body Documents 27 Total Number 29 Disease Relevance 14.85 Pain Relevance 6.06

peptidase activity (MMP2) extracellular space (MMP2) extracellular region (MMP2) proteinaceous extracellular matrix (MMP2) plasma membrane (MMP2) nucleus (MMP2)

Anatomy Link Frequency extracellular matrix 3 HDFs 2 nucleus pulposus 2 chorion 1 amnion 1 MMP2 (Homo sapiens)

Pain Link Frequency Relevance Heat metalloproteinase 613 100.00 cytokine 152 100.00 rheumatoid arthritis 48 99.52 COX-2 inhibitor 24 99.38 Arthritis 45 99.18 Inflammation 210 98.82 Pain 27 98.48 Nicotine 86 95.52 agonist 4 92.64 Kinase C 5 92.60

Disease Link Frequency Relevance Heat Prostate Cancer 89 99.68 Rheumatoid Arthritis 48 99.52 Cancer 346 99.46 Fibrosarcoma 19 99.20 Arthritis 61 99.18 Transitional Cell Carcinoma 78 99.04 INFLAMMATION 248 98.82 Arthralgia 5 98.48 Intervertebral Disk Degeneration 4 97.96 Infection 125 94.76

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Protein

Mutation

Event

Anatomy

Negation

Speculation

Pain term

Disease term

The aim of the present study was to evaluate the regulation of MMP-2 (gelatinase-A) and MMP-3 (stromelysin) produced by cultured ovine nucleus pulposus (NP) cells stimulated with interleukin-1beta (IL-1beta).

Regulation (regulation) of gelatinase-A in nucleus pulposus

1) Confidence 0.60 Published 2003 Journal Eur Spine J Section Abstract Doc Link 12592549 Disease Relevance 0.35 Pain Relevance 0.26

Activated MMP1, MMP3 and latent forms of MMP2 and MMP9 are regulated and inhibited by endogenous proteins known as tissue inhibitors of metalloproteinase TIMP1 and TIMP2 [17].

Regulation (regulated) of MMP2 associated with metalloproteinase

2) Confidence 0.58 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.83 Pain Relevance 0.23

In the present study, sulfated glucosamine (SGlc) that has been reported to relieve joint pain and inflammation in many arthritis patients was studied for its inhibitory effects on MMP-2 and MMP-9 in human fibrosarcoma cells.

Regulation (effects) of MMP-2 in joint associated with pain, fibrosarcoma, arthralgia, inflammation and arthritis

3) Confidence 0.50 Published 2007 Journal Bioorg. Med. Chem. Section Abstract Doc Link 17498959 Disease Relevance 0.47 Pain Relevance 0.20

The aim of the present study was to evaluate the regulation of MMP-2 (gelatinase-A) and MMP-3 (stromelysin) produced by cultured ovine nucleus pulposus (NP) cells stimulated with interleukin-1beta (IL-1beta).

Regulation (regulation) of MMP-2 in nucleus pulposus

4) Confidence 0.48 Published 2003 Journal Eur Spine J Section Abstract Doc Link 12592549 Disease Relevance 0.35 Pain Relevance 0.26

Comparing our data on different MMPs MMP2 was proved to be the best marker alone.

Regulation (different) of MMP2 associated with metalloproteinase

5) Confidence 0.42 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.61 Pain Relevance 0.18

Moreover, down-regulation of NF-kappaB resulted in production of low levels of both NF-kappaB p50 and p65 proteins and directly affected activation process of MMP-2 and MMP-9 expressions.

Regulation (affected) of MMP-2

6) Confidence 0.37 Published 2007 Journal Bioorg. Med. Chem. Section Abstract Doc Link 17498959 Disease Relevance 0.44 Pain Relevance 0.22

These include paracellular permeability (down-regulation of OCLN) [54], degradation of extracellular matrix (up-regulation of TIMP and MMP2) [55,56] and barrier protection against bacterial invasion of the epithelial surface (up-regulation of MUC1) [57].

Regulation (regulation) of MMP2 in extracellular matrix

7) Confidence 0.34 Published 2005 Journal PLoS Medicine Section Body Doc Link PMC1188246 Disease Relevance 1.36 Pain Relevance 0.05

Niranjan et al. studied for SG inhibitory effects on MMP-2 and MMP-9 in human fibrosarcoma cells.

Regulation (effects) of MMP-2 associated with fibrosarcoma

8) Confidence 0.30 Published 2009 Journal Marine Drugs Section Body Doc Link PMC2707034 Disease Relevance 0.56 Pain Relevance 0.24

COS with 3–5 kDa exhibited the highest inhibitory effect on MMP-2 activity in HDFs, and protein expression of MMP-2 was also inhibited by COS with same molecular weight.

Regulation (effect) of MMP-2 in HDFs

9) Confidence 0.30 Published 2009 Journal Marine Drugs Section Body Doc Link PMC2707034 Disease Relevance 0 Pain Relevance 0.05

In this study the concentrations of MMP1, MMP2, MMP3, MMP9, their inhibitors TIMP1, TIMP2, and the MMP1/TIMP1-complex (MTC1) were quantified in blood plasma with the sandwich enzyme-linked immunosorbent assay (ELISA).

Regulation (concentrations) of MMP2 in blood

10) Confidence 0.25 Published 2006 Journal BMC Urol Section Abstract Doc Link PMC1560390 Disease Relevance 0.44 Pain Relevance 0.13

Higher active-MMP-2 levels even upon COX-2 inhibitor treatment suggest that either MMP-2 might be controlled by factors other than COX-2/PGE2 or the inhibitor dose was insufficient to regulate its secretion.

Spec (might) Regulation (controlled) of MMP-2 associated with metalloproteinase and cox-2 inhibitor

11) Confidence 0.24 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 0.95 Pain Relevance 0.63

In this study we assessed labour-associated changes in gelatinase activity in cultured human amnion, chorion and decidua, as well as in amniotic fluid.

Regulation (changes) of gelatinase in amnion

12) Confidence 0.23 Published 2003 Journal Mol. Hum. Reprod. Section Abstract Doc Link 12771238 Disease Relevance 0.24 Pain Relevance 0.27

First, we tested the effects of both fruit powders on the activities of the enzymes hyaluronidase and collagenase type 2.

Regulation (effects) of collagenase type 2

13) Confidence 0.23 Published 2008 Journal Evidence-based Complementary and Alternative Medicine : eCAM Section Abstract Doc Link PMC2529383 Disease Relevance 0.25 Pain Relevance 0.13

Therefore, in the first assay, we tested effects of P. emblica fruit powder on the gelatinase activity of pure collagenase type 2.

Regulation (effects) of gelatinase

14) Confidence 0.20 Published 2008 Journal Evidence-based Complementary and Alternative Medicine : eCAM Section Body Doc Link PMC2529383 Disease Relevance 0.50 Pain Relevance 0.19

In contrast to the small differences in maximal inhibition by progrado on MMP-2 and MMP-9 activity, within the dose range examined in this protocol, MMP-2 activity appeared to be more sensitive to inhibition by progrado at concentrations below 4 ?

Regulation (sensitive) of MMP-2

15) Confidence 0.19 Published 2007 Journal J Inflamm (Lond) Section Body Doc Link PMC1971260 Disease Relevance 0.24 Pain Relevance 0.08

HT-1080 cells, which express MMP-14 and MMP-2, were used to assess the effect on MMP-2 activity by the selective inhibition of endogenous MMP-14 by DX-2400.

Regulation (effect) of MMP-2 in HT-1080

16) Confidence 0.12 Published 2011 Journal Biochemistry Research International Section Body Doc Link PMC2989751 Disease Relevance 0.56 Pain Relevance 0.16

As per their investigations, CM-chitin exhibited a higher MMP inhibitory, (MMP-2 and MMP-9) effect than CM-chitosan through transcriptional downregulations of activator protein-1 (AP-1) and nuclear factor ?

Regulation (effect) of MMP-2

17) Confidence 0.12 Published 2010 Journal Biochemistry Research International Section Body Doc Link PMC3004377 Disease Relevance 0.18 Pain Relevance 0.11

/CXCL1, and ENA-78/CXCL5, suggesting a novel mechanism of MMP-2 regulation by EGCG in RA synovial fibroblasts [37].

Regulation (regulation) of MMP-2 in fibroblasts associated with rheumatoid arthritis

18) Confidence 0.09 Published 2010 Journal Arthritis Res Ther Section Body Doc Link PMC2888220 Disease Relevance 0.46 Pain Relevance 0.52

The 26 genes that were significantly dysregulated (23 up-regulated and three down-regulated) in the group B samples mainly encoded proteins involved in immune response (interferon pathway, growth factor, growth factor receptor, cytokine: IL8, CXCR4, CCL2, CXCL1, IL6, CCL3, CCL4, LIF) and matrix remodeling (angiogenesis, extracellular matrix, extracellular matrix protease, inhibitors of matrix protease: PAI1, THBS1, PTGS2, HIF1A, MMP9, CTGF, HAS2, PAI2, and MMP2).

Regulation (dysregulated) of MMP2 in extracellular matrix associated with cytokine

19) Confidence 0.08 Published 2008 Journal Hepatology (Baltimore, Md.) Section Body Doc Link PMC2816363 Disease Relevance 1.08 Pain Relevance 0.17

In this study we assessed labour-associated changes in gelatinase activity in cultured human amnion, chorion and decidua, as well as in amniotic fluid.

Regulation (changes) of gelatinase in chorion

20) Confidence 0.08 Published 2003 Journal Mol. Hum. Reprod. Section Abstract Doc Link 12771238 Disease Relevance 0.24 Pain Relevance 0.27

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