Development, Vol 110, Issue 3 805-813, Copyright © 1990 by Company of Biologists

JOURNAL ARTICLES

Concurrent reduction in the sulfation of heparan sulfate and basement membrane assembly in a cell model system

PR Brauer, KM Keller and JM Keller
Department of Cell Biology and Anatomy, UHS/Chicago Medical School, IL 60064.

Basement membranes (BMs) are specialized extracellular matrices that have important roles in cell attachment, migration, growth and differentiation. The murine teratocarcinoma cell line, M1536-B3, has been shown to produce a model BM composed of laminin, entactin and heparan sulfate proteoglycans but lacking collagen. Therefore, M1536-B3 cells are an excellent model system in which to study the role of non-collagenous components in BM assembly. We have used these cells to test for a requirement of mature heparan sulfate (HS) chains in BM assembly. Growth of M1536-B3 cells in the presence of chlorate, an inhibitor of activated sulfate synthesis, resulted in a dose-dependent decrease in the sulfation of glycosaminoglycans and reduction in the charge density of the isolated HS. The undersulfated HS from chlorate-treated cells had a decreased binding capacity for laminin when compared with control HS. Concurrent with these changes in sulfation, chlorate treatment of M1536-B3 cells resulted in the failure of BM assembly, which was restored upon removal of the chlorate from the growth medium. These results were not due to major alterations in cell attachment, spreading, growth, protein synthesis, or to an inability of the cells to synthesize and secrete laminin. These data suggest that the sulfation of HS and its subsequent ability to interact with other BM components play major roles in the assembly and structure of BMs.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				D.J. Lalor, T. Schnyder, V. Saridakis, D.E. Pilloff, A. Dong, H. Tang, T.S. Leyh, and E.F. Pai Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity Protein Eng. Des. Sel., December 1, 2003; 16(12): 1071 - 1079. [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]

				K. Norgard-Sumnicht, N. Varki, and A Varki Calcium-dependent heparin-like ligands for L-selectin in nonlymphoid endothelial cells Science, July 23, 1993; 261(5120): 480 - 483. [Abstract] [PDF]