Question 1

What are Ig-domains and how do they enable Ig-CAM function?

Accepted Answer

Ig-domains are characteristic immunoglobulin protein folds found in multiple extracellular binding domains of Ig-CAMs. These domains allow Ig-CAMs to function diversely across different tissue types by mediating both homophilic interactions, where Ig-CAMs bind to identical molecules, and heterophilic interactions, where they bind to different ligands like integrins. This structural versatility enables Ig-CAMs to perform varied roles in cell adhesion and signaling.

Question 2

How do NCAMs facilitate neural development through homophilic interactions?

Accepted Answer

Neural CAMs, or NCAMs, expressed on neurons bind to each other via their Ig-domains to form homophilic interactions. These interactions activate signaling pathways during neuronal differentiation and direct contact-dependent processes such as axon and dendrite growth. NCAMs continue to maintain neural connections crucial for learning and memory formation throughout life.

Question 3

What is the role of Ig-CAMs in leukocyte recruitment during immune responses?

Accepted Answer

During immune responses, vascular endothelium expresses VCAMs and ICAMs, which are Ig-CAMs that bind integrins on leukocyte surfaces through heterophilic interactions. As leukocytes slow via selectin-mediated interactions, their surface integrins become activated and firmly bind these Ig-CAMs, triggering signaling cascades. This process enables leukocytes to pass between endothelial cells and reach target tissues.

Question 4

How do Ig-CAMs differ from other cell adhesion molecules in forming junctions?

Accepted Answer

While most Ig-CAMs mediate transient cell adhesion, the nectin class of Ig-CAMs forms stable junctions such as adherens junctions in conjunction with other cell adhesion molecules. This distinction reflects the versatility of Ig-CAMs, which can function in both temporary cell-cell contacts and permanent structural connections depending on their molecular class and associated proteins.

Question 5

Why are Ig-CAMs important markers in cancer pathology?

Accepted Answer

Many cancers including myeloid leukemia, pheochromocytoma, and Wilm's tumor stain positive for NCAM2, making it a valuable diagnostic marker in pathology. Cancer cells exploit the leukocyte recruitment mechanisms mediated by Ig-CAMs during metastasis to infiltrate new sites and form secondary tumors. This hijacking of normal Ig-CAM functions demonstrates how cancer cells misuse cell adhesion pathways.

Question 6

How do viruses use Ig-CAMs to enter host cells?

Accepted Answer

Some Ig-CAMs function as receptors for viral entry into host cells. The rabies virus and human rhinovirus are examples of pathogens that utilize Ig-CAMs as entry points. This viral exploitation of Ig-CAM receptors highlights how cell surface adhesion molecules can be repurposed by infectious agents to establish infection.

Question 7

What structural features make Ig-CAMs versatile across different tissue types?

Accepted Answer

Ig-CAMs possess characteristic immunoglobulin protein domains and other domains such as fibronectin type III domains, with varying degrees of glycosylation across different Ig-CAMs. This structural diversity enables them to exhibit either homophilic or heterophilic binding and perform diverse functions including cell adhesion, signaling, development, and infection across neural, vascular, and immune tissues.

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