title: Current status of tissue kallikrein inhibitors: importance in cancer.
abstract: The past decade has seen an increase in the understanding of the structure and function of protease inhibitors. The molecular basis of the interaction between a variety of biological substrates or synthetic inhibitors and serine proteases of the kallikrein family has provided insights into inhibitor protein-protease reactive site interactions, which have proved of value in the design of new kallikrein inhibitors. This review focuses on the current understanding of the functional status of kallikrein inhibitors, which include a variety of molecules derived from plant, reptile and mammalian sources, as well as synthetic agents.
authors.affiliation: Lung Institute of Western Australia and Centre for Asthma, Allergy and Respiratory Research, University of Western Australia, Ground Floor E Block, Sir Charles Gairdner Hospital, Hospital Avenue, Nedlands 6009, Perth, Australia. profbhoola@iinet.net.au
authors.forename: Kanti D
authors.initials: KD
authors.lastname: Bhoola
authors.forename: Neil L
authors.initials: NL
authors.lastname: Misso
authors.forename: Anupam
authors.initials: A
authors.lastname: Naran
authors.forename: Philip J
authors.initials: PJ
authors.lastname: Thompson
mesh_terms: D000818:Animals; D000970:Antineoplastic Agents / Q000494:pharmacology* / Q000627:therapeutic use*; D006801:Humans; D007610:Kallikreins / Q000037:antagonists & inhibitors* / Q000737:chemistry; D008297:Male; D008958:Models, Molecular; D008968:Molecular Conformation; D009369:Neoplasms / Q000188:drug therapy*; D011471:Prostatic Neoplasms / Q000188:drug therapy; D011480:Protease Inhibitors / Q000494:pharmacology* / Q000627:therapeutic use*; D009626:Terminology as Topic
chemical_list: D000970:Antineoplastic Agents; D011480:Protease Inhibitors; D007610:Kallikreins