Anti-ADAMTSL4 antibody

Supplementary info

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

Activity summary

ADAMTSL4 also known as ADAMTS-like protein 4 is a glycoprotein with a molecular mass approximately 80 kDa. This protein does not contain protease activity but shares structural similarities with the ADAMTS family. It is primarily expressed in ocular tissues including the retina lens and corneal epithelium as well as in heart and skin tissues. The primary structure of ADAMTSL4 lacks the catalytic domain typical of other ADAMTS proteins but retains features important for protein interactions which influence tissue stability and extracellular matrix organization.

Biological function summary

ADAMTSL4 plays a role in maintaining the structural integrity of the extracellular matrix in tissues where it is present. It doesn’t function as part of a complex but contributes to processes that stabilize connective tissues. The protein likely interacts with other extracellular matrix proteins to regulate the proper assembly of microfibrils which are important for tissue strength and elasticity. Disruptions in this function could compromise tissue stability impacting various biological systems.

Pathways

Researchers have identified that ADAMTSL4 interacts within the extracellular matrix organization and elastic fiber formation pathways. In these pathways ADAMTSL4 regulates the assembly and turnover of microfibrillar components alongside proteins like fibrillin-1 and latent transforming growth factor-binding proteins. This ensures the appropriate composition and functionality of fibrillar structures. Understanding these interactions is important for elucidating the molecular mechanisms that maintain connective tissue architecture.

Associated diseases and disorders

Mutations in ADAMTSL4 have a strong link to ocular pathologies such as ectopia lentis and autosomal recessive eye disorders like isolated ectopia lentis. The protein’s dysfunction often involves impaired microfibril formation or maintenance within the eye leading to lens dislocation. The impaired interaction with proteins like fibrillin-1 can exacerbate the displacement of lens fibers further contributing to these conditions. These associations emphasize the need for further study concerning therapeutic interventions targeting ADAMTSL4-related pathways.