The Proteoglycan Aggregate : Structure and Function

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Author(s)

    • WATANABE Hideto
    • Institute for Molecular Science of Medicine, Aichi Medical University
    • MATSUMOTO Kazu
    • Institute for Molecular Science of Medicine, Aichi Medical University
    • KIMATA Koji
    • Institute for Molecular Science of Medicine, Aichi Medical University

Abstract

The proteoglycan aggregate is the major structural component of the extracellular matrix of the cartilage, composed of aggrecan, hyaluronan (HA) and link protein (LP). Cartilage matrix deficiency and LP-null mice demonstrate in vivo roles of the aggregate in cartilage development and homeostasis. Our recent studies demonstrate that PG-M/versican, another member of aggrecan family with a similar domain structure, binds both HA and LP, suggesting the presence of PG-M/versican aggregate. Further functional analyses of domains and subdomains showed that two tandemly repeated B-B' segment interacts with both HA and LP, distinct from aggrecan Gl, whose A subdomain binds to LP. Recently, three other members of LP family have been identified, resulting in total four members, and they are named HAPLNs. Although four members of HAPLNs may exhibit binding specificity to four aggrecan family members, LP (HAPLN-1) interacts with both aggrecan and PG-M/versican, suggesting a more complex manner of aggregate formation.

Journal

  • Connective tissue

    Connective tissue 35(4), 201-205, 2003-12-25

    日本結合組織学会

References:  32

Codes

  • NII Article ID (NAID)
    110003994259
  • NII NACSIS-CAT ID (NCID)
    AN10169901
  • Text Lang
    ENG
  • Article Type
    REV
  • ISSN
    0916572X
  • Data Source
    CJP  NII-ELS  NDL-Digital 
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