Abstract |
Tumor cells are characterized by uncontrolled cell growth at a primary site that is caused by genetic alterations. Tumor cells that metastasize from their primary site to distant locations are commonly referred to as malignant. Cell migration is a critical step in this process. The ability of tumor cells to migrate and invade is partly controlled by proteolytic enzymes. These enzymes are secreted by either the tumor cells themselves or adjacent cells. They represent all classes of proteases, including serine and cysteine proteases. Serine proteases, in particular urokinase plasminogen activator (uPA), initiate a proteolytic cascade that culminates in degrading components of the extracellular matrix (ECM). Some serine proteases are controlled by a superfamily of proteins known as serpins. This minireview provides an overview of serpins that are vital in regulating tumor cell migration and progressing cancer.
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Authors | Yolanda Fortenberry |
Journal | Biological chemistry
(Biol Chem)
Vol. 396
Issue 3
Pg. 205-13
(Mar 2015)
ISSN: 1437-4315 [Electronic] Germany |
PMID | 25381952
(Publication Type: Journal Article, Research Support, N.I.H., Extramural, Review)
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Chemical References |
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Topics |
- Animals
- Cell Movement
- Humans
- Models, Biological
- Neoplasms
(metabolism, pathology)
- Serpins
(metabolism)
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