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Fibronectins pp 176-199 | Cite as

Biosynthesis and Fibrillogenesis

  • Richard O. Hynes
Part of the Springer Series in Molecular Biology book series (SSMOL)

Abstract

FN is a large and complex glycoprotein with extensive intramolecular and intermolecular disulfide bonding (Chapter 6). It is both a secreted protein and a fibrillar matrix protein (Chapter 4) and in the latter situation, interacts with other macromolecules. The production and secretion of FN and the formation of FN-rich matrices are, therefore, complex problems of some intrinsic interest. In addition, these processes are all potentially sites of regulation and/or perturbation of FN structure and function, e.g., during normal cellular growth and differentiation (Chapters 10 and 11), oncogenic transformation (Chapter 12), or inflammatory processes (Chapter 14). In this chapter I will discuss the processes of synthesis, posttranslational modification, secretion and fibrillogenesis of FN, and some aspects of the regulation of these processes in cultured cells.

Keywords

Hyaluronic Acid Rough Endoplasmic Reticulum Human Skin Fibroblast Extracellular Matrice High Molecular Weight Complex 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag New York Inc. 1990

Authors and Affiliations

  • Richard O. Hynes
    • 1
  1. 1.Department of Biology Massachusetts Institute of TechnologyHoward Hughes Medical Institute and Center for Cancer ResearchCambridgeUSA

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