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Cell Membrane Vesicles as a Tool for the Study of Direct Epithelial–Stromal Interaction: Lessons from CD147

  • Eric Gabison
  • Farah Khayati
  • Samia Mourah
  • Suzanne Menashi
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1066)

Abstract

Communication between the epithelial and stromal tissue layers, separated by basement membrane, is known to provide the information necessary for development, differentiation, and homeostasis. These interactions are altered in benign or malignant diseases, in particular when the basement membrane barrier is disrupted allowing a greater proximity between the two cell layers that triggers tissue remodeling. Epithelial–stromal interactions (ESI) have been examined in vitro by various approaches that can be broadly divided into interactions arising from secreted diffusible factors and interactions through direct cell–cell contact. Here we describe a method for the study of direct ESI through CD147, an adhesion molecule present on the epithelial cell surface and which is known to interact with stromal cells, such as fibroblasts and endothelial cells, and signal them to increase production of matrix metalloproteinases. This method can be extended to other adhesion molecules involved in ESI.

Key words

Tumor–stroma interactions CD147 Membrane vesicles Stromal cells Epithelial cells 

References

  1. 1.
    Biswas C, Zhang Y, DeCastro R et al (1995) The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. Cancer Res 55:434–439PubMedGoogle Scholar
  2. 2.
    Gabison EE, Hoang-Xuan T, Mauviel A et al (2005) EMMPRIN/CD147, an MMP modulator in cancer, development and tissue repair. Biochimie 87:361–368PubMedCrossRefGoogle Scholar
  3. 3.
    Kataoka H, DeCastro R, Zucker S et al (1993) Tumor cell-derived collagenase-stimulatory factor increases expression of interstitial collagenase, stromelysin, and 72-kDa gelatinase. Cancer Res 53:3154–3158PubMedGoogle Scholar
  4. 4.
    Caudroy S, Polette M, Tournier JM et al (1999) Expression of the extracellular matrix metalloproteinase inducer (EMMPRIN) and the matrix metalloproteinase-2 in bronchopulmonary and breast lesions. J Histochem Cytochem 47:1575–1580PubMedCrossRefGoogle Scholar
  5. 5.
    Gabison EE, Huet E, Baudouin C et al (2009) Direct epithelial-stromal interaction in corneal wound healing: role of EMMPRIN/CD147 in MMPs induction and beyond. Prog Retin Eye Res 28:19–33PubMedCrossRefGoogle Scholar
  6. 6.
    Gabison EE, Mourah S, Steinfels E et al (2005) Differential expression of extracellular matrix metalloproteinase inducer (CD147) in normal and ulcerated corneas: role in epithelio-stromal interactions and matrix metalloproteinase induction. Am J Pathol 166:209–219PubMedCrossRefGoogle Scholar
  7. 7.
    Huet E, Vallee B, Szul D et al (2008) Extracellular matrix metalloproteinase inducer/CD147 promotes myofibroblast differentiation by inducing alpha-smooth muscle actin expression and collagen gel contraction: implications in tissue remodeling. FASEB J 22:1144–1154PubMedCrossRefGoogle Scholar
  8. 8.
    Miyauchi T, Masuzawa Y, Muramatsu T (1991) The basigin group of the immunoglobulin superfamily: complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen. J Biochem 110:770–774PubMedGoogle Scholar
  9. 9.
    Fadool JM, Linser PJ (1996) Evidence for the formation of multimeric forms of the 5A11/HT7 antigen. Biochem Biophys Res Commun 229:280–286PubMedCrossRefGoogle Scholar
  10. 10.
    Yoshida S, Shibata M, Yamamoto S et al (2000) Homo-oligomer formation by basigin, an immunoglobulin superfamily member, via its N-terminal immunoglobulin domain. Eur J Biochem 267:4372–4380PubMedCrossRefGoogle Scholar
  11. 11.
    Bougatef F, Menashi S, Khayati F et al (2010) EMMPRIN promotes melanoma cells malignant properties through a HIF-2alpha mediated up-regulation of VEGF-receptor-2. PLoS One 5:e12265PubMedCrossRefGoogle Scholar
  12. 12.
    Bougatef F, Quemener C, Kellouche S et al (2009) EMMPRIN promotes angiogenesis through hypoxia-inducible factor-2alpha-mediated regulation of soluble VEGF isoforms and their receptor VEGFR-2. Blood 114: 5547–5556PubMedCrossRefGoogle Scholar
  13. 13.
    Vishwanath M, Ma L, Otey CA et al (2003) Modulation of corneal fibroblast contractility within fibrillar collagen matrices. Invest Ophthalmol Vis Sci 44:4724–4735PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, New York 2013

Authors and Affiliations

  • Eric Gabison
    • 1
  • Farah Khayati
    • 2
  • Samia Mourah
    • 2
  • Suzanne Menashi
    • 3
  1. 1.Univ Paris Diderot and Fondation A. de RothschildParisFrance
  2. 2.Laboratoire de Pharmacologie and INSERM U940Hôpital Saint- LouisParisFrance
  3. 3.CNRS EAC 7149, Faculté des SciencesUniversité Paris-Est CréteilCréteilFrance

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