2.50
Hdl Handle:
http://hdl.handle.net/10033/621279
Title:
The CLU-files: disentanglement of a mystery.
Authors:
Rohne, Philipp; Prochnow, Hans; Koch-Brandt, Claudia
Abstract:
The 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.
Affiliation:
Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunshweig, Germany.
Citation:
The CLU-files: disentanglement of a mystery. 2016, 7 (1):1-15 Biomol Concepts
Journal:
Biomolecular concepts
Issue Date:
Feb-2016
URI:
http://hdl.handle.net/10033/621279
DOI:
10.1515/bmc-2015-0026
PubMed ID:
26673020
Type:
Article
Language:
en
ISSN:
1868-503X
Appears in Collections:
Publications of the research group Chemical Biology (CBIO)

Full metadata record

DC FieldValue Language
dc.contributor.authorRohne, Philippen
dc.contributor.authorProchnow, Hansen
dc.contributor.authorKoch-Brandt, Claudiaen
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.en
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
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