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The Biochemical journal2001; 356(Pt 2); 369-376; doi: 10.1042/0264-6021:3560369

Uterocalin, a lipocalin provisioning the preattachment equine conceptus: fatty acid and retinol binding properties, and structural characterization.

Abstract: The equine conceptus is surrounded by a fibrous capsule that persists until about day 20 of pregnancy, whereupon the capsule is lost, the conceptus attaches to the endometrium and placentation proceeds. Before attachment, the endometrium secretes in abundance a protein of the lipocalin family, uterocalin. The cessation of secretion coincides with the end of the period during which the conceptus is enclosed in its capsule, suggesting that uterocalin is essential for the support of the embryo before direct contact between maternal and foetal tissues is established. Using recombinant protein and fluorescence-based assays, we show that equine uterocalin binds the fluorescent fatty acids 11-(dansylamino)undecanoic acid, dansyl-D,L-alpha-amino-octanoic acid and cis-parinaric acid, and, by competition, oleic, palmitic, arachidonic, docosahexaenoic, gamma-linolenic, cis-eicosapentaenoic and linoleic acids. Uterocalin also binds all-trans-retinol, the binding site for which is coincident or interactive with that for fatty acids. Molecular modelling and intrinsic fluorescence analysis of the wild-type protein and a Trp-->Glu mutant protein indicated that uterocalin has an unusually solvent-exposed Trp side chain projecting from its large helix directly into solvent. This feature is unusual among lipocalins and might relate to binding to, and uptake by, the trophoblast. Uterocalin therefore has the localization and binding activities for the provisioning of the equine conceptus with lipids including those essential for morphogenesis and pattern formation. The possession of a fibrous capsule surrounding the conceptus might be an ancestral condition in mammals; homologues of uterocalin might be essential for early development in marsupials and in eutherians in which there is a prolonged preimplantation period.
Publication Date: 2001-05-23 PubMed ID: 11368763PubMed Central: PMC1221847DOI: 10.1042/0264-6021:3560369Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research focuses on a protein called uterocalin, a lipocalin family member, which is secreted by the endometrium during the early stages of equine pregnancy. The study investigates how this protein binds to fatty acids and retinol, suggesting a significant role in supporting the developing embryo before it attaches to maternal tissues.

Understanding Uterocalin and its Role

  • The study delves into the role of a protein called uterocalin, greatly secreted by the endometrium before commencing an equine pregnancy. The protein is released during the period when the conceptus (the developing embryo and its surrounding membranes) is surrounded by a fibrous capsule, leading to the hypothesis that uterocalin is crucial before the direct contact between maternal and foetal tissues.
  • The cessation of uterocalin production aligns with the loss of this capsule around day 20 of pregnancy when the conceptus attaches to the endometrium, further illustrating the protein’s role in the preattachment phase.

Uterocalin’s Binding Properties

  • Researchers used recombinant protein and fluorescence-based assays to study how equine uterocalin interacts with certain fluorescent fatty acids and all-trans-retinol. The findings revealed that uterocalin binds to these substances, suggesting the protein’s role in lipid and retinol transportation to the conceptus.
  • The binding site for all-trans-retinol was found to overlap or interact with that for fatty acids, indicating a possible synergistic relationship in lipid provisioning to the embryo.

Structural Characterization of Uterocalin

  • Molecular modelling and intrinsic fluorescence analysis were used to study uterocalin’s structure. Researchers found that the protein has an usually solvent-exposed Trp side chain that projects directly into the solvent from its large helix.
  • This attribute is rare among lipocalins and may be linked to uterocalin’s potential ability to bind to and be taken up by the trophoblast (the layer of cells that form the outer layer of a blastocyst providing nutrients to the embryo and develop into a large part of the placenta).

Implications and Further Studies

  • The study suggests that uterocalin’s localization and binding activities provide essential lipids to the conceptus, vital for morphogenesis (the biological process leading to the development of an organism’s shape) and pattern formation.
  • The researchers propose that the existence of a fibrous capsule around the conceptus could be an ancestral condition in mammals, implying that homologues of uterocalin might be crucial for early development in marsupials and eutherians with extended preimplantation periods.

Cite This Article

APA
Suire S, Stewart F, Beauchamp J, Kennedy MW. (2001). Uterocalin, a lipocalin provisioning the preattachment equine conceptus: fatty acid and retinol binding properties, and structural characterization. Biochem J, 356(Pt 2), 369-376. https://doi.org/10.1042/0264-6021:3560369

Publication

ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 356
Issue: Pt 2
Pages: 369-376

Researcher Affiliations

Suire, S
  • Babraham Institute, Babraham, Cambridge CB2 4AT, UK.
Stewart, F
    Beauchamp, J
      Kennedy, M W

        MeSH Terms

        • Animals
        • Base Sequence
        • Blastocyst / metabolism
        • Carrier Proteins / chemistry
        • Carrier Proteins / genetics
        • Carrier Proteins / metabolism
        • DNA Primers / genetics
        • Fatty Acids / metabolism
        • Female
        • Horses
        • In Vitro Techniques
        • Models, Molecular
        • Molecular Structure
        • Mutagenesis, Site-Directed
        • Pregnancy
        • Protein Conformation
        • Recombinant Proteins / chemistry
        • Recombinant Proteins / genetics
        • Recombinant Proteins / metabolism
        • Spectrometry, Fluorescence
        • Tryptophan / chemistry
        • Vitamin A / metabolism

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        Citations

        This article has been cited 21 times.
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