Functional and biochemical characterization of ADAMs and their predicted role in protein ectodomain shedding Journal Article
| Author: | Blobel, C. P. |
| Article Title: | Functional and biochemical characterization of ADAMs and their predicted role in protein ectodomain shedding |
| Abstract: | Proteolysis on the cell surface and in the extracellular matrix is essential for normal cellular functions during development and in the adult, but it may also have undesirable consequences by promoting diseases such as cancer, arthritis, and Alzheimer's disease. A particularly interesting function of proteolysis on the cell surface is to release ectodomains of membrane proteins from the plasma membrane. This process, which is referred to as protein ectodomain shedding, affects a variety of proteins with important roles in development and in disease, including cytokines, growth factors, receptors, adhesion proteins and other proteins such as the amyloid precursor protein. In principle, protein ectodomain shedding can dramatically change the properties of a substrate protein. For example, membrane anchored growth factors such as transforming growth factorα (TGF-α) are only able to activate their receptor, the epidermal growth factor receptor (EGFR), after they are shed from the plasma membrane. Inhibitor studies have implicated zinc-dependent metalloproteases in protein ectodomain shedding, and in particular a family of metalloproteases termed ADAMs (a disintegrin and metalloprotease). The main focus of my lab is to understand the role of different ADAMs in protein ectodomain shedding, and to learn about the functional consequences of protein ectodomain shedding for individual substrates. |
| Keywords: | controlled study; unclassified drug; pathogenesis; nonhuman; protein domain; animal cell; mouse; animals; animal tissue; protein degradation; epidermal growth factor receptor; animal experiment; membrane proteins; in vitro study; enzyme activity; extracellular matrix; molecular mechanics; cytokine; tumor necrosis factor alpha; tumor necrosis factor-alpha; enzyme analysis; membrane glycoproteins; carrier proteins; recombinant proteins; membrane protein; cell membrane; short survey; development; rheumatoid arthritis; catalysis; zinc; enzyme specificity; growth factor; alzheimer disease; knockout mouse; metalloprotease; metalloproteinase; transforming growth factor alpha; rank ligand; amyloid precursor protein; cell adhesion molecule; cell surface; protein ectodomain shedding; membrane receptor; disintegrins; metalloendopeptidases; cancer; adams; cell enzyme; a disintegrin and metalloprotease; cytokine trance; transforming growth factor alpha receptor |
| Journal Title: | Inflammation Research |
| Volume: | 51 |
| Issue: | 2 |
| ISSN: | 1023-3830 |
| Publisher: | Birkhauser Verlag Ag |
| Date Published: | 2002-02-01 |
| Start Page: | 83 |
| End Page: | 84 |
| Language: | English |
| PUBMED: | 11926318 |
| PROVIDER: | scopus |
| DOI: | 10.1007/BF02684007 |
| DOI/URL: | |
| Notes: | Export Date: 14 November 2014 -- Source: Scopus |
