INT130005

Context Info Confidence 0.36 First Reported 2003 Last Reported 2007 Negated 0 Speculated 0 Reported most in Body Documents 4 Total Number 4 Disease Relevance 3.02 Pain Relevance 0.95

peptidase activity (MMP13) extracellular space (MMP13) extracellular region (MMP13) Golgi apparatus (MMP13) proteinaceous extracellular matrix (MMP13) lysosome (MMP13)

Anatomy Link Frequency cartilage 2 joint 1 nociceptor 1 MMP13 (Homo sapiens)

Pain Link Frequency Relevance Heat metalloproteinase 64 100.00 Osteoarthritis 180 99.32 nociceptor 1 99.04 Inflammatory response 1 97.44 licofelone 45 50.00 Arthritis 10 26.24 cINOD 17 15.04 Inflammation 20 5.00 rheumatoid arthritis 15 5.00 cytokine 7 5.00

Disease Link Frequency Relevance Heat Osteoarthritis 182 99.32 Cramps 1 98.24 Urological Neuroanatomy 1 97.92 INFLAMMATION 24 97.24 Calcification 8 95.64 Phenylketonuria 8 92.60 Hypertrophy 4 86.84 Arthritis 24 86.60 Disease 25 84.56 Arthropathy 6 83.36

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Key:

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Mutation

Event

Anatomy

Negation

Speculation

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Disease term

Four are involved in defense and inflammatory responses of neutrophils (NE, MPO, NGP, and CRAMP), three other overexpressed genes are related to extracellular matrix organization and degradation (COL1A1, COL1A2, and MMP13); the remainder were a nociceptor in sensory neurons (MrgA1), a structural gene of P lysozyme (Lzp-s), an immunoglobulin alpha heavy chain constant region gene (Igh-2), an osteocalcin-related protein precursor (Bglap-rs1), and a membrane-spanning 4 domain, subfamily A, member 3 (Ms4a3).

Protein_catabolism (degradation) of MMP13 in nociceptor associated with cramps, inflammatory response, nociceptor and urological neuroanatomy

1) Confidence 0.36 Published 2005 Journal Mol. Genet. Metab. Section Abstract Doc Link 16150627 Disease Relevance 1.14 Pain Relevance 0.15

Furthermore, degradation of the matrix by catabolic factors such as MMP-13 make the cartilage susceptible to further mechanical erosion.

Protein_catabolism (degradation) of MMP-13 in cartilage

2) Confidence 0.26 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC1860072 Disease Relevance 0.85 Pain Relevance 0.27

Fibrillar collagen is resistant to proteolytic degradation but at neutral pH is susceptible to degradation from the collagenases MMP-1, MMP-8 and MMP-13 that are all found within the joint.

Protein_catabolism (degradation) of MMP-13 in joint

3) Confidence 0.25 Published 2003 Journal Arthritis Res Ther Section Body Doc Link PMC154424 Disease Relevance 0.25 Pain Relevance 0.04

Comprehensive investigation has indicated that the MMPs, including MMP-13, aggrecanase-1 (a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS-4), and aggrecanase-2 (ADAMTS-5), are the proteolytic enzymes that seem the most likely to be involved in the degradation of aggrecans in osteoarthritis cartilage (Lark et al 1997; Chambers et al 2001).

Protein_catabolism (degradation) of MMP-13 in cartilage associated with metalloproteinase and osteoarthritis

4) Confidence 0.07 Published 2007 Journal Clinical Interventions in Aging Section Body Doc Link PMC2684079 Disease Relevance 0.77 Pain Relevance 0.49

General Comments

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