Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 59:894-900 (1977)
© 1977 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
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 CrossRef
Right arrow Citing Articles via Web of Science (83)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pope, D. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pope, D. G.
Agricola
Right arrow Articles by Pope, D. G.
Articles

Relationships between Hydroxyproline-containing Proteins Secreted into the Cell Wall and Medium by Suspension-cultured Acer pseudoplatanus Cells 1

David G. Pope

a MSU/ERDA Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824

The pathway of hydroxyproline-containing proteins to the cell wall, and to the growth medium in suspension-cultured Acer pseudoplatanus cells is traced by following the kinetics of the transfer of protein-bound 14C-hydroxyproline into various fractions, and by comparing the hydroxyproline-arabinoside profiles of these fractions after alkaline hydrolysis.

Hydroxyproline-rich protein passes directly from a membrane-bound compartment in the cytoplasm to the cell wall, not via an intermediate salt-soluble pool in the wall.

There are at least three hydroxyproline-containing glycoproteins in the cell wall. One which possesses mono, tri, and tetraarabinoside side chains accounts for over 90% of the total hydroxyproline. This glycoprotein is "extensin."

The hydroxyproline-containing proteins secreted into the medium have a glycosylation pattern markedly different from that of the major cell wall glycoprotein. It appears that there is little or no wall-like extensin in the medium.

Approximately half of the protein-bound hydroxyproline secreted into the medium is linked to an arabinogalactan. This linkage is also found in a particulate wall protein precursor fraction from the cytoplasm, but only trace amounts can be detected in the cell wall.


1 This work was supported by United States Atomic Energy Commission Contract AT(11-1)-1338).




This article has been cited by other articles:


Home page
Plant Physiol.Home page
H. S. Sardar, J. Yang, and A. M. Showalter
Molecular Interactions of Arabinogalactan Proteins with Cortical Microtubules and F-Actin in Bright Yellow-2 Tobacco Cultured Cells
Plant Physiology, December 1, 2006; 142(4): 1469 - 1479.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
J. M. Estevez, M. J. Kieliszewski, N. Khitrov, and C. Somerville
Characterization of Synthetic Hydroxyproline-Rich Proteoglycans with Arabinogalactan Protein and Extensin Motifs in Arabidopsis
Plant Physiology, October 1, 2006; 142(2): 458 - 470.
[Abstract] [Full Text] [PDF]


Home page
GlycobiologyHome page
A. S. Karnoup, V. Turkelson, and W.H. K. Anderson
O-Linked glycosylation in maize-expressed human IgA1
Glycobiology, October 1, 2005; 15(10): 965 - 981.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
L. Tan, F. Qiu, D. T. A. Lamport, and M. J. Kieliszewski
Structure of a Hydroxyproline (Hyp)-Arabinogalactan Polysaccharide from Repetitive Ala-Hyp Expressed in Transgenic Nicotiana tabacum
J. Biol. Chem., March 26, 2004; 279(13): 13156 - 13165.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
L. Tan, J. F. Leykam, and M. J. Kieliszewski
Glycosylation Motifs That Direct Arabinogalactan Addition to Arabinogalactan-Proteins
Plant Physiology, July 1, 2003; 132(3): 1362 - 1369.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
E. Shpak, J. F. Leykam, and M. J. Kieliszewski
Synthetic genes for glycoprotein design and the elucidation of hydroxyproline-O-glycosylation codes
PNAS, December 21, 1999; 96(26): 14736 - 14741.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. J. Kieliszewski, M. O'Neill, J. Leykam, and R. Orlando
Tandem Mass Spectrometry and Structural Elucidation of Glycopeptides from a Hydroxyproline-rich Plant Cell Wall Glycoprotein Indicate That Contiguous Hydroxyproline Residues Are the Major Sites of Hydroxyproline O-Arabinosylation
J. Biol. Chem., February 10, 1995; 270(6): 2541 - 2549.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
N. CARPITA, D. SABULARSE, D. MONTEZINOS, and D. P. DELMER
Determination of the Pore Size of Cell Walls of Living Plant Cells
Science, September 14, 1979; 205(4411): 1144 - 1147.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1977 by the American Society of Plant Biologists