Mast cell glycosaminoglycans

Mast cells contain granules packed with a mixture of proteins that are released on degranulation. The proteoglycan serglycin carries an array of glycosaminoglycan (GAG) side chains, sometimes heparin, sometimes chondroitin or dermatan sulphate. Tight packing of granule proteins is dependent on the presence of serglycin carrying these GAGs. The GAGs of mast cells were most intensively studied in the 1970s and 1980s, and though something is known about the fine structure of chondroitin sulphate and dermatan sulphate in mast cells, little is understood about the composition of the heparin/heparan sulphate chains. Recent emphasis on the analysis of mast cell heparin from different species and tissues, arising from the use of this GAG in medicine, lead to the question of whether variations within heparin structures between mast cell populations are as significant as variations in the mix of chondroitins and heparins.

• Publication year

  2016

• Venue

  Glycoconjugate Journal

• Publication date

  2016-11-30

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1007/s10719-016-9749-0PMID 27900574PMCID 5487770
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  2016cited by this paper
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  2016cited by this paper
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  2016cited by this paper
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  2015cited by this paper
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  2014cited by this paper
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  2014cited by this paper
• A Liquid Chromatography-Mass Spectrometry-based Approach to Characterize the Substrate Specificity of Mammalian Heparanase*

  2014cited by this paper
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  2014cited by this paper
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  2014cited by this paper
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  2013cited by this paper
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  2012cited by this paper
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  2012cited by this paper
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  2012cited by this paper
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  2012cited by this paper
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  2012cited by this paper
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  2012cited by this paper
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  2011influential reference
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  2011cited by this paper
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  2011cited by this paper
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  2010cited by this paper
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  2010cited by this paper
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  2010cited by this paper
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  2010cited by this paper
• Serpins Flex Their Muscle

  2010cited by this paper
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  2009cited by this paper
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  2008cited by this paper
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  2008influential reference
• Serglycin – Structure and biology

  2008cited by this paper
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  2007cited by this paper
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  2007cited by this paper
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  2007cited by this paper
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  2006cited by this paper
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  2005cited by this paper
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  2005cited by this paper
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  2005cited by this paper
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  2005cited by this paper
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  2005cited by this paper
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  2004cited by this paper
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  2004cited by this paper
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  2004cited by this paper
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  2004cited by this paper
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  2004cited by this paper
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  2003cited by this paper
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  2003cited by this paper
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  2003cited by this paper
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  2003cited by this paper
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  2002cited by this paper
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  2002cited by this paper
• The histological localization of heparin in the northern quahog clam, Mercenaria mercenaria.

  2001cited by this paper
• Structural Requirements and Mechanism for Heparin-induced Activation of a Recombinant Mouse Mast Cell Tryptase, Mouse Mast Cell Protease-6

  2001cited by this paper
• Characterization of Unfractionated Heparin: Comparison of Materials from the last 50 Years

  2000cited by this paper
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  2000cited by this paper
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  2000cited by this paper
• Distribution of sulfated glycosaminoglycans in the animal kingdom: widespread occurrence of heparin-like compounds in invertebrates.

  2000cited by this paper
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  1999cited by this paper
• Multiple Isoforms of Heparan Sulfate d-Glucosaminyl 3-O-Sulfotransferase

  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1998cited by this paper
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  1997cited by this paper
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  1996cited by this paper
• The Interaction of Glycosaminoglycans with Heparin Cofactor II

  1994cited by this paper
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  1993cited by this paper
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  1993cited by this paper
• Isolation and characterization of human heparin.

  1992cited by this paper
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  1992cited by this paper
• One explanation of the asthma paradox: inhibition of natural anti-inflammatory mechanism by beta 2-agonists.

  1991cited by this paper
• Proteoglycans in haemopoietic cells.

  1990cited by this paper
• Molecular cloning of a cDNA that encodes the peptide core of a mouse mast cell secretory granule proteoglycan and comparison with the analogous rat and human cDNA.

  1989cited by this paper
• Structure and biology of proteoglycans.

  1988cited by this paper
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  1988cited by this paper
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  1987cited by this paper
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  1986cited by this paper
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  1986cited by this paper
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  1985cited by this paper
• Glycosaminoglycans in rat mucosal mast cells.

  1985cited by this paper
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  1983cited by this paper
• Isolation and characterization of sulphated mucopolysaccharides from rat leukaemic (RBL-1) basophils.

  1980cited by this paper
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  1980cited by this paper
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  1980cited by this paper
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  1977cited by this paper
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