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The extracellular matrix of Volvox carteri: molecular structure of the cellular compartment

The extracellular matrix (ECM) of Volvox contains insoluble fibrous layers that surround individual cells at a distance to form contiguous cellular compartments. Using immunological techniques, we identified a sulfated surface glycoprotein (SSG 185) as the monomeric precursor of this substructure wi...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1989
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115946/
https://www.ncbi.nlm.nih.gov/pubmed/2689458
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description The extracellular matrix (ECM) of Volvox contains insoluble fibrous layers that surround individual cells at a distance to form contiguous cellular compartments. Using immunological techniques, we identified a sulfated surface glycoprotein (SSG 185) as the monomeric precursor of this substructure within the ECM. The primary structure of the SSG 185 poly-peptide chain has been derived from cDNA and genomic DNA. A central domain of the protein, 80 amino acid residues long, consists almost exclusively of hydroxyproline residues. The chemical structure of the highly sulfated polysaccharide covalently attached to SSG 185 has been determined by permethylation analysis. As revealed by EM, SSG 185 is a rod-shaped molecule with a 21-nm-long polysaccharide strand protruding from its central region. The chemical nature of the cross- links between SSG 185 monomers is discussed.
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spelling pubmed-21159462008-05-01 The extracellular matrix of Volvox carteri: molecular structure of the cellular compartment J Cell Biol Articles The extracellular matrix (ECM) of Volvox contains insoluble fibrous layers that surround individual cells at a distance to form contiguous cellular compartments. Using immunological techniques, we identified a sulfated surface glycoprotein (SSG 185) as the monomeric precursor of this substructure within the ECM. The primary structure of the SSG 185 poly-peptide chain has been derived from cDNA and genomic DNA. A central domain of the protein, 80 amino acid residues long, consists almost exclusively of hydroxyproline residues. The chemical structure of the highly sulfated polysaccharide covalently attached to SSG 185 has been determined by permethylation analysis. As revealed by EM, SSG 185 is a rod-shaped molecule with a 21-nm-long polysaccharide strand protruding from its central region. The chemical nature of the cross- links between SSG 185 monomers is discussed. The Rockefeller University Press 1989-12-01 /pmc/articles/PMC2115946/ /pubmed/2689458 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
The extracellular matrix of Volvox carteri: molecular structure of the cellular compartment
title The extracellular matrix of Volvox carteri: molecular structure of the cellular compartment
title_full The extracellular matrix of Volvox carteri: molecular structure of the cellular compartment
title_fullStr The extracellular matrix of Volvox carteri: molecular structure of the cellular compartment
title_full_unstemmed The extracellular matrix of Volvox carteri: molecular structure of the cellular compartment
title_short The extracellular matrix of Volvox carteri: molecular structure of the cellular compartment
title_sort extracellular matrix of volvox carteri: molecular structure of the cellular compartment
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115946/
https://www.ncbi.nlm.nih.gov/pubmed/2689458