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Polydom: a secreted protein with pentraxin, complement control protein, epidermal growth factor and von Willebrand
D Gilgès1, M A Vinit, I Callebaut
1INSERM U474, maternité Port-Royal, 123 Bld de Port-Royal 75014 Paris, France.
Abstract:
To identify extracellular proteins with epidermal growth factor (EGF) domains that are potentially involved in the control of haemopoiesis, we performed degenerate reverse-transcriptase-mediated PCR on the murine bone-marrow stromal cell line MS-5 and isolated a new partial cDNA encoding EGF-like domains related to those in the Notch proteins. Cloning and sequencing of the full-length cDNA showed that it encoded a new extracellular multi-domain protein that we named polydom. This 387 kDa mosaic protein contained a signal peptide followed by a new association of eight different protein domains, including a pentraxin domain and a von Willebrand factor type A domain, ten EGF domains, and 34 complement control protein modules. The human polydom mRNA is strongly expressed in placenta, its expression in the other tissues being weak or undetectable. The particular multidomain structure of the encoded protein suggests an important biological role in cellular adhesion and/or in the immune system.
Insights
Researchers identified polydom, a novel 387 kDa extracellular protein with multiple domains including epidermal growth factor (EGF) domains, potentially involved in hematopoiesis and the immune system.
Area of Science:
- Molecular Biology
- Immunology
- Cell Biology
Background:
- Extracellular proteins with epidermal growth factor (EGF) domains are implicated in regulating hematopoiesis.
- Understanding novel proteins involved in these processes is crucial for advancing research in cell biology and immunology.
Purpose of the Study:
- To identify novel extracellular proteins with EGF domains involved in the control of hematopoiesis.
- To characterize the structure and potential function of newly discovered proteins.
Main Methods:
- Degenerate reverse-transcriptase-mediated PCR was used on murine bone-marrow stromal cell line MS-5.
- Full-length cDNA cloning and sequencing were performed to identify and characterize the novel protein.
Main Results:
- A new partial cDNA encoding EGF-like domains was isolated, leading to the identification of the full-length cDNA for a novel protein named polydom.
- Polydom is a 387 kDa mosaic protein featuring a signal peptide and a unique combination of eight domains, including pentraxin, von Willebrand factor type A, ten EGF domains, and 34 complement control protein modules.
- Human polydom mRNA shows strong expression in the placenta, with weak or undetectable expression in other tissues.
Conclusions:
- The unique multidomain structure of polydom suggests significant roles in cellular adhesion and/or the immune system.
- Further research into polydom's function could provide insights into hematopoiesis, cellular adhesion mechanisms, and immune system regulation.