Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||Extracellular matrix of ovarian tumors|
|Citation:||Seminars in Reproductive Medicine, 2006; 24(4):270-282|
|Publisher:||Thieme Medical Publ Inc|
|Carmela Ricciardelli, Raymond J. Rodgers|
|Abstract:||Tumor cells interfere with the normal programming of extracellular matrix (ECM) biosynthesis and can extensively modify the structure and composition of the matrix. The role of ECM components is becoming increasingly recognized as an important determinant for the growth and progression of solid tumors. The extensive remodeling of the normal ECM in tumors can proceed through the degradation of pre-existing ECM molecules and/or by the neosynthesis of ECM components, which in many cases are not present in the ECM of normal tissues. In the ovary the ECM comprises a variety of molecules including the collagen superfamily and noncollagenous proteins such as glycoproteins, proteoglycans, and hyaluronan. Elevated levels of laminin-gamma2, collagen types I and III, fibronectin, syndecan-1, glypican-1, versican, and hyaluronan and its receptors CD44 have all been associated with a poor prognosis of ovarian cancers. Generally, there is a differential expression of laminin chains alpha1, alpha4, and beta2 among serous (alpha1, beta2), mucinous (alpha4), and endometrioid (alpha1) tumors. This review focuses on these and other ECM molecules in ovarian tumors.|
collagen type IV
|Appears in Collections:||Aurora harvest 2|
Obstetrics and Gynaecology publications
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.