File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Two-dimensional liquid chromatography with tandem mass spectrometry-based proteomic characterization of endometrial luminal epithelial surface proteins responsible for embryo implantation

TitleTwo-dimensional liquid chromatography with tandem mass spectrometry-based proteomic characterization of endometrial luminal epithelial surface proteins responsible for embryo implantation
Authors
KeywordsAminopeptidase N
embryo implantation
endometrial surface proteome
integrin-β1
Issue Date2015
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/fertnstert
Citation
Fertility and Sterility, 2015, v. 103 n. 3, p. 853-861.e3 How to Cite?
AbstractOBJECTIVE: To identify endometrial epithelial cell surface proteins essential for blastocysts implantation. DESIGN: Isolation of cell-surface labeled prereceptive (pregnancy day 1) and receptive (pregnancy day 4) mouse endometrial proteins coupled to two-dimensional liquid chromatography with tandem mass spectrometry. SETTING: University research laboratory. ANIMAL(S): Sexually mature female imprinting control region (ICR) mice. INTERVENTION(S): Labeling, purification, and identification of endometrial luminal surface proteins with differentially expressing proteins determined by significant analysis of a microarray algorithm and selected differentially expressed proteins verified by immunohistochemistry and functional assay. MAIN OUTCOME MEASURE(S): Investigation in endometrial luminal surface proteome of prereceptive and receptive endometria of the expression of four of the differentially expressed proteins and functional analysis of aminopeptidase N in a three-dimensional blastocyst-endometrial coculture model. RESULT(S): We identified 104 cell surface proteins from prereceptive and receptive pregnant mouse endometria and found that 27 were statistically significantly up-regulated and 18 were statistically significantly down-regulated in the receptive endometrium. Immunohistochemical analysis of four of the differentially expressed proteins in the endometrium showed concordant results. Functional assay showed that blastocyst attachment was statistically significantly reduced upon inhibition of aminopeptidase N. CONCLUSION(S): The luminal cell surface proteome of the prereceptive and receptive endometria differs, and aminopeptidase N is potentially involved in embryo attachment.
Persistent Identifierhttp://hdl.handle.net/10722/219186
ISSN
2023 Impact Factor: 6.6
2023 SCImago Journal Rankings: 1.858
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYe, T-
dc.contributor.authorPang, TKR-
dc.contributor.authorLeung, ON-
dc.contributor.authorChiu, JF-
dc.contributor.authorYeung, WSB-
dc.date.accessioned2015-09-18T07:16:47Z-
dc.date.available2015-09-18T07:16:47Z-
dc.date.issued2015-
dc.identifier.citationFertility and Sterility, 2015, v. 103 n. 3, p. 853-861.e3-
dc.identifier.issn0015-0282-
dc.identifier.urihttp://hdl.handle.net/10722/219186-
dc.description.abstractOBJECTIVE: To identify endometrial epithelial cell surface proteins essential for blastocysts implantation. DESIGN: Isolation of cell-surface labeled prereceptive (pregnancy day 1) and receptive (pregnancy day 4) mouse endometrial proteins coupled to two-dimensional liquid chromatography with tandem mass spectrometry. SETTING: University research laboratory. ANIMAL(S): Sexually mature female imprinting control region (ICR) mice. INTERVENTION(S): Labeling, purification, and identification of endometrial luminal surface proteins with differentially expressing proteins determined by significant analysis of a microarray algorithm and selected differentially expressed proteins verified by immunohistochemistry and functional assay. MAIN OUTCOME MEASURE(S): Investigation in endometrial luminal surface proteome of prereceptive and receptive endometria of the expression of four of the differentially expressed proteins and functional analysis of aminopeptidase N in a three-dimensional blastocyst-endometrial coculture model. RESULT(S): We identified 104 cell surface proteins from prereceptive and receptive pregnant mouse endometria and found that 27 were statistically significantly up-regulated and 18 were statistically significantly down-regulated in the receptive endometrium. Immunohistochemical analysis of four of the differentially expressed proteins in the endometrium showed concordant results. Functional assay showed that blastocyst attachment was statistically significantly reduced upon inhibition of aminopeptidase N. CONCLUSION(S): The luminal cell surface proteome of the prereceptive and receptive endometria differs, and aminopeptidase N is potentially involved in embryo attachment.-
dc.languageeng-
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/fertnstert-
dc.relation.ispartofFertility and Sterility-
dc.subjectAminopeptidase N-
dc.subjectembryo implantation-
dc.subjectendometrial surface proteome-
dc.subjectintegrin-β1-
dc.titleTwo-dimensional liquid chromatography with tandem mass spectrometry-based proteomic characterization of endometrial luminal epithelial surface proteins responsible for embryo implantation-
dc.typeArticle-
dc.identifier.emailPang, TKR: rtkpang@hku.hk-
dc.identifier.emailLeung, ON: conleung@hku.hk-
dc.identifier.emailYeung, WSB: wsbyeung@hku.hk-
dc.identifier.authorityPang, TKR=rp01761-
dc.identifier.authorityYeung, WSB=rp00331-
dc.identifier.doi10.1016/j.fertnstert.2014.12.110-
dc.identifier.pmid25624195-
dc.identifier.scopuseid_2-s2.0-84961696239-
dc.identifier.hkuros253084-
dc.identifier.volume103-
dc.identifier.issue3-
dc.identifier.spage853-
dc.identifier.epage861.e3-
dc.identifier.isiWOS:000352109000043-
dc.publisher.placeUnited States-
dc.identifier.issnl0015-0282-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats