Show simple item record

dc.contributor.authorRohne, Philipp
dc.contributor.authorProchnow, Hans
dc.contributor.authorKoch-Brandt, Claudia
dc.date.accessioned2018-02-15T09:22:27Z
dc.date.available2018-02-15T09:22:27Z
dc.date.issued2016-02
dc.identifier.citationThe CLU-files: disentanglement of a mystery. 2016, 7 (1):1-15 Biomol Conceptsen
dc.identifier.issn1868-503X
dc.identifier.pmid26673020
dc.identifier.doi10.1515/bmc-2015-0026
dc.identifier.urihttp://hdl.handle.net/10033/621279
dc.description.abstractThe multifaceted protein clusterin (CLU) has been challenging researchers for more than 35 years. The characterization of CLU as a molecular chaperone was one of the major breakthroughs in CLU research. Today, secretory clusterin (sCLU), also known as apolipoprotein J (apoJ), is considered one of the most important extracellular chaperones ever found. It is involved in a broad range of physiological and pathophysiological functions, where it exerts a cytoprotective role. Descriptions of various forms of intracellular CLU have led to further and even contradictory functions. To untangle the current state of knowledge of CLU, this review will combine old views in the field, with new discoveries to highlight the nature and function of this fascinating protein(s). In this review, we further describe the expression and subcellular location of various CLU forms. Moreover, we discuss recent insights into the structure of CLU and assess how structural properties as well as the redox environment determine the chaperone activity of CLU. Eventually, the review connects the biochemistry and molecular cell biology of CLU with medical aspects, to formulate a hypothesis of a CLU function in health and disease.
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAnimalsen
dc.subject.meshCellular Structuresen
dc.subject.meshClusterinen
dc.subject.meshHumansen
dc.subject.meshOxidative Stressen
dc.subject.meshProtein Conformationen
dc.titleThe CLU-files: disentanglement of a mystery.en
dc.typeArticleen
dc.contributor.departmentHelmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunshweig, Germany.en
dc.identifier.journalBiomolecular conceptsen
refterms.dateFOA2018-06-13T05:43:25Z
html.description.abstractThe multifaceted protein clusterin (CLU) has been challenging researchers for more than 35 years. The characterization of CLU as a molecular chaperone was one of the major breakthroughs in CLU research. Today, secretory clusterin (sCLU), also known as apolipoprotein J (apoJ), is considered one of the most important extracellular chaperones ever found. It is involved in a broad range of physiological and pathophysiological functions, where it exerts a cytoprotective role. Descriptions of various forms of intracellular CLU have led to further and even contradictory functions. To untangle the current state of knowledge of CLU, this review will combine old views in the field, with new discoveries to highlight the nature and function of this fascinating protein(s). In this review, we further describe the expression and subcellular location of various CLU forms. Moreover, we discuss recent insights into the structure of CLU and assess how structural properties as well as the redox environment determine the chaperone activity of CLU. Eventually, the review connects the biochemistry and molecular cell biology of CLU with medical aspects, to formulate a hypothesis of a CLU function in health and disease.


Files in this item

Thumbnail
Name:
Rohne et al.pdf
Size:
1.307Mb
Format:
PDF
Description:
OPen Access article

This item appears in the following Collection(s)

Show simple item record

http://creativecommons.org/licenses/by-nc-sa/4.0/
Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/4.0/