Oligomerization of the proteolytic products is an intrinsic property of prion proteins

Dessislava Georgieva; Mirjam Koker; Lars Redecke; Markus Perbandt; Joachim Clos; Reinhard Bredehorst; Nicolay Genov; Christian Betzel

doi:10.1016/j.bbrc.2004.08.230

Oligomerization of the proteolytic products is an intrinsic property of prion proteins

Dessislava Georgieva, Mirjam Koker, Lars Redecke, Markus Perbandt, Joachim Clos, Reinhard Bredehorst, Nicolay Genov, Christian Betzel

Institut für Biochemie

23 Zitate (Scopus)

Abstract

In the present study we show that the oligomerization of the proteolytic products is an intrinsic property of prion proteins. No such oligomerization was observed for the proteolytic products of other proteins after identical treatment. The rate of enzymatic hydrolysis of recombinant human (rhPrP) (23-231) and golden hamster (rmaPrP) (23-231) prion proteins as well as that of rmaPrP (90-231), corresponding to the infectious fragment of the scrapie form, drastically increases in the presence of chemical chaperones like dimethyl sulphoxide and glycerol as well as in 20% ethanol. A bacterial proteinase, termed "prionase," has a superior efficiency towards prion proteins in comparison to proteinase K and subtilisin DY. The early steps in the proteolysis by the latter enzymes have been identified. The results have potential impact on the treatment of scrapie-infected materials.

Originalsprache	Englisch
Zeitschrift	Biochemical and Biophysical Research Communications
Jahrgang	323
Ausgabenummer	4
Seiten (von - bis)	1278-1286
Seitenumfang	9
ISSN	0006-291X
DOIs	https://doi.org/10.1016/j.bbrc.2004.08.230
Publikationsstatus	Veröffentlicht - 29.10.2004

Fördermittel

The work was supported by grants of the Deutsche Luft- und Raumfahrtagentur (DLR, Projektträger Gesundheitsforschung) via Grant 01KO0206 and the RiNA GmbH Berlin. This work was also supported in part by the Bulgarian National Foundation for Scientific Research, Grant X-1301.

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Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

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10.1016/j.bbrc.2004.08.230

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title = "Oligomerization of the proteolytic products is an intrinsic property of prion proteins",

abstract = "In the present study we show that the oligomerization of the proteolytic products is an intrinsic property of prion proteins. No such oligomerization was observed for the proteolytic products of other proteins after identical treatment. The rate of enzymatic hydrolysis of recombinant human (rhPrP) (23-231) and golden hamster (rmaPrP) (23-231) prion proteins as well as that of rmaPrP (90-231), corresponding to the infectious fragment of the scrapie form, drastically increases in the presence of chemical chaperones like dimethyl sulphoxide and glycerol as well as in 20\% ethanol. A bacterial proteinase, termed {"}prionase,{"} has a superior efficiency towards prion proteins in comparison to proteinase K and subtilisin DY. The early steps in the proteolysis by the latter enzymes have been identified. The results have potential impact on the treatment of scrapie-infected materials.",

author = "Dessislava Georgieva and Mirjam Koker and Lars Redecke and Markus Perbandt and Joachim Clos and Reinhard Bredehorst and Nicolay Genov and Christian Betzel",

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AU - Georgieva, Dessislava

AU - Koker, Mirjam

AU - Redecke, Lars

AU - Perbandt, Markus

AU - Clos, Joachim

AU - Bredehorst, Reinhard

AU - Genov, Nicolay

AU - Betzel, Christian

N1 - Funding Information: The work was supported by grants of the Deutsche Luft- und Raumfahrtagentur (DLR, Projektträger Gesundheitsforschung) via Grant 01KO0206 and the RiNA GmbH Berlin. This work was also supported in part by the Bulgarian National Foundation for Scientific Research, Grant X-1301. Copyright: Copyright 2012 Elsevier B.V., All rights reserved.

PY - 2004/10/29

Y1 - 2004/10/29

N2 - In the present study we show that the oligomerization of the proteolytic products is an intrinsic property of prion proteins. No such oligomerization was observed for the proteolytic products of other proteins after identical treatment. The rate of enzymatic hydrolysis of recombinant human (rhPrP) (23-231) and golden hamster (rmaPrP) (23-231) prion proteins as well as that of rmaPrP (90-231), corresponding to the infectious fragment of the scrapie form, drastically increases in the presence of chemical chaperones like dimethyl sulphoxide and glycerol as well as in 20% ethanol. A bacterial proteinase, termed "prionase," has a superior efficiency towards prion proteins in comparison to proteinase K and subtilisin DY. The early steps in the proteolysis by the latter enzymes have been identified. The results have potential impact on the treatment of scrapie-infected materials.

AB - In the present study we show that the oligomerization of the proteolytic products is an intrinsic property of prion proteins. No such oligomerization was observed for the proteolytic products of other proteins after identical treatment. The rate of enzymatic hydrolysis of recombinant human (rhPrP) (23-231) and golden hamster (rmaPrP) (23-231) prion proteins as well as that of rmaPrP (90-231), corresponding to the infectious fragment of the scrapie form, drastically increases in the presence of chemical chaperones like dimethyl sulphoxide and glycerol as well as in 20% ethanol. A bacterial proteinase, termed "prionase," has a superior efficiency towards prion proteins in comparison to proteinase K and subtilisin DY. The early steps in the proteolysis by the latter enzymes have been identified. The results have potential impact on the treatment of scrapie-infected materials.

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M3 - Journal articles

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SN - 0006-291X

VL - 323

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EP - 1286

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

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ER -

Oligomerization of the proteolytic products is an intrinsic property of prion proteins

Abstract

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