SPARC and tumor growth: where the seed meets the soil?

PE Framson, EH Sage - Journal of cellular biochemistry, 2004 - Wiley Online Library
PE Framson, EH Sage
Journal of cellular biochemistry, 2004Wiley Online Library
Matricellular proteins mediate interactions between cells and their extracellular environment.
This functional protein family includes several structurally unrelated members, such as
SPARC, thrombospondin 1, tenascin C, and osteopontin, as well as some homologs of
these proteins, such as thrombospondin 2 and tensascin X. SPARC, a prototypic
matricellular protein, and its homolog hevin, have deadhesive effects on cultured cells and
have been characterized as antiproliferative factors in some cellular contexts. Both proteins …
Abstract
Matricellular proteins mediate interactions between cells and their extracellular environment. This functional protein family includes several structurally unrelated members, such as SPARC, thrombospondin 1, tenascin C, and osteopontin, as well as some homologs of these proteins, such as thrombospondin 2 and tensascin X. SPARC, a prototypic matricellular protein, and its homolog hevin, have deadhesive effects on cultured cells and have been characterized as antiproliferative factors in some cellular contexts. Both proteins are produced at high levels in many types of cancers, especially by cells associated with tumor stroma and vasculature. In this Prospect article we summarize evidence for SPARC and hevin in the regulation of tumor cell growth, differentiation, and metastasis, and we propose that matricellular proteins such as these perform critical functions in desmoplastic responses of tumors that culminate in their dissemination and eventual colonization of other sites. © 2004 Wiley‐Liss, Inc.
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