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Three Wavelength Substrate System of Neutrophil Serine Proteinases.

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Title: Three Wavelength Substrate System of Neutrophil Serine Proteinases.
Authors: Wysocka, Magdalena1, Lesner, Adam1 adas@chem.univ.gda.pl, Gruba, Natalia1, Korkmaz, Brice2, Gauthier, Francis2, Kitamatsu, Mizuki3, Łęgowska, Anna1, Rolka, Krzysztof1
Source: Analytical Chemistry. 8/21/2012, Vol. 84 Issue 16, p7241-7248. 8p.
Subjects: Substrates (Materials science), Neutrophils, Serine proteinases, Inflammation, Fluorescence resonance energy transfer, Proteolytic enzymes, Granulomatosis with polyangiitis, Elastases
Abstract: Neutrophil serine proteases, including elastase, proteinase 3, and cathepsin G, are closely related enzymes stored in similar amounts in azurophil granules and released at the same time from triggered neutrophils at inflammatory sites. We have synthesized new fluorescence resonance energy transfer (FRET) substrates with different fluorescence donor-acceptor pairs that allow all three proteases to be quantified at the same time and in the same reaction mixture. This was made possible because the fluorescence emission spectra of the fluorescence donors do not overlap and because the values of the specificity constants were in the same range. Thus, similar activities of proteases can be measured with the same sensitivity. In addition, these substrates contain an N-terminal 2-(2-(2-aminoethoxy)ethoxy)acetic acid (PEG) moiety that makes them cell permeable. Using the mixture of these selected substrates, we were able to detect the neutrophil serine protease (NSP) activity on the activated neutrophil membrane and in the neutrophil lysate in a single measurement. Also, using the substrate mixture, we were in a position to efficiently determine NSP activity in human serum of healthy individuals and patients with diagnosed Wegener disease or microscopic polyangiitis. [ABSTRACT FROM AUTHOR]
Copyright of Analytical Chemistry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Three Wavelength Substrate System of Neutrophil Serine Proteinases.
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  Data: <searchLink fieldCode="AR" term="%22Wysocka%2C+Magdalena%22">Wysocka, Magdalena</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Lesner%2C+Adam%22">Lesner, Adam</searchLink><relatesTo>1</relatesTo><i> adas@chem.univ.gda.pl</i><br /><searchLink fieldCode="AR" term="%22Gruba%2C+Natalia%22">Gruba, Natalia</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Korkmaz%2C+Brice%22">Korkmaz, Brice</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Gauthier%2C+Francis%22">Gauthier, Francis</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Kitamatsu%2C+Mizuki%22">Kitamatsu, Mizuki</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Łęgowska%2C+Anna%22">Łęgowska, Anna</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Rolka%2C+Krzysztof%22">Rolka, Krzysztof</searchLink><relatesTo>1</relatesTo>
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  Data: <searchLink fieldCode="JN" term="%22Analytical+Chemistry%22">Analytical Chemistry</searchLink>. 8/21/2012, Vol. 84 Issue 16, p7241-7248. 8p.
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  Data: <searchLink fieldCode="DE" term="%22Substrates+%28Materials+science%29%22">Substrates (Materials science)</searchLink><br /><searchLink fieldCode="DE" term="%22Neutrophils%22">Neutrophils</searchLink><br /><searchLink fieldCode="DE" term="%22Serine+proteinases%22">Serine proteinases</searchLink><br /><searchLink fieldCode="DE" term="%22Inflammation%22">Inflammation</searchLink><br /><searchLink fieldCode="DE" term="%22Fluorescence+resonance+energy+transfer%22">Fluorescence resonance energy transfer</searchLink><br /><searchLink fieldCode="DE" term="%22Proteolytic+enzymes%22">Proteolytic enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Granulomatosis+with+polyangiitis%22">Granulomatosis with polyangiitis</searchLink><br /><searchLink fieldCode="DE" term="%22Elastases%22">Elastases</searchLink>
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  Data: Neutrophil serine proteases, including elastase, proteinase 3, and cathepsin G, are closely related enzymes stored in similar amounts in azurophil granules and released at the same time from triggered neutrophils at inflammatory sites. We have synthesized new fluorescence resonance energy transfer (FRET) substrates with different fluorescence donor-acceptor pairs that allow all three proteases to be quantified at the same time and in the same reaction mixture. This was made possible because the fluorescence emission spectra of the fluorescence donors do not overlap and because the values of the specificity constants were in the same range. Thus, similar activities of proteases can be measured with the same sensitivity. In addition, these substrates contain an N-terminal 2-(2-(2-aminoethoxy)ethoxy)acetic acid (PEG) moiety that makes them cell permeable. Using the mixture of these selected substrates, we were able to detect the neutrophil serine protease (NSP) activity on the activated neutrophil membrane and in the neutrophil lysate in a single measurement. Also, using the substrate mixture, we were in a position to efficiently determine NSP activity in human serum of healthy individuals and patients with diagnosed Wegener disease or microscopic polyangiitis. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
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  Data: <i>Copyright of Analytical Chemistry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1021/ac301684w
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        Text: English
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      – SubjectFull: Substrates (Materials science)
        Type: general
      – SubjectFull: Neutrophils
        Type: general
      – SubjectFull: Serine proteinases
        Type: general
      – SubjectFull: Inflammation
        Type: general
      – SubjectFull: Fluorescence resonance energy transfer
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      – SubjectFull: Proteolytic enzymes
        Type: general
      – SubjectFull: Granulomatosis with polyangiitis
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      – SubjectFull: Elastases
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      – TitleFull: Three Wavelength Substrate System of Neutrophil Serine Proteinases.
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              M: 08
              Text: 8/21/2012
              Type: published
              Y: 2012
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