Human placenta β-galactoside-binding lectin. Purification and some properties

A full-length cDNA clone for the 14 kDa soluble beta-galactoside-binding lectin of man has been isolated from a cDNA library from HepG2 hepatoma cells. The derived amino acid sequence is identical with that of the 14 kDa lectin from human placenta. The results of Northern and Southern blotting of several different human cell lines using a cDNA probe for the 14 kDa lectin suggest the presence of a single gene for this protein. Thus, although there are multiple proteins in the range 14-200 kDa which are antigenically related to this lectin, we would conclude from the present study that there is only one gene for the 14 kDa lectin.

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Heparin-binding lectin from human placenta: further characterization of ligand binding and structural properties and its relationship to histones and heparin-binding growth factors

Biochemistry ◽

10.1021/bi00215a009 ◽

1991 ◽

Vol 30 (1) ◽

pp. 55-65 ◽

Cited By ~ 29

Author(s):

Beatrix Kohnke-Godt ◽

Hans Joachim Gabius

Keyword(s):

Growth Factors ◽

Ligand Binding ◽

Structural Properties ◽

Human Placenta ◽

Heparin Binding ◽

Heparin Binding Growth Factors ◽

Binding Lectin

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Heparin-binding lectin from human placenta: purification and partial molecular characterization and its relationship to basic fibroblast growth factors

Biochemistry ◽

10.1021/bi00442a001 ◽

1989 ◽

Vol 28 (16) ◽

pp. 6531-6538 ◽

Cited By ~ 27

Author(s):

Beatrix Kohnke-Godt ◽

Hans Joachim Gabius

Keyword(s):

Growth Factors ◽

Molecular Characterization ◽

Human Placenta ◽

Fibroblast Growth Factors ◽

Fibroblast Growth ◽

Heparin Binding ◽

Binding Lectin

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

Biochemistry and Cell Biology ◽

10.1139/o90-113 ◽

1990 ◽

Vol 68 (4) ◽

pp. 790-795 ◽

Cited By ~ 3

Author(s):

Howard Ceri ◽

Wei Sek Hwang ◽

Helen Cheung

Keyword(s):

Human Placenta ◽

First Trimester ◽

Cross Reactivity ◽

Developmental Expression ◽

Rat Tissues ◽

Heparin Binding ◽

Placental Development ◽

Lectin Activity ◽

Heparin Affinity ◽

Binding Lectin

Human placental extracts contain a herapin-inhibitable lectin activity. The lectin, which closely resembles those from chicken and rat tissues, was purified by heparin-affinity chromatography. It shares many properties with the previously reported lectins, including hapten specificity, molecular weight of monomers, and immunological cross-reactivity. Sections from different stages of placental development, stained by immunohistochemistry procedures using lectin-specific antibody, showed that the lectin was initially present only in cytotrophoblasts of early first trimester villi. Later in the first trimester, both cytotrophoblasts and syncytiotrophoblasts were stained positively for lectin. From second trimester to term, the lectin was seen only in syncytiotrophoblasts.Key words: lectin, human placenta, development, heparin, cytotrophoblast, syncytiotrophoblast.

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