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Proteoglycan Form and Function: A Comprehensive Nomenclature of Proteoglycans

Overview
Journal Matrix Biol
Publisher Elsevier
Date 2015 Feb 22
PMID 25701227
Citations 524
Authors
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Abstract

We provide a comprehensive classification of the proteoglycan gene families and respective protein cores. This updated nomenclature is based on three criteria: Cellular and subcellular location, overall gene/protein homology, and the utilization of specific protein modules within their respective protein cores. These three signatures were utilized to design four major classes of proteoglycans with distinct forms and functions: the intracellular, cell-surface, pericellular and extracellular proteoglycans. The proposed nomenclature encompasses forty-three distinct proteoglycan-encoding genes and many alternatively-spliced variants. The biological functions of these four proteoglycan families are critically assessed in development, cancer and angiogenesis, and in various acquired and genetic diseases where their expression is aberrant.

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References
1.
Stetefeld J, Alexandrescu A, Maciejewski M, Jenny M, Rathgeb-Szabo K, Schulthess T . Modulation of agrin function by alternative splicing and Ca2+ binding. Structure. 2004; 12(3):503-15. DOI: 10.1016/j.str.2004.02.001. View

2.
Mongiat M, Taylor K, Otto J, Aho S, Uitto J, Whitelock J . The protein core of the proteoglycan perlecan binds specifically to fibroblast growth factor-7. J Biol Chem. 2000; 275(10):7095-100. DOI: 10.1074/jbc.275.10.7095. View

3.
Hedbom E, Heinegard D . Interaction of a 59-kDa connective tissue matrix protein with collagen I and collagen II. J Biol Chem. 1989; 264(12):6898-905. View

4.
Xu W, Neill T, Yang Y, Hu Z, Cleveland E, Wu Y . The systemic delivery of an oncolytic adenovirus expressing decorin inhibits bone metastasis in a mouse model of human prostate cancer. Gene Ther. 2014; 22(3):247-56. PMC: 4361227. DOI: 10.1038/gt.2014.110. View

5.
Rucci N, Capulli M, Ventura L, Angelucci A, Peruzzi B, Tillgren V . Proline/arginine-rich end leucine-rich repeat protein N-terminus is a novel osteoclast antagonist that counteracts bone loss. J Bone Miner Res. 2013; 28(9):1912-24. DOI: 10.1002/jbmr.1951. View