Related Experiment Videos
The EMILIN protein family
A Colombatti1, R Doliana, S Bot
1Divisione di Oncologia Sperimentale 2, CRO-IRCCS, 33081, Aviano, Italy.acolombatti@ets.it
Summary
Extracellular matrix glycoproteins, EMILINs, were identified and characterized. EMILIN-1 acts as an efficient ligand, promoting cell adhesion.
Area of Science:
- Biochemistry
- Molecular Biology
- Extracellular Matrix Research
Background:
- The Extracellular Matrix (ECM) contains glycoproteins like EMILINs.
- EMILINs are associated with elastin and microfibrils in various tissues.
- EMILINs possess unique structural domains, including a gC1q globular domain.
Purpose of the Study:
- To isolate and characterize novel EMILIN family members.
- To elucidate the structural features and functional properties of EMILINs.
- To investigate the role of EMILIN-1 in cell adhesion.
Main Methods:
- Isolation of chicken and human EMILIN cDNAs using RT/PCR.
- Yeast two-hybrid system to identify EMILIN-2.
- Characterization of EMILIN structure and function using recombinant proteins.
- Gene mapping of EMILIN-1.
Main Results:
- EMILIN-1 and EMILIN-2 were identified and their cDNAs isolated.
- EMILINs exhibit a conserved domain structure: gC1q, collagenous, coiled-coil, and cysteine-rich N-terminal domains.
- EMILIN-1's gC1q domain forms homotrimers and multimeric assemblies.
- Recombinant EMILIN-1 effectively mediates cell adhesion.
Conclusions:
- EMILINs represent a distinct family of ECM glycoproteins.
- EMILIN-1's structural features facilitate self-assembly and ligand activity.
- EMILIN-1 plays a significant role in cell adhesion processes.