Localisation of bradykinin-like immunoreactivity and modulation of bradykinin-evoked phospholipase d activity by 17βoestradiol in human endometrium

Research output: Contribution to journalArticle


Colleges, School and Institutes

External organisations

  • Reproductive Physiopathology Group
  • Department of Obstetrics and Gynaecology
  • University of Cambridge
  • Signalling Group


Bradykinin may act as a promoter of endometrial regeneration. Bradykinin-like immunoreactivity was detected immunocytochemically in the glandular epithelium and stroma of human endometrium. The staining was localized around the stroma and especially in the cells undergoing mitosis. Relatively weak staining was seen in the stromal cells of secretory endometrium, which was predominantly localised around the basal vacuoles of endometrial glands. During the late secretory phase, the intensity of staining was diminished throughout the endometrium: the glandular epithelium showed weak staining and stroma appeared negative. As phosphatidate, the product of phospholipase D pathway, may mediate cell proliferation, the effect of 17βoestradiol on bradykinin-evoked phospholipase D activity assayed as accumulation of [3H]phosphatidylbutanol ([3H]PtdBut) was examined in [3H]myristic acid-labelled primary cultures of human endometrial stromal cells. Bradykinin induced a rapid accumulation of [3H]PtdBut in a time-dependent manner, indicating phospholipase D activation. Pretreatment of stromal cells with 17βoestradiol enhanced the bradykinin-evoked phospholipase D activity. These results suggest that bradykinin-like immunoreactivity is strongly associated with proliferative stromal cells undergoing mitosis, a process that may be mediated by phospholipase D activation as the magnitude of this enzyme's activation in vitro appears to be regulated by 17βoestradiol.


Original languageEnglish
Pages (from-to)203-209
Number of pages7
JournalGrowth Factors
Issue number3
Publication statusPublished - 1 Jan 1995


  • Bradykinin, Endometrium, Oestrogen, Phospholipase D. proliferation