INT118097

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Context Info
Confidence 0.70
First Reported 2004
Last Reported 2010
Negated 1
Speculated 1
Reported most in Body
Documents 18
Total Number 19
Disease Relevance 9.99
Pain Relevance 1.42

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

extracellular space (COMP) extracellular region (COMP) cell adhesion (COMP)
proteinaceous extracellular matrix (COMP)
Anatomy Link Frequency
cartilage 5
chondrocytes 3
growth plate 2
joints 1
COMP (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 14 97.56 Very High Very High Very High
Osteoarthritis 85 96.96 Very High Very High Very High
Pain 23 95.16 Very High Very High Very High
Arthritis 58 94.16 High High
psoriasis 19 93.20 High High
cytokine 2 89.48 High High
rheumatoid arthritis 53 64.64 Quite High
imagery 13 52.80 Quite High
metalloproteinase 2 50.72 Quite High
Lasting pain 8 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Osteochondrodysplasias 280 100.00 Very High Very High Very High
Disease 141 99.92 Very High Very High Very High
Stress 104 99.58 Very High Very High Very High
Death 47 99.44 Very High Very High Very High
Chondrosarcoma 96 98.90 Very High Very High Very High
Cleidocranial Dysplasia 32 98.64 Very High Very High Very High
INFLAMMATION 12 97.56 Very High Very High Very High
Osteoarthritis 87 96.96 Very High Very High Very High
Rheumatic Diseases 7 96.12 Very High Very High Very High
Growth Problems 15 95.88 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Additionally, CRT and MT-COMP co-localize to the ER, demonstrating intracellular retention (Fig. 3H).
Localization (localize) of MT-COMP
1) Confidence 0.70 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858657 Disease Relevance 0.64 Pain Relevance 0
Alternatively, increased ER stress (CRT levels) and co-localization of CRT and COMP were greatly diminished in cells overexpressing MT-COMP in the presence of shRNA 3B (Fig. 3I–L).
Localization (localization) of COMP associated with stress
2) Confidence 0.70 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858657 Disease Relevance 0.71 Pain Relevance 0
shRNA 3B is effective in reducing intracellular retention of MT-COMP and other ECM proteins
Localization (retention) of MT-COMP
3) Confidence 0.70 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858657 Disease Relevance 0.18 Pain Relevance 0
They stimulate chondrocytes to release destructive proteases which lead to loss of proteoglycans, to destruction of collagen bundles and to the release of COMP.13 Despite the presence of previous studies on the utility of ultrasound and serum COMP in many rheumatic diseases, their combined validity, sensitivity and specificity in patients with psoriasis and psoriatic arthritis has not been previously reported.
Localization (release) of COMP in chondrocytes associated with seronegative spondarthritis, psoriasis, rheumatic diseases and arthritis
4) Confidence 0.70 Published 2010 Journal Clin Med Insights Arthritis Musculoskelet Disord Section Body Doc Link PMC2989640 Disease Relevance 1.55 Pain Relevance 0.54
More recently, Hecht et al. [2005] showed that mutant COMP can also dramatically affect the secretion of normal matrilin-3 from PSACH chondrocytes.
Localization (secretion) of PSACH in chondrocytes
5) Confidence 0.68 Published 2005 Journal Human Mutation Section Body Doc Link PMC2726956 Disease Relevance 0.45 Pain Relevance 0
One possible reason for the changes in serum COMP during physical exercise is mobilization of COMP from cartilage or other pressure loaded tissues.
Localization (mobilization) of COMP in cartilage
6) Confidence 0.66 Published 2006 Journal BMC Musculoskelet Disord Section Body Doc Link PMC1712338 Disease Relevance 0.07 Pain Relevance 0.04
One possible reason for the changes in serum COMP during physical exercise is mobilization of COMP from cartilage or other pressure loaded tissues.
Localization (mobilization) of COMP in cartilage
7) Confidence 0.66 Published 2006 Journal BMC Musculoskelet Disord Section Body Doc Link PMC1712338 Disease Relevance 0.07 Pain Relevance 0.04
Moreover, these findings also suggest that surpressing intracellular retention of mutant COMP by reducing COMP expression could be used as a therapeutic approach.
Localization (retention) of mutant COMP
8) Confidence 0.65 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858657 Disease Relevance 0.54 Pain Relevance 0.04
These mutations lead to massive intracellular retention of COMP, chondrocyte death and loss of growth plate chondrocytes that are necessary for linear growth.
Localization (retention) of COMP in growth plate associated with death
9) Confidence 0.65 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2858657 Disease Relevance 0.37 Pain Relevance 0
We also demonstrated in RCS cells that shRNA 3B efficiently reduced intracellular retention of MT-COMP, MATN3 and type IX collagen, thereby preventing the development of intracellular matrix that defines the PSACH and MED/EDM1 cellular phenotype.
Localization (retention) of MT-COMP associated with chondrosarcoma
10) Confidence 0.65 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858657 Disease Relevance 0.35 Pain Relevance 0
The goal of these studies was to determine if reduction in MT-COMP synthesis by the most effective shRNA (3B) can prevent and/or eliminate intracellular retention of COMP and other ECM proteins.
Localization (retention) of COMP
11) Confidence 0.65 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858657 Disease Relevance 0.26 Pain Relevance 0
To determine the effect of MED mutations on the secretion of matrilin-3 we cloned and expressed in mammalian cells full-length wt matrilin-3 and matrilin-3 harboring a MED mutation (p.Val194Asp) and non-synonymous polymorphism (p.Glu252Lys).
Localization (secretion) of MED associated with osteochondrodysplasias
12) Confidence 0.63 Published 2005 Journal Human Mutation Section Body Doc Link PMC2726956 Disease Relevance 0.67 Pain Relevance 0
Several genes have been implicated in autosomal dominant MED, including those encoding cartilage oligomeric matrix protein (COMP; MIM# 132400) [Briggs et al., 1995], all three ?
Spec (implicated) Localization (implicated) of COMP in cartilage associated with osteochondrodysplasias
13) Confidence 0.63 Published 2005 Journal Human Mutation Section Body Doc Link PMC2726956 Disease Relevance 0.90 Pain Relevance 0.14
Several genes have been implicated in autosomal dominant MED, including those encoding cartilage oligomeric matrix protein (COMP; MIM# 132400) [Briggs et al., 1995], all three ?
Localization (implicated) of MED in cartilage associated with osteochondrodysplasias
14) Confidence 0.63 Published 2005 Journal Human Mutation Section Body Doc Link PMC2726956 Disease Relevance 0.90 Pain Relevance 0.14
In summary, the data presented in this paper suggest that MED caused by MATN3 mutations is the result of an intracellular retention of the mutant protein.



Localization (caused) of MED associated with osteochondrodysplasias
15) Confidence 0.63 Published 2005 Journal Human Mutation Section Abstract Doc Link PMC2726956 Disease Relevance 0.36 Pain Relevance 0
COMP is a pentameric protein comprised of five identical monomers assembled in the rER, modified in the Golgi and then exported to the matrix where it is incorporated into the extracellular matrix of the growth plate [1].
Localization (exported) of COMP in growth plate
16) Confidence 0.61 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858657 Disease Relevance 0.21 Pain Relevance 0
This massive retention causes impaired chondrocyte function with little COMP secreted into the matrix and premature loss of chondrocytes.
Neg (little) Localization (secreted) of COMP in chondrocytes
17) Confidence 0.60 Published 2004 Journal Int. J. Biochem. Cell Biol. Section Abstract Doc Link 15094116 Disease Relevance 0.34 Pain Relevance 0.15
Multiple epiphyseal dysplasia mutations in MATN3 cause misfolding of the A-domain and prevent secretion of mutant matrilin-3

Multiple epiphyseal dysplasia (MED) is a relatively common skeletal dysplasia that can present in childhood with a variable phenotype of short stature and pain and stiffness in the large joints, and often progresses to early-onset osteoarthritis in adulthood.

Localization (secretion) of MED in joints associated with pain, osteochondrodysplasias, cleidocranial dysplasia, osteoarthritis and growth problems
18) Confidence 0.59 Published 2005 Journal Human Mutation Section Title Doc Link PMC2726956 Disease Relevance 0.91 Pain Relevance 0.14
COMP is a 524-kDa, homopentameric, extracellular-matrix protein and it constitutes 0.5–1% of the wet weight of cartilage and is released from cartilage during the erosive process [26].
Localization (released) of COMP in cartilage
19) Confidence 0.49 Published 2004 Journal Arthritis Res Ther Section Body Doc Link PMC546286 Disease Relevance 0.51 Pain Relevance 0.20

General Comments

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