Literature DB >> 8349827

Glycosylation-dependent cell adhesion molecule 1 (GlyCAM 1) mucin is expressed by lactating mammary gland epithelial cells and is present in milk.

D Dowbenko1, A Kikuta, C Fennie, N Gillett, L A Lasky.   

Abstract

Glycosylation-dependent cell adhesion molecule 1 (GlyCAM 1) is a mucinlike endothelial glycoprotein that acts as an adhesive ligand for L selectin by presenting one or more O-linked carbohydrates to the lectin domain of this leukocyte cell surface selectin. The GlyCAM 1 glycoprotein has been previously shown to be expressed specifically by the endothelial cells of peripheral and mesenteric lymph nodes and in an unknown site in lung. Here we report that this protein is also expressed during lactation by mammary epithelial cells. Northern blot analysis has shown that the mRNA for GlyCAM 1 appears to be induced during pregnancy in a manner similar to that previously described for hormonally induced milk proteins. In situ hybridization analysis reveals that the site of GlyCAM 1 synthesis in the mammary gland is in the epithelial cells that produce these same milk proteins. Immunohistochemistry of mammary glands using antisera directed against GlyCAM 1 peptides demonstrates that these epithelial cells contain GlyCAM 1 protein, and that this protein is also found lumenally in the milk of the secreting mammary gland. Analysis of murine milk shows that immunoreactive GlyCAM 1 is found in the soluble whey fraction. Finally, labeling analysis of milk GlyCAM 1 has demonstrated that this form of the glycoprotein lacks the sulfate-modified carbohydrate that has recently been shown to be required for the ligand binding activity to L selectin. The nonsulfated mammary GlyCAM 1 is unable to interact with L selectin, consistent with the hypothesis that milk GlyCAM 1 has a different function than endothelial GlyCAM 1. These data thus suggest that milk GlyCAM 1 is a hormonally regulated milk protein that is part of the milk mucin complex. In addition, the finding that the mammary form of GlyCAM 1 contains different carbohydrate modifications than the endothelial form suggests that this glycoprotein may be a scaffold for carbohydrates that mediate functions in addition to cell adhesion.

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Year:  1993        PMID: 8349827      PMCID: PMC294935          DOI: 10.1172/JCI116671

Source DB:  PubMed          Journal:  J Clin Invest        ISSN: 0021-9738            Impact factor:   14.808


  41 in total

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3.  Sialic acid glycoproteins inhibit in vitro and in vivo replication of rotaviruses.

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Journal:  J Biochem       Date:  1987-01       Impact factor: 3.387

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Authors:  D E Greenwalt; I H Mather
Journal:  J Cell Biol       Date:  1985-02       Impact factor: 10.539

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Authors:  H M Florman; P M Wassarman
Journal:  Cell       Date:  1985-05       Impact factor: 41.582

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  13 in total

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5.  Structure of the O-glycopeptides isolated from bovine milk component PP3.

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Authors:  S V Onrust; P M Hartl; S D Rosen; D Hanahan
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7.  The host defense proteome of human and bovine milk.

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8.  Sialomucin CD34 is the major L-selectin ligand in human tonsil high endothelial venules.

Authors:  K D Puri; E B Finger; G Gaudernack; T A Springer
Journal:  J Cell Biol       Date:  1995-10       Impact factor: 10.539

9.  Human vascular adhesion protein 1 (VAP-1) is a unique sialoglycoprotein that mediates carbohydrate-dependent binding of lymphocytes to endothelial cells.

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10.  Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin.

Authors:  A Bistrup; S Bhakta; J K Lee; Y Y Belov; M D Gunn; F R Zuo; C C Huang; R Kannagi; S D Rosen; S Hemmerich
Journal:  J Cell Biol       Date:  1999-05-17       Impact factor: 10.539

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