SwePub
Sök i LIBRIS databas

  Extended search

onr:"swepub:oai:lup.lub.lu.se:a1a052b3-a831-44a2-a904-864ef216ec3d"
 

Search: onr:"swepub:oai:lup.lub.lu.se:a1a052b3-a831-44a2-a904-864ef216ec3d" > New specific HSP47 ...

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

New specific HSP47 functions in collagen subfamily chaperoning

Köhler, Anna (author)
University of Cologne
Mörgelin, Matthias (author)
Lund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine,Colzyx AB
Gebauer, Jan M. (author)
University of Cologne
show more...
Öcal, Sinan (author)
University of Cologne
Imhof, Thomas (author)
University of Cologne
Koch, Manuel (author)
University of Cologne
Nagata, Kazuhiro (author)
Kyoto Sangyo University
Paulsson, Mats (author)
University of Cologne
Zaucke, Frank (author)
University Hospital Frankfurt
Baumann, Ulrich (author)
University of Cologne
Sengle, Gerhard (author)
University of Cologne,University Hospital of Cologne
show less...
 (creator_code:org_t)
2020
2020
English 13 s.
In: FASEB Journal. - 0892-6638. ; 34:9, s. 12040-12052
  • Journal article (peer-reviewed)
Abstract Subject headings
Close  
  • Although collagens are the most abundant proteins implicated in various disease pathways, essential mechanisms required for their proper folding and assembly are poorly understood. Heat-shock protein 47 (HSP47), an ER-resident chaperone, was mainly reported to fulfill key functions in folding and secretion of fibrillar collagens by stabilizing pro-collagen triple-helices. In this study, we demonstrate unique functions of HSP47 for different collagen subfamilies. Our results show that HSP47 binds to the N-terminal region of procollagen I and is essential for its secretion. However, HSP47 ablation does not majorly impact collagen VI secretion, but its lateral assembly. Moreover, specific ablation of Hsp47 in murine keratinocytes revealed a new role for the transmembrane collagen XVII triple-helix formation. Incompletely folded collagen XVII C-termini protruding from isolated HSP47 null keratinocyte membrane vesicles could be fully restored upon the application of recombinant HSP47. Thus, our study expands the current view regarding the client repertoire and function of HSP47, as well as emphasizes its importance for transmembrane collagen folding.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)

Keyword

collagen
collagen XVII
FACIT
HSP47
MACIT

Publication and Content Type

art (subject category)
ref (subject category)

Find in a library

To the university's database

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view