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Related Experiment Videos

Endogenous heparin-binding lectin activity in human placenta: purification and developmental expression.

H Ceri1, W S Hwang, H Cheung

  • 1Department of Biology, University of Calgary, Alta., Canada.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|April 1, 1990
PubMed
Summary

Human placental extracts contain a heparin-inhibitable lectin. This protein, found in various placental cells, changes location during pregnancy, indicating its dynamic role in human placenta development.

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Area of Science:

  • Biochemistry
  • Reproductive Biology
  • Cell Biology

Background:

  • Human placental extracts exhibit heparin-inhibitable lectin activity.
  • This lectin shares characteristics with lectins found in chicken and rat tissues.

Purpose of the Study:

  • To purify and characterize the heparin-inhibitable lectin from human placental extracts.
  • To investigate the localization and expression of this lectin during different stages of human placental development.

Main Methods:

  • Heparin-affinity chromatography was used for lectin purification.
  • Immunohistochemistry with lectin-specific antibodies was employed to determine lectin distribution in placental tissues.

Main Results:

  • The purified lectin demonstrated properties consistent with previously reported lectins, including hapten specificity, monomer molecular weight, and immunological cross-reactivity.

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  • Lectin expression was observed in cytotrophoblasts in early first trimester villi.
  • Later in gestation, the lectin was found in both cytotrophoblasts and syncytiotrophoblasts, and by the second trimester to term, it was localized exclusively to syncytiotrophoblasts.

    • Conclusions:

    • The human placental lectin is a distinct entity with conserved properties.
    • The dynamic expression pattern of this lectin suggests a significant role in human placental development and function.