Identification of IHABP, a 95 kDa intracellular hyaluronate binding protein

Martin Hofmann, Christina Fieber, Volker Assmann, Martin Göttlicher, Jonathan Sleeman, Ria Plug, Norma Howells, Oliver Von Stein, Helmut Ponta, Peter Herrlich

Research output: Contribution to journalArticlepeer-review

74 Scopus citations


The extracellular matrix component hyaluronan is believed to play important roles in various processes of organogenesis, cell migration and cancer. Recognition of and binding to hyaluronan is mediated by cell surface receptors. Three of them, CD44, ICAM-1 and RHAMM (receptor for hyaluronic acid mediated motility), have been identified. A cDNA clone designated RHAMM turned out to possess transforming capacity. Based on this published sequence, we isolated the complete cDNA of the murine gene. The cDNA comprises an open reading frame of 2.3 kb and encodes a 95 kDa protein. The protein carries a hyaluronan binding motif which binds to hyaluronan in vitro but not to heparin or chondroitin sulphate. It is ubiquitously expressed in normal cells and in all tumour cell lines irrespective of their metastatic properties. One tumour cell line, the metastatic Lewis lung carcinoma, expresses a larger 105 kDa variant form of the protein due to a genomic rearrangement. Antibodies raised against the 95 kDa protein were used for subcellular localization studies. The hyaluronan binding protein is not detectable at the cell surface but is rather localized exclusively intracellularly. Clearly, the sequence we have identified encodes a protein with properties substantially different to the RHAMM protein. We tentatively name the protein intracellular hyaluronic acid binding protein, IHABP.

Original languageEnglish
Pages (from-to)1673-1684
Number of pages12
JournalJournal of Cell Science
Issue number12
StatePublished - 1998
Externally publishedYes


  • Hyaluronate
  • Metastasis
  • Receptor


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