Role of mp 170 Seprase in Breast Cancer
Abstract
The fibroblast growth factor (FGF) family comprises of at least 20 genetically distinct gene members which play an important role in embryonic developmental processes, in angiogenesis, wound healing, tumor growth, and in neuronal function and neuronal regeneration. In vitro, they are potent regulators of proliferation, differentiation, motility and survival for various cell lines (Reviews in 1,2). The prototypic members of this family are the acidic and basic FGF (FGF-l and FOF-2, respectively) that are widely expressed and distributed in the extracellular matrix of embryonic, adult and tumor tissues (3,4). In the extracellular matrix, these fibroblast growth factors are bound to matrix heparin sulfate proteoglycans and remain in a latent state until they are activated and mobilized to their high affinity tyrosine kinase receptors to elicit their biological activities. One established mechanism that can release active FGFs from the extracellular storage site is the digestion of heparin sulfate chains and proteoglycan protein cores by extracellular heparanases and proteinases, respectively (5,6). Recently, we proposed an alternative mechanism that involves a secreted FOF-binding protein, FGF-BPl (7,8,9).
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 2001
- Accession Number
- ADA407250
Entities
People
- Emma T. Bowden
- Quang Nguyen
Organizations
- Georgetown University