Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print July 28, 2004
Mol. Biol. Cell 10.1091/mbc.E04-01-0050

A more recent version of this article appeared on October 1, 2004
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Figure
Right arrow All Versions of this Article:
E04-01-0050v1
15/10/4467    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Matsuoka, Y.
Right arrow Articles by Nagata, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Matsuoka, Y.
Right arrow Articles by Nagata, K.

Submitted on January 20, 2004
Revised on May 25, 2004
Accepted on July 6, 2004

Insufficient Folding of Type IV Collagen and Formation of Abnormal Basement Membrane-like Structure in Embryoid Bodies Derived from Hsp47-null ES Cells

Yasuhiro Matsuoka*, Hiroshi Kubota*{dagger}, Eijiro Adachi{ddagger}, Naoko Nagai*{sect}, Toshihiro Marutani*, Nobuko Hosokawa*{dagger}, and Kazuhiro Nagata*{dagger}||

*Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8397, Japan; {dagger}CREST (Core Research for Evolution Science and Technology), Japan Science and Technology Agency, Japan; {ddagger}Department of Molecular Morphology, Kitasato University Graduate School of Medicine, Sagamihara, Kanagawa 228-8555, Japan

Monitoring Editor: Peter Walter

Hsp47 is a molecular chaperone that specifically recognizes procollagen in the endoplasmic reticulum. Hsp47-null mouse embryos produce immature type I collagen and form discontinuous basement membranes. We established Hsp47-/- embryonic stem cell lines and examined formation of basement membrane and production of type IV collagen in embryoid bodies, a model for postimplantation egg-cylinder stage embryos. The visceral endodermal cell layers surrounding Hsp47-/- embryoid bodies were often disorganized, a result which suggested abnormal function of the basement membrane under the visceral endoderm. Rate of type IV collagen secretion by Hsp47-/- cells was fourfold lower than that of Hsp47+/+ cells. Furthermore, type IV collagen secreted from Hsp47-/- cells was much more sensitive to protease digestion than was type IV collagen secreted from Hsp47+/+ cells, which suggested insufficient or incorrect triple helix formation in type IV collagen in the absence of Hsp47. These results indicate for the first time that Hsp47 is required for the molecular maturation of type IV collagen and suggest that misfolded type IV collagen causes abnormal morphology of embryoid bodies.

{sect}Present address: Institute for Molecular Science of Medicine, Aichi Medical University, Nagakute, Aichi 480-1195, Japan

||Corresponding author. E-mail: nagata{at}frontier.kyoto-u.ac.jp




This article has been cited by other articles:


Home page
 J. Cell Sci.Home page
N. Martinek, J. Shahab, M. Saathoff, and M. Ringuette
Haemocyte-derived SPARC is required for collagen-IV-dependent stability of basal laminae in Drosophila embryos
J. Cell Sci., May 15, 2008; 121(10): 1671 - 1680.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Sipila, H. Ruotsalainen, R. Sormunen, N. L. Baker, S. R. Lamande, M. Vapola, C. Wang, Y. Sado, A. Aszodi, and R. Myllyla
Secretion and Assembly of Type IV and VI Collagens Depend on Glycosylation of Hydroxylysines
J. Biol. Chem., November 16, 2007; 282(46): 33381 - 33388.
[Abstract] [Full Text] [PDF]

Home page
 J. Dent. Res.Home page
N. Martinek, J. Shahab, J. Sodek, and M. Ringuette
Is SPARC an Evolutionarily Conserved Collagen Chaperone?
J. Dent. Res., April 1, 2007; 86(4): 296 - 305.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Holster, O. Pakkanen, R. Soininen, R. Sormunen, M. Nokelainen, K. I. Kivirikko, and J. Myllyharju
Loss of Assembly of the Main Basement Membrane Collagen, Type IV, but Not Fibril-forming Collagens and Embryonic Death in Collagen Prolyl 4-Hydroxylase I Null Mice
J. Biol. Chem., January 26, 2007; 282(4): 2512 - 2519.
[Abstract] [Full Text] [PDF]

Home page
 GENES CELLSHome page
A. Oguro, T. Sakurai, Y. Fujita, S. Lee, H. Kubota, K. Nagata, and Y. Atomi
The molecular chaperone HSP47 rapidly senses gravitational changes in myoblasts
Genes Cells, November 1, 2006; 11(11): 1253 - 1265.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
Y. Ishida, H. Kubota, A. Yamamoto, A. Kitamura, H. P. Bachinger, and K. Nagata
Type I Collagen in Hsp47-null Cells Is Aggregated in Endoplasmic Reticulum and Deficient in N-Propeptide Processing and Fibrillogenesis
Mol. Biol. Cell, May 1, 2006; 17(5): 2346 - 2355.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
T. Marutani, A. Yamamoto, N. Nagai, H. Kubota, and K. Nagata
Accumulation of type IV collagen in dilated ER leads to apoptosis in Hsp47-knockout mouse embryos via induction of CHOP
J. Cell Sci., November 15, 2004; 117(24): 5913 - 5922.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2004 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.