Absence of cell-surface annexin V is accompanied by defective collagen matrix binding in the swarm rat chondrosarcoma

Karen B. King, Susan Chubinskaya, David L. Reid, Lawrence H. Madsen, Juergen Mollenhauer

Research output: Contribution to journalArticlepeer-review


Annexin V has been characterized as a major collagen type II binding cell-surface component of normal chondrocytes and is also called anchorin CII in chondrogenic populations. Herein we present evidence that in vitro cultured Swarm rat chondrosarcoma cells are not capable of binding collagen type II in significant quantities to their surfaces, as compared to normal rat chondrocytes. This finding coincides with a deficiency of annexin V on the surface of these cells. A small quantity of an intracellular polypeptide could be detected which is immunologically crossreactive with annexin V but displayed a mobility in SDS-PAGE of less than 34 kD compared to the M(r) 36 kD of intact rat annexin V. By immunohistochemistry the protein could be localized in the cytoplasm of in vitro and in vivo grown tumor cells. By reverse transcription polymerase chain reaction and Northern blot analysis, a regular-sized mRNA for annexin V could be detected in the chondrosarcoma cells that is expressed in only slightly lower quantifies than in normal chondrocytes. Taken together, the data suggest a modified processing or turnover for annexin V in the chondrosarcoma excluding it from being a functionally active collagen type II binding protein. The findings support the hypothesis of cell-surface annexin V as a key component for the formation of the pericellular matrix of chondrocytes.

Original languageEnglish (US)
Pages (from-to)131-144
Number of pages14
JournalJournal of Cellular Biochemistry
Issue number2
StatePublished - May 1997
Externally publishedYes


  • annexin V
  • cell surface
  • chondrocytes
  • chondrosarcoma
  • extracellular matrix

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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