QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

This Article Full Text (PDF) Submit an eLetter 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Iwata, M. Articles by Carlson, S. S. Search for Related Content PubMed PubMed Citation Articles by Iwata, M. Articles by Carlson, S. S.

 Previous Article  |  Next Article 

Journal of Neuroscience, Vol 13, 195-207, Copyright © 1993 by Society for Neuroscience

ARTICLE

A large chondroitin sulfate proteoglycan has the characteristics of a general extracellular matrix component of adult brain

M Iwata and SS Carlson
Department of Physiology and Biophysics, University of Washington, Seattle 98195.

Extracellular matrix (ECM) is a secreted extracellular network. Few components of adult brain ECM are known. We have identified a new, large chondroitin sulfate proteoglycan (T1 antigen) that acts like a general ECM protein of brain. First, it is present throughout the brain; second, it has the properties of an extracellular protein; and third, it is extracted only under denaturing conditions. Immunocytochemical localization of the T1 antigen by light microscope shows it to be present throughout the rat brain in both white and gray matter. The T1 antigen outlines Purkinje and other large cells. No antigenicity is seen inside these cells. Biochemical evidence suggests that the T1 antigen is extracellular rather than cytosolic or intravesicular. The T1 antigen is disulfide-linked to two other proteins. Disulfide bonds are found only in extracellular or intravesicular proteins, not in intracellular cytosolic proteins. Moreover, the T1 antigen is probably not intravesicular. Unlike intravesicular proteins, only a small amount of T1 antigen is solubilized by nondenaturing detergents. While nondenaturing detergents extract but a small amount of T1 antigen from rat brain, the majority is solubilized by denaturing conditions (6 M guanidine-HCl). This behavior is similar to that of ECM components in other tissues and is unlike that of membrane proteins, even those linked to the cytoskeleton. We hypothesize that the insolubility of the T1 antigen in brain is due to its presence in an extracellular aggregate. The T1 antigen is a proteoglycan with a highly glycosylated protein core of 300 kDa. It does not appear to be related to the large, heavily glycosylated chondroitin sulfate proteoglycans aggrecan and versican, which were discovered in non-neural tissues. Antibodies to a 15 residue peptide present in both aggrecan and versican do not react with the T1 antigen.

This article has been cited by other articles:

				Y.-J. Son, T. W. Scranton, W. J. Sunderland, S. J. Baek, J. H. Miner, J. R. Sanes, and S. S. Carlson The Synaptic Vesicle Protein SV2 Is Complexed with an alpha 5-Containing Laminin on the Nerve Terminal Surface J. Biol. Chem., January 7, 2000; 275(1): 451 - 460. [Abstract] [Full Text] [PDF]

				U. Rauch, A. Clement, C. Retzler, L. Frohlich, R. Fassler, W. Gohring, and A. Faissner Mapping of a Defined Neurocan Binding Site to Distinct Domains of Tenascin-C J. Biol. Chem., October 24, 1997; 272(43): 26905 - 26912. [Abstract] [Full Text] [PDF]

				C. Retzler, H. Wiedemann, G. Kulbe, and U. Rauch Structural and Electron Microscopic Analysis of Neurocan and Recombinant Neurocan Fragments J. Biol. Chem., July 19, 1996; 271(29): 17107 - 17113. [Abstract] [Full Text] [PDF]

				C. I. Seidenbecher, K. Richter, U. Rauch, R. Fässler, C. C. Garner, and E. D. Gundelfinger Brevican, a Chondroitin Sulfate Proteoglycan of Rat Brain, Occurs as Secreted and Cell Surface Glycosylphosphatidylinositol-anchored Isoforms J. Biol. Chem., November 10, 1995; 270(45): 27206 - 27212. [Abstract] [Full Text] [PDF]

				M. Zako, T. Shinomura, M. Ujita, K. Ito, and K. Kimata Expression of PG-M(V3), an Alternatively Spliced Form of PG-M without a Chondroitin Sulfate Attachment Region in Mouse and Human Tissues J. Biol. Chem., February 24, 1995; 270(8): 3914 - 3918. [Abstract] [Full Text] [PDF]

				M. W. Lark, J. T. Gordy, J. R. Weidner, J. Ayala, J. H. Kimura, H. R. Williams, R. A. Mumford, C. R. Flannery, S. S. Carlson, M. Iwata, et al. Cell-mediated Catabolism of Aggrecan J. Biol. Chem., February 10, 1995; 270(6): 2550 - 2556. [Abstract] [Full Text] [PDF]

				L. Smith-Thomas, J Stevens, J Fok-Seang, A Faissner, J. Rogers, and J. Fawcett Increased axon regeneration in astrocytes grown in the presence of proteoglycan synthesis inhibitors J. Cell Sci., January 3, 1995; 108(3): 1307 - 1315. [Abstract] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help