INT106468

Context Info Confidence 0.50 First Reported 2002 Last Reported 2011 Negated 2 Speculated 1 Reported most in Body Documents 11 Total Number 12 Disease Relevance 3.53 Pain Relevance 2.77

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

Anatomy Link Frequency endothelial cells 4 fibroblasts 4 nucleus pulposus 4 arms 2 MMP2 (Homo sapiens)

Pain Link Frequency Relevance Heat metalloproteinase 348 100.00 IPN 4 98.76 Inflammation 60 97.60 backache 4 89.12 Osteoarthritis 1 84.96 chemokine 8 84.36 COX-2 inhibitor 19 75.88 Arthritis 17 67.72 Pain 7 66.32 cytokine 24 32.80

Disease Link Frequency Relevance Heat Cancer 120 99.12 Arthritis 18 98.08 Intervertebral Disk Degeneration 4 97.96 Adhesions 35 96.56 Prostate Cancer 90 92.08 Low Back Pain 4 89.12 Reprotox - General 1 4 88.24 Metastasis 59 87.92 Adenoma 36 85.60 Colorectal Cancer 16 84.00

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Key:

Protein

Mutation

Event

Anatomy

Negation

Speculation

Pain term

Disease term

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 Gene_expression (expressions) of MMP-2

1) Confidence 0.50 Published 2007 Journal Bioorg. Med. Chem. Section Abstract Doc Link 17498959 Disease Relevance 0.45 Pain Relevance 0.22

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 Gene_expression (produced) of MMP-2 in nucleus pulposus

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

Ciprofloxacin also potentiated IL-1beta-stimulated MMP-1 mRNA expression, but did not potentiate the output of MMP-1, and had no significant effects on MMP-2 mRNA expression or output.

Neg (no) Regulation (effects) of Gene_expression (expression) of MMP-2 mRNA

3) Confidence 0.46 Published 2002 Journal Arthritis Rheum. Section Body Doc Link 12428247 Disease Relevance 0 Pain Relevance 0

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 Gene_expression (produced) of gelatinase-A in nucleus pulposus

4) Confidence 0.44 Published 2003 Journal Eur Spine J Section Abstract Doc Link 12592549 Disease Relevance 0.35 Pain Relevance 0.26

Kim et al. report the inhibitory effect of chitooligosaccharides (COS) on activation and expression of matrix metalloproteinase-2 (MMP-2) in primary human dermal fibroblasts (HDFs) for the first time.

Regulation (effect) of Gene_expression (expression) of MMP-2 in fibroblasts associated with metalloproteinase

5) Confidence 0.30 Published 2009 Journal Marine Drugs Section Body Doc Link PMC2707034 Disease Relevance 0 Pain Relevance 0.08

Wang et al. isolated the sulfated S. maindroni ink polysaccharide (SIP-SII) from cuttlefish Sepiella maindroni, and examined the effects of SIP-SII on the expression of matrix metalloproteinases MMP-2 and MMP-9 as well as tumor cell invasion and migration.

Spec (examined) Regulation (effects) of Gene_expression (expression) of MMP-2 associated with cancer and metalloproteinase

6) Confidence 0.30 Published 2009 Journal Marine Drugs Section Body Doc Link PMC2707034 Disease Relevance 0.30 Pain Relevance 0.10

Kim et al. report the inhibitory effect of chitooligosaccharides (COS) on activation and expression of matrix metalloproteinase-2 (MMP-2) in primary human dermal fibroblasts (HDFs) for the first time.

Regulation (effect) of Gene_expression (expression) of matrix metalloproteinase-2 in fibroblasts associated with metalloproteinase

7) Confidence 0.30 Published 2009 Journal Marine Drugs Section Body Doc Link PMC2707034 Disease Relevance 0 Pain Relevance 0.08

g/mL), through down-regulation of intracellular matrix metalloproteinases (MMP-2) expression on endothelial cells. [30].

Regulation (regulation) of Gene_expression (expression) of MMP-2 in endothelial cells associated with metalloproteinase

8) Confidence 0.26 Published 2009 Journal Marine Drugs Section Body Doc Link PMC2707034 Disease Relevance 0.28 Pain Relevance 0.09

The results also reveal that MMP-2/-9 protein and gene expression is influenced by the presence of gelatin and not the ligands immobilized on the PEG arms of the IPN.

Regulation (influenced) of Gene_expression (expression) of MMP-2 in arms associated with ipn

9) Confidence 0.22 Published 2007 Journal Biomaterials Section Abstract Doc Link 16979234 Disease Relevance 0.23 Pain Relevance 0.41

In addition, CCL23 confers angiogenic properties [21], mediated through up-regulation of MMP2 gene expression in endothelial cells [22].

Regulation (regulation) of Gene_expression (expression) of MMP2 in endothelial cells

10) Confidence 0.22 Published 2011 Journal PLoS ONE Section Body Doc Link PMC3017541 Disease Relevance 0.83 Pain Relevance 0.14

We observed a significant 2 log-fold and 4 log-fold decline in MMP-2 and MMP-3 expression levels when the cells were treated with 10 ?

Regulation (decline) of Gene_expression (expression) of MMP-2 associated with metalloproteinase

11) Confidence 0.10 Published 2006 Journal BMC Cancer Section Body Doc Link PMC1559713 Disease Relevance 0.11 Pain Relevance 0.73

There was no significant difference in MMP-2 expression between cancerous and normal tissues; however, there was a significant difference in the ratios of MMP-2 and MMP-9 to the tissue inhibitor of metalloproteinases 1 (TIMP-1), with cancerous tissue having a higher ratio.

Neg (no) Regulation (difference) of Gene_expression (expression) of MMP-2 associated with metalloproteinase

12) Confidence 0.06 Published 2004 Journal Reprod Biol Endocrinol Section Body Doc Link PMC320496 Disease Relevance 0.64 Pain Relevance 0.40

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