HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Beck, K. Articles by Bächinger, H. P. Search for Related Content PubMed PubMed Citation Articles by Beck, K. Articles by Bächinger, H. P. Social Bookmarking                      What's this?

Volume 271, Number 35, Issue of August 30, 1996 pp. 21566-21573
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Triple Helix Formation of Procollagen Type I Can Occur at the Rough Endoplasmic Reticulum Membrane

(Received for publication, February 7, 1996, and in revised form, April 15, 1996)

Konrad Beck , Bruce A. Boswell , Catherine C. Ridgway and Hans Peter Bächinger ^¶

From the  Shriners Hospital for Children, Research Unit, Portland, Oregon 97201 and the ^¶ Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201

One key problem in understanding the biosynthesis of collagens remains the assembly of the three -chains. How and when are the different gene products selected, aligned, and folded into a triple helix? As the spatial arrangement during biosynthesis might be important, we concentrated on whether the rough endoplasmic reticular membrane is involved in this process. Microsomes were prepared from biosynthetically labeled chick tendon fibroblasts. Vesicles were spread as a monomolecular film which was then transferred over several compartments of a filmbalance containing fresh subphase. Fluorograms of the surface film showed that the monolayer contains procollagen chains. When the monolayer was transferred onto a chymotrypsin/trypsin-containing subphase, the gel bands of the pro-chains were shifted into the position of mature -chains, indicating that only the propeptides were digested and the collagenous regions were protected due to triple helix formation. Our results suggest that newly synthesized pro-chains can associate as trimers and fold into a triple helical conformation while they are still associated with the membranes of the rough endoplasmic reticulum. These processes also occur when interchain disulfide linkage is inhibited, indicating that chain selection and registration is not dependent on formation of covalent bonds among the carboxyl propeptides.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				B. Stefanovic, L. Stefanovic, B. Schnabl, R. Bataller, and D. A. Brenner TRAM2 Protein Interacts with Endoplasmic Reticulum Ca2+ Pump Serca2b and Is Necessary for Collagen Type I Synthesis Mol. Cell. Biol., February 15, 2004; 24(4): 1758 - 1768. [Abstract] [Full Text] [PDF]

				B. Stefanovic and D. A. Brenner 5' Stem-Loop of Collagen alpha 1(I) mRNA Inhibits Translation in Vitro but Is Required for Triple Helical Collagen Synthesis in Vivo J. Biol. Chem., January 3, 2003; 278(2): 927 - 933. [Abstract] [Full Text] [PDF]

				A. Veis and A. Veis Mineralization in Organic Matrix Frameworks Reviews in Mineralogy and Geochemistry, January 1, 2003; 54(1): 249 - 289. [Full Text] [PDF]

				G. Z. Lederkremer, Y. Cheng, B. M. Petre, E. Vogan, S. Springer, R. Schekman, T. Walz, and T. Kirchhausen Structure of the Sec23p/24p and Sec13p/31p complexes of COPII PNAS, September 4, 2001; (2001) 191359398. [Abstract] [Full Text] [PDF]

				J. N. Lindquist, W. F. Marzluff, and B. Stefanovic Fibrogenesis: III. Posttranscriptional regulation of type I collagen Am J Physiol Gastrointest Liver Physiol, September 1, 2000; 279(3): G471 - G476. [Abstract] [Full Text] [PDF]

				P. S. Kim and P. Arvan Endocrinopathies in the Family of Endoplasmic Reticulum (ER) Storage Diseases: Disorders of Protein Trafficking and the Role of ER Molecular Chaperones Endocr. Rev., April 1, 1998; 19(2): 173 - 202. [Abstract] [Full Text]

				B. K. Maddox, D. R. Keene, L. Y. Sakai, N. L. Charbonneau, N. P. Morris, C. C. Ridgway, B. A. Boswell, M. D. Sussman, W. A. Horton, H. P. Bachinger, et al. The Fate of Cartilage Oligomeric Matrix Protein Is Determined by the Cell Type in the Case of a Novel Mutation in Pseudoachondroplasia J. Biol. Chem., December 5, 1997; 272(49): 30993 - 30997. [Abstract] [Full Text] [PDF]

				G. Z. Lederkremer, Y. Cheng, B. M. Petre, E. Vogan, S. Springer, R. Schekman, T. Walz, and T. Kirchhausen Structure of the Sec23p/24p and Sec13p/31p complexes of COPII PNAS, September 11, 2001; 98(19): 10704 - 10709. [Abstract] [Full Text] [PDF]