Association of the Src homology 2 domain-containing inositol 5′ phosphatase (SHIP) to releasability in human basophils

Susan M. MacDonald, Becky M. Vonakis

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


During the study of the biology of the Human recombinant Histamine Releasing Factor (HrHRF), we uncovered a hyperreleasable phenotype of basophils from HrHRF-responder donors. Basophils from these donors released histamne to HrHRF, IL-3 and D2O. While there has been a significant amount of work elucidating signal transduction events in human basophils, the reason for this hyperreleasable phenotype remained illusive. A clue to the releasability of these highly allergic, asthmatic HrHRF-responder donor basophils was demonstrated in studies using SHIP knockout mice. Bone marrow-derived mast cells from the SHIP knockout mice demonstrated hyperreleasability to stimuli through the IgE receptor and alteration of subsequent signal transduction events. We have demonstrated a highly significant negative correlation between the amount of SHIP protein per cell equivalent and maximum histamine release to HrHRF. These results provide a clue to the hyperreleasable phenotype and implicate SHIP as an additional regulator of secretion in human basophils.

Original languageEnglish (US)
Pages (from-to)1323-1327
Number of pages5
JournalMolecular Immunology
Issue number16-18
StatePublished - 2002


  • Human Recombinant Histamine Releasing Factor (HrHRF)
  • Human basophils
  • Releasability
  • Src homology 2 domain-containing 5′ phosphatase (SHIP)

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology


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