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Biochemistry Connective Tissue

Glycoproteins: Fibronectin, Laminin

Topic overview

Start with the big picture

Fibronectin is a dimeric matrix protein whose RGD motif supports integrin binding and links cells with extracellular components. Produced by fibroblasts and hepatocytes, it can assemble into fibrils as mechanical forces expose sites that guide organization. Its functions include cell adhesion, migration, and wound healing. Laminin is a three-chain protein that forms networks in the basal lamina, binds other matrix components and integrins, and helps establish basement-membrane structure, filtration, and cell polarity. The lesson also introduces laminin-332’s role in keratinocyte anchorage and clinical associations involving laminin-chain mutations. Together, these proteins illustrate how matrix assembly and integrin signaling influence cell behavior, while glycosylation and protein fragments contribute to matrix interactions and responses to injury.

Learning objectives

What you'll learn

  • Compare the structures and principal matrix roles of fibronectin and laminin.
  • Explain how fibronectin binds integrins and assembles into tension-aligned fibrils.
  • Describe laminin’s binding partners and contribution to basement-membrane assembly.
  • Identify the roles of laminin-332 and the stated clinical associations of laminin-chain mutations.
  • Relate integrin engagement and glycosylation to matrix signaling and assembly.
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