|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 276, Issue 27, 25399-25403, July 6, 2001
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the ¶ Shriners Hospital for Children and the
HSP47, a collagen-specific molecular chaperone,
interacts with unfolded and folded procollagens. Binding of
chicken HSP47 to native bovine type I collagen was studied by
fluorescence quenching and cooperative binding with a collagen
concentration at half saturation (Khalf) of
1.4 × 10
HSP47 Binds Cooperatively to Triple Helical Type I
Collagen but Has Little Effect on the Thermal Stability or Rate of
Refolding*
§ and¶
Department of Biochemistry and Molecular Biology, Oregon
Health Sciences University, Portland, Oregon 97201
7 M, and a Hill coefficient of
4.3 was observed. Similar results are observed for the binding of mouse
HSP47 recombinantly expressed in Escherichia coli. Chicken
HSP47 binds equally well to native type II and type III procollagen
without the carboxyl-terminal propeptide (pN type III collagen),
but binding to triple helical collagen-like peptides is much weaker.
Weak binding occurred to both hydroxylated and nonhydroxylated
collagen-like peptides, and a significant chain length dependence was
observed. Binding of HSP47 to native type I collagen had no effect on
the thermal stability of the triple helix. Refolding of type I collagen
in the presence of HSP47 showed minor changes, but these are probably not biologically significant. Binding of HSP47 to bovine pN type III
collagen has only minor effects on the thermal stability of the triple
helix and does not influence the refolding kinetics of the triple helix.
*
This work was supported by a grant from Shriners Hospitals.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
To whom correspondence should be addressed: Shriners
Hospital for Children, Research Unit, 3101 S.W. Sam Jackson Park Rd., Portland, OR 97201. Tel.: 503-221-3433; Fax: 503-221-3451; E-mail: hpb@shcc.org.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  Y. Ishikawa, J. Vranka, J. Wirz, K. Nagata, and H. P. Bachinger The Rough Endoplasmic Reticulum-resident FK506-binding Protein FKBP65 Is a Molecular Chaperone That Interacts with Collagens J. Biol. Chem., November 14, 2008; 283(46): 31584 - 31590. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Koide, Y. Nishikawa, S. Asada, C. M. Yamazaki, Y. Takahara, D. L. Homma, A. Otaka, K. Ohtani, N. Wakamiya, K. Nagata, et al. Specific Recognition of the Collagen Triple Helix by Chaperone HSP47: II. THE HSP47-BINDING STRUCTURAL MOTIF IN COLLAGENS AND RELATED PROTEINS J. Biol. Chem., April 21, 2006; 281(16): 11177 - 11185. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Koide, S. Asada, Y. Takahara, Y. Nishikawa, K. Nagata, and K. Kitagawa Specific Recognition of the Collagen Triple Helix by Chaperone HSP47: MINIMAL STRUCTURAL REQUIREMENT AND SPATIAL MOLECULAR ORIENTATION J. Biol. Chem., February 10, 2006; 281(6): 3432 - 3438. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Ju and R. D. Cummings A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase PNAS, December 24, 2002; 99(26): 16613 - 16618. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Meyer, L. Notari, and S. P. Becerra Mapping the Type I Collagen-binding Site on Pigment Epithelium-derived Factor. IMPLICATIONS FOR ITS ANTIANGIOGENIC ACTIVITY J. Biol. Chem., November 15, 2002; 277(47): 45400 - 45407. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. F. Rocnik, E. van der Veer, H. Cao, R. A. Hegele, and J. G. Pickering Functional Linkage between the Endoplasmic Reticulum Protein Hsp47 and Procollagen Expression in Human Vascular Smooth Muscle Cells J. Biol. Chem., October 4, 2002; 277(41): 38571 - 38578. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Tasab, L. Jenkinson, and N. J. Bulleid Sequence-specific Recognition of Collagen Triple Helices by the Collagen-specific Molecular Chaperone HSP47 J. Biol. Chem., September 13, 2002; 277(38): 35007 - 35012. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Koide, Y. Takahara, S. Asada, and K. Nagata Xaa-Arg-Gly Triplets in the Collagen Triple Helix Are Dominant Binding Sites for the Molecular Chaperone HSP47 J. Biol. Chem., February 15, 2002; 277(8): 6178 - 6182. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. V. Persikov and B. Brodsky Unstable molecules form stable tissues PNAS, February 5, 2002; 99(3): 1101 - 1103. [Full Text] [PDF]
|
|
|
|
|
|
T. R. Dafforn, M. Della, and A. D. Miller The Molecular Interactions of Heat Shock Protein 47 (Hsp47) and Their Implications for Collagen Biosynthesis J. Biol. Chem., December 21, 2001; 276(52): 49310 - 49319. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |