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Shorter forms of the proteoglycan, Perlecan; Adding complexity to an already complex molecule
Author(s) -
Whitelock John Michael,
Jung Moon Sun,
Chuang Christine Yunang,
Cheng Bill,
Koo Tony,
Lyons James Guy,
Lord Megan Susan
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.795.2
Subject(s) - perlecan , proteoglycan , extracellular matrix , heparan sulfate , microbiology and biotechnology , population , proteome , alternative splicing , basement membrane , biology , chemistry , rna splicing , cell , messenger rna , biochemistry , gene , rna , demography , sociology
Proteoglycans are a group of molecules that exist on cell surfaces and in the extracellular matrix and are characterized by their polydisperse glycosaminoglycan chains, which make this group of molecules one of the most complex in the proteome. The aim of our study was to investigate whether the proteoglycan, perlecan, the major heparan sulfate PG of basement membranes and basal laminae is alternatively spliced using both semi‐quantitative PCR and antibodies specific for the domains on the protein core. Our results indicated that is in some cell types, notably mast cells, transcripts from the C‐terminal region containing the endorepellin sequence, were over represented in the mRNA population suggesting either the use of an alternative promoter or transcripts that have arisen from mRNA splicing events. This data supports our hypothesis that the structure of proteoglycans is inherently more complex than first thought and this complexity changes dynamically in response to environmental and cell signals and being fundamentally important for many biological and pathological processes involving angiogenesis.