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Suramin potently inhibits the enzymatic activity of PSM

✍ Scribed by Barbara S. Slusher; Carol W. Tiffany; Aviva Merion; Rena G. Lapidus; Paul F. Jackson

Book ID
101321057
Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
230 KB
Volume
44
Category
Article
ISSN
0270-4137

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## BACKGROUND. The prostate cancer marker prostate-specific membrane antigen (PSM) is highly homologous to the brain enzyme N-acetylated alpha-linked acidic dipeptidase (NA-ALADase). NAALADase is known to cleave terminal carboxy glutamates from both the neuronal peptide N-acetylaspartylglutamate (

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## Abstract Heparanase, a heparan sulfate‐specific endo‐β‐D‐glucuronidase, plays an important role in tumor cell metastasis through the degradation of extracellular matrix heparan sulfate proteoglycans (ECM HSPG). Heparanase activity correlates with the metastatic propensity of tumor cells. Suramin