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231225s2017 xx |||||o 00| ||eng c |
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|a 10.2144/000114597
|2 doi
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|a pubmed25n0923.xml
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|a (DE-627)NLM277167922
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|a (NLM)29048269
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Inanc, Seniz
|e verfasserin
|4 aut
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| 245 |
1 |
3 |
|a An improved collagen zymography approach for evaluating the collagenases MMP-1, MMP-8, and MMP-13
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| 264 |
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1 |
|c 2017
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 19.06.2018
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|a Date Revised 10.12.2019
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|a published: Electronic
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|a Citation Status MEDLINE
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|a Collagen zymography is an SDS-PAGE-based method for detecting both the proenzyme and active forms of collagenases. Although collagen zymography is used for assessment of the matrix metalloproteinases MMP-1 and MMP-13, it can be difficult to detect these collagenases due to technical issues. Moreover, it remains unclear whether the collagenase activity of MMP-8 can be detected by this method. Here, we present an improved collagen zymography method that allows quantification of the activities of MMP-1, MMP-8, and MMP-13. Activities of recombinant collagenases could be detected in collagen zymogram gels copolymerized with 0.3 mg/mL type I collagen extracted from rat tail tendon. This improved method is sensitive enough to detect the activity of as little as 1 ng of collagenase. We generated standard curves for the three collagenases to quantify the collagenolytic activity levels of unknown samples. To validate our improved method, we investigated MMP-1 activity levels in human thyroid cancer (8505C) and normal thyroid (Nthy-ori-3-1) cell lines, finding that the proenzyme and active MMP-1 levels were greater in 8505C cells than in Nthy-ori-3-1 cells. Taken together, our data show that collagen zymography can be used in both molecular and clinical investigations to evaluate collagenase activities in various pathological conditions
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| 650 |
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4 |
|a Journal Article
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4 |
|a Validation Study
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| 650 |
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7 |
|a Collagen Type I
|2 NLM
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| 650 |
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7 |
|a Enzyme Precursors
|2 NLM
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| 650 |
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7 |
|a Isoenzymes
|2 NLM
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| 650 |
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7 |
|a Recombinant Proteins
|2 NLM
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| 650 |
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7 |
|a MMP13 protein, human
|2 NLM
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| 650 |
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7 |
|a EC 3.4.24.-
|2 NLM
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| 650 |
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7 |
|a Matrix Metalloproteinase 13
|2 NLM
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| 650 |
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7 |
|a EC 3.4.24.-
|2 NLM
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| 650 |
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7 |
|a MMP8 protein, human
|2 NLM
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| 650 |
|
7 |
|a EC 3.4.24.34
|2 NLM
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| 650 |
|
7 |
|a Matrix Metalloproteinase 8
|2 NLM
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| 650 |
|
7 |
|a EC 3.4.24.34
|2 NLM
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| 650 |
|
7 |
|a MMP1 protein, human
|2 NLM
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| 650 |
|
7 |
|a EC 3.4.24.7
|2 NLM
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| 650 |
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7 |
|a Matrix Metalloproteinase 1
|2 NLM
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| 650 |
|
7 |
|a EC 3.4.24.7
|2 NLM
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| 700 |
1 |
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|a Keles, Didem
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Oktay, Gulgun
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t BioTechniques
|d 1993
|g 63(2017), 4 vom: 01. Okt., Seite 174-180
|w (DE-627)NLM012627046
|x 1940-9818
|7 nnns
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| 773 |
1 |
8 |
|g volume:63
|g year:2017
|g number:4
|g day:01
|g month:10
|g pages:174-180
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| 856 |
4 |
0 |
|u http://dx.doi.org/10.2144/000114597
|3 Volltext
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|d 63
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|h 174-180
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