An Epithelial-Derived, Integral Membrane, Kunitz-Type serine Protease Inhibitor in Breast Cancer
Abstract
In the current research plan, we proposed to study the anti-tumor and anti-protease activity of a membrane-bound Kunitz-type serine protease inhibitor (KSPI; also known as HAI-1). In order to investigate how HAI-1 regulates matriptase function, we investigated the cellular events associated with matriptase activation. During matriptase activation induced either by S1P or suramin, HAI-1 along with matriptase is translocated and accumulated at cell-cell junctions or in vesicle-like structures, which were named as matriptase activation foci. In activation foci, HAI-1 binds active matriptase to form a 120-kDa complex immediately following the activation of matriptase. The close temporal and spatial coupling of matriptase activation with its inhibition suggests that the proteolytic activity of this enzyme must be well controlled, and that the activation of matriptase substrates may be tightly regulated by this mechanism.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 01, 2004
- Accession Number
- ADA435266
Entities
People
- Chen-yong Lin
Organizations
- Georgetown University