Cell Adhesion and Signalling Quiz

A network of macromolecules in the extracellular space that helps organize and support tissues.

Tissue composed of tightly packed cells with strong cell-to-cell connections.

Tissue with a large extracellular matrix and fewer tightly packed cells.

The mechanisms by which cells stick to each other and to the extracellular matrix.

Mechanisms that allow cells to attach to each other.

Mechanisms that allow cells to attach to the extracellular matrix.

Cells and ECM structured into specific groupings that determine tissue function.

ECM determines a connective tissue's physical properties, like strength, resilience, and flexibility.

A type of connective tissue with high tensile strength, primarily due to collagen fibrils.

Blood vessel walls are resilient and flexible, containing elastic fibers.

Cartilage combines tensile strength and elasticity, relying on collagen and proteoglycans like aggrecan.

Bone is rigid and incompressible, featuring calcified collagen.

The vitreous content of the eye is a transparent jelly comprised of collagen and hyaluronan.

GAGs are polysaccharide chains often covalently attached to proteins (proteoglycans).

Fibrous proteins like collagen, elastin, and fibrillin form structural components of the ECM.

Proteins and glycosaminoglycans that form the extracellular matrix.

A long GAG with repeating disaccharides. It attracts water and creates space.

A common unit in a GAG chain. Usually an amino sugar & a uronic acid.

The process of assembling proteoglycans, including adding linker and polysaccharide modifications.

Hyaluronan, chondroitin sulfate, dermatan sulfate, heparan sulfate, keratan sulfate are example classes of GAGs.

Two-sugar units that compose long chains of glycosaminoglycans.

Describing certain GAGs that do not have sulfate groups attached.

Shape of GAGs that maximizes space filling in the ECM

A type of collagen that binds to type II collagen fibrils in cartilage, contributing to the tissue's structural integrity.

A type of collagen that binds to type I collagen fibrils in tendons, contributing to the tissue's strength and flexibility.

Fibers composed primarily of elastin, providing resilience and the ability to recoil after stretching. Found in tissues like blood vessels, lungs, and skin.

A hydrophobic protein that forms the main component of elastic fibers. Secreted as tropoelastin, it undergoes cross-linking to create a network of fibers and sheets.

A dimeric protein that acts as a bridge between cells and the ECM. It forms fibrils that provide structural support and contribute to cell adhesion.

Large, complex molecules in the extracellular matrix, composed of a core protein with attached glycosaminoglycan (GAG) chains. These chains can be highly variable in number and type, resulting in diverse proteoglycan structures.

A major proteoglycan found in cartilage, contributing to its resilience and shock-absorbing properties. It has a central protein core with numerous attached chondroitin sulfate and keratan sulfate GAG chains.

A family of fibrous proteins that are the major component of the extracellular matrix. They provide structural support, tensile strength, and organization to tissues.

Individual polypeptide chains that fold into a helix and then assemble into collagen trimers. Each chain has a repeating sequence of glycine, proline, and hydroxyproline, which contributes to its unique structure.

Stable triple helices formed by three collagen -chains. These trimers further assemble into fibrils, which are the primary structural units of collagen.

Bundles of collagen trimers that assemble into larger structures, providing tensile strength and structural support to tissues. They are interconnected by covalent crosslinks between lysines and hydroxylysines.

A group of collagens that form fibrils, contributing to the structural framework of various tissues. They have a characteristic repeating pattern of glycine, proline, and hydroxyproline residues.

Collagens that don't form fibrils themselves but interact with existing fibrils, influencing their organization and interactions with other ECM molecules. They have interrupted triple helices, making them more flexible.

A disease caused by vitamin C deficiency, leading to impaired collagen synthesis and weakening of blood vessels, bones, and connective tissues. This is due to a lack of hydroxyproline, which is essential for collagen stability.