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Did you hear the one about the chemist, the biochemist, the molecular biologist, the physiologist, the physician-scientist, and the clinical oncologist? They went out to learn about a mysterious and complex creature called a heparan sulfate (HS) proteoglycan. Their interest was piqued by an intriguing paper in this issue of PNAS (1) with the title “Tumor Cell Surface Heparan Sulfate as Cryptic Promoters or Inhibitors of Tumor Growth and Metastasis.” They came upon a knowledgeable female scientist who told them that HS chains belonged to a class of long acidic sugar chains called glycosaminoglycans (GAGs), which usually are attached to cell surfaces via a core protein (2). The combination of one or more HS chains and a core protein is called an HS proteoglycan (Fig. 1). Diagram of a typical HS proteoglycan with its core protein and HS chains. Heparanases (heparin lyases)-I and -III have different specificities in cleaving HS chains (inside and outside the modified blocks of HS chains, respectively), thus generating different kinds of HS-GAG fragments. All six men felt they understood the primary observations in the paper. First, when mice carrying malignant tumors were injected with cloned purified bacterial enzymes called heparanases (also called heparinases or heparin lyases) that cleaved HS chains internally, the biological outcome depended on the type of enzyme used. Heparanase (Hep)-I induced significant acceleration of tumor growth, whereas Hep-III caused a reduction. The latter also seemed to limit the ability of the tumor to spread (metastasize) to other parts of the body. Second, when tumor cells were pretreated with enzymes before their i.v. injection, the …

Six blind men and the elephant—the many faces of heparan sulfate