dc.contributor.author
Blois, Sandra M.
dc.contributor.author
Dveksler, Gabriela
dc.contributor.author
Vasta, Gerardo R.
dc.contributor.author
Freitag, Nancy
dc.contributor.author
Blanchard, Véronique
dc.contributor.author
Barrientos, Gabriela
dc.date.accessioned
2019-08-02T11:42:08Z
dc.date.available
2019-08-02T11:42:08Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/25210
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-3915
dc.description.abstract
Galectins are a phylogenetically conserved family of soluble beta-galactoside binding proteins, consisting of 15 different types, each with a specific function. Galectins contribute to placentation by regulating trophoblast development, migration, and invasion during early pregnancy. In addition, galectins are critical players regulating maternal immune tolerance to the embedded embryo. Recently, the role of galectins in angiogenesis during decidualization and in placenta formation has gained attention. Altered expression of galectins is associated with abnormal pregnancies and infertility. This review focuses on the role of galectins in pregnancy-associated processes and discusses the relevance of galectin-glycan interactions as potential therapeutic targets in pregnancy disorders.
en
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
placentation
en
dc.subject
preeclampsia
en
dc.subject.ddc
600 Technik, Medizin, angewandte Wissenschaften::610 Medizin und Gesundheit::610 Medizin und Gesundheit
dc.title
Pregnancy Galectinology: Insights Into a Complex Network of Glycan Binding Proteins
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.articlenumber
1166
dcterms.bibliographicCitation.doi
10.3389/fimmu.2019.01166
dcterms.bibliographicCitation.journaltitle
Frontiers in Immunology
dcterms.bibliographicCitation.originalpublishername
Frontiers Media S.A.
dcterms.bibliographicCitation.volume
10
refubium.affiliation
Charité - Universitätsmedizin Berlin
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.bibliographicCitation.pmid
31231368
dcterms.isPartOf.eissn
1664-3224