The kinin system has been recognized as a locally operating hormone system of cardiovascular cells, however, the molecular mechanisms regulating circumscribed kinin release on cell surfaces are not fully understood. In particular, the principal cell docking sites for the kinin precursor, high molecular weight kininogen (HK), are not fully explored. Here we demonstrate by enzymatic digestion, recombinant overexpression, and affinity cross-linking studies that cell surface chondroitin sulfate (CS) chains of proteoglycans (PGs) serve as major HK binding sites on platelet, fibroblast, liver, and endothelial kidney cells. In this way, CS-type PGs may contribute to a local accumulation of kinin precursors on cell surfaces and modulate circumscribed release of short-lived kinin hormones at or next to their site of action.