27.7
Matrix Proteoglycans and Glycoproteins
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Q1: What is the structural difference between proteoglycans and glycoproteins?
Proteoglycans consist of multiple glycosaminoglycan chains covalently attached to a core protein, while glycoproteins have a protein core covalently attached to oligosaccharide chains. Proteoglycans are typically found in the extracellular matrix and at cell membranes, whereas glycoproteins appear on cell membranes, in the ECM, and in blood.
Q2: How do proteoglycans regulate growth factor signaling in the extracellular matrix?
Proteoglycans with multiple binding sites act as local reservoirs for vascular endothelial growth factors, limiting their diffusion and localizing effects to nearby cells. They also protect signaling proteins from degradation by proteases, allowing growth factors to remain active longer and influence specific cell populations within the dense ECM network.
Q3: Why do proteoglycans absorb water and what is the functional consequence?
Proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water swells the proteoglycan like a water-soaked gel, enabling it to withstand compression forces. This property is especially important in hyaline cartilage, which contains large amounts of proteoglycans dispersed among collagen fibers.
Q4: What role do integrins and fibronectin play in connecting cells to the extracellular matrix?
Integrins are integral proteins that span the cell membrane and serve as cell surface receptors for fibronectin, a glycoprotein in the ECM. Together, fibronectins connect cells with ECM by linking collagen and proteoglycans to integrin proteins, creating a structural bridge that anchors cells to the matrix.
Q5: What functions do laminins serve in the basal lamina?
Laminins are important for cell migration, growth, and differentiation. In association with type IV collagen, laminins form an interconnected network that provides strength and flexibility to the basal lamina. This network supports cellular processes while maintaining structural integrity of the basement membrane.
Q6: How do pathogenic bacteria exploit glycoproteins in the extracellular matrix?
Streptococcus pyogenes, which causes strep throat, attaches to fibronectin present in the extracellular matrix of cells lining the oropharynx. By binding to this glycoprotein, the bacterium can adhere to host tissues and establish infection, demonstrating how pathogens exploit ECM components for cellular attachment.
Q7: What are the multiple roles of glycoproteins in cell recognition and structure?
Glycoproteins such as integrins serve as cell surface receptors and structural attachments for cytoskeleton fibers. They also function as part of the cell's recognition sites, enabling cell-to-cell communication and ECM interactions. These diverse roles make glycoproteins essential for cell adhesion, signaling, and tissue organization.