Hyaluronan-Binding Proteoglycans

Edward N. Harris, Paul H. Weigel

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Scopus citations

Abstract

Molecular components of the extracellular matrix (ECM) are critical for matrix stabilization, cellular differentiation, and tissue morphogenesis. Once thought to function only as the extracellular glue that primarily binds cells together, proteoglycans in the ECM carry out a diverse array of activities and can be grouped into fi ve functionally based families: (i) hyalectins (lecticans), which contain lectin-like carbohydrate-recognition domains (CRDs) and bind hyaluronan (HA); (ii) heparan sulfate (HS) proteoglycans that sequester growth factors via their HS chains; (iii) small leucine-rich proteoglycans (SLRPs) containing leucine-rich domains that interact with collagens and other ECM proteins; (iv) phosphacans that function primarily as receptor-like protein-tyrosine phosphatases; and (v) part-time proteoglycans that reside both on the cell surface and in the ECM. More than 40 cDNAs encoding proteoglycan core proteins have been discovered thus far [1]. For the sake of brevity, this chapter will focus only on the four lecticans that bind HA (Figure 15.1): Aggrecan, neurocan, brevican, and versican.

Original languageEnglish (US)
Title of host publicationAnimal Lectins
Subtitle of host publicationA Functional View
PublisherCRC Press
Pages223-231
Number of pages9
ISBN (Electronic)9781420006971
ISBN (Print)9780849372698
DOIs
StatePublished - Jan 1 2008
Externally publishedYes

ASJC Scopus subject areas

  • General Medicine
  • General Immunology and Microbiology

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