Recombinant Human EMILIN1 protein

Supplementary information

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

EMILIN1 also known as elastin microfibril interface located protein 1 is a glycoprotein that plays a role in the extracellular matrix. The protein has a molecular mass of approximately 120 kDa. It is expressed in several tissues with high levels observed in vascular tissues skin and other connective tissues. EMILIN1 interacts with other matrix proteins which helps maintain the structural integrity of tissues.

Biological function summary

EMILIN1 contributes to maintaining elastogenesis and modulating cell adhesion by interacting with integrins. It forms part of the extracellular matrix where it supports elastin fibers which gives elasticity to tissues. EMILIN1 also influences cell behavior by modulating the signaling pathways through its binding to integrins. The proper function of EMILIN1 is important for tissue elasticity and cell migration.

Pathways

EMILIN1 is integral to the Notch signaling and TGF-β pathways. It interacts with Notch receptors affecting cell differentiation and proliferation. Additionally its interplay with TGF-β signaling regulates extracellular matrix organization and angiogenesis. These connections link EMILIN1 to proteins like TGF-β and Notch receptors highlighting its role in maintaining cellular and tissue homeostasis.

Defects or altered expression of EMILIN1 have been implicated in cardiovascular diseases and skin disorders. It has connections to proteins such as integrins and TGF-β which are also involved in these conditions. In cardiovascular disorders EMILIN1 dysfunction can lead to improper vessel formation and elasticity contributing to hypertension and atherosclerosis. Skin disorders involving EMILIN1 may present as conditions with compromised elastic fiber architecture such as cutis laxa.