Distribution and immunoelectron microscopic localization of laminin, a noncollagenous basement membrane glycoprotein

J. M. Foidart, E. W. Bere, M. Yaar, S. I. Rennard, M. Gullino, G. R. Martin, S. I. Katz

Research output: Contribution to journalArticle

368 Scopus citations

Abstract

Laminin is a noncollagenous glycoprotein isolated from a transplantable mouse tumor producing basement membrane (BM). Purified antibodies to laminin do not cross-react with other known BM antigens including type IV collagen, fibronectin, bullous pemphigoid antigen, and a BM proteoglycan. Using immunofluorescence, laminin is localized in the BM zones of those human, chick, guinea pig, bovine, monkey, rat, and mouse tissues examined. Epithelial and endothelial cells in culture synthesize laminin while mesenchymal cells do not. By immunoelectron microscopy, laminin was localized to the lamina lucida of human epidermal BM and of mouse esophagus epithelial BM. The wide distribution of laminin among diverse tissues and species, and in early stages of embryonic development, suggests that laminin is a ubiquitous component of basement membranes.

Original languageEnglish (US)
Pages (from-to)336-342
Number of pages7
JournalLaboratory Investigation
Volume42
Issue number3
StatePublished - 1980

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Distribution and immunoelectron microscopic localization of laminin, a noncollagenous basement membrane glycoprotein'. Together they form a unique fingerprint.

  • Cite this

    Foidart, J. M., Bere, E. W., Yaar, M., Rennard, S. I., Gullino, M., Martin, G. R., & Katz, S. I. (1980). Distribution and immunoelectron microscopic localization of laminin, a noncollagenous basement membrane glycoprotein. Laboratory Investigation, 42(3), 336-342.