Reticulum Stain Kit

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Reticular fibers also known as reticulin fibers serve as a supportive scaffolding in connective tissues. They primarily consist of type III collagen a protein with a molecular mass that varies but is generally around 300 kDa. These fibers form intricate networks that are abundantly expressed in the extracellular matrix of several organs including the liver lymph nodes and bone marrow. Their unique structure permits a certain degree of flexibility and elasticity offering support to the surrounding cellular components.

Biological function summary

The structural framework provided by reticular fibers supports cellular organization in connective tissue environments. These fibers often associate with other extracellular matrix components such as glycoproteins and proteoglycans to form a complex that enhances the maintenance and resilience of connective tissue. They play an important role in filtering bodily fluids due to presence in lymphoid tissues like the spleen and lymph nodes where they aid in trapping particulates and pathogens.

Pathways

Type III collagen in reticular fibers functions within the complex processes of tissue organization and repair. Specifically they are part of the extracellular matrix pathway which includes interactions with other collagens and matrix metalloproteinases. Another related pathway is the wound healing pathway where type III collagen collaborates with fibronectin and type I collagen to facilitate tissue repair and regeneration.

Associated diseases and disorders

Alterations in reticular fiber networks associate with certain conditions such as liver fibrosis and Ehlers-Danlos syndrome. In liver fibrosis excessive reticular fiber deposition occurs leading to tissue stiffness due to increased type III collagen production. In Ehlers-Danlos syndrome mutations in the genes coding for collagen can disrupt reticular fiber function affecting tissue elasticity and strength. In both conditions changes in other collagens like type I collagen are often observed which further complicate the tissue integrity and contribute to disease pathology.