Literature DB >> 10765973

Subcellular localization of prostaglandin H synthase-2 in a human amnion cell line: implications for nuclear localized prostaglandin signaling pathways.

K W Marvin1, R L Eykholt, M D Mitchell.   

Abstract

We have determined that prostaglandin H synthase-2 localises strongly to the nuclear membrane as well as being found in the endoplasmic reticulum in human amnion-derived WISH cells which have been stimulated with interleukin 1beta and phorbol ester. This is consistent with findings in cells of non-reproductive origin. There is strong evidence that prostaglandin J2 derivatives, which in other tissues exhibit tumour suppressing, antiproliferative and/or differentiation promoting activities, act through binding of intracellular receptors which then enter the nucleus. In addition, some arachidonic acid derivatives are clearly generated by enzymes at the nuclear envelope and localise to sites in nuclei or bind sites in nuclei. The WISH cell line will make an excellent system for studying these perinuclear intracellular prostanoid signaling mechanisms.

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Year:  2000        PMID: 10765973     DOI: 10.1054/plef.1999.0118

Source DB:  PubMed          Journal:  Prostaglandins Leukot Essent Fatty Acids        ISSN: 0952-3278            Impact factor:   4.006


  1 in total

1.  Membrane fluidity is a key modulator of membrane binding, insertion, and activity of 5-lipoxygenase.

Authors:  Abhay H Pande; Shan Qin; Suren A Tatulian
Journal:  Biophys J       Date:  2005-03-18       Impact factor: 4.033

  1 in total

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