Literature DB >> 3416017

Identification and characterization of the pulmonary alveolar type II cell Maclura pomifera agglutinin-binding membrane glycoprotein.

B C Marshall1, M F Joyce-Brady, J S Brody.   

Abstract

The lectin Maclura pomifera agglutinin (MPA) binds to the apical surface of pulmonary alveolar type II but not type I cells. We show that MPA binds to a single membrane glycoprotein in type II cells with a molecular mass of 230 kDa in the rabbit and 200 kDa in the rat. The glycoprotein has an abundance of terminal N-acetylgalactosamine residues. It is a hydrophilic integral membrane protein suggesting that it has an extensive extramembrane domain or is an ion channel. The glycoprotein is similar in rat and rabbit, with the exception that the rat glycoprotein is partially sialylated and is trypsin sensitive. The MPA-binding glycoprotein represents a new integral membrane marker of the apical domain of the pulmonary alveolar type II cell.

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Year:  1988        PMID: 3416017     DOI: 10.1016/0304-4165(88)90091-8

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Comparison of the Maclura pomifera lectin-binding glycoprotein in late fetal and adult rat lung.

Authors:  M J Kresch; J Lwebuga-Mukasa; C M Wilson; I Gross
Journal:  Lung       Date:  1991       Impact factor: 2.584

2.  Immuno- and lectin histochemistry of epithelial subtypes and their changes in a radiation-induced lung fibrosis model of the mini pig.

Authors:  M Kasper; T Rudolf; R Hahn; I Peterson; M Müller
Journal:  Histochemistry       Date:  1993-11
  2 in total

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