title: Imaging of protease functions--current guide to spotting cysteine cathepsins in classical and novel scenes of action in mammalian epithelial cells and tissues.
abstract: The human genome encodes some hundreds of proteases. Many of these are well studied and understood with respect to their biochemistry, molecular mechanisms of proteolytic cleavage, expression patterns, molecular structure, substrate preferences and regulatory mechanisms, including their endogenous inhibitors. Moreover, precise determination of protease localisation within subcellular compartments, peri- and extracellular spaces has been extremely useful in elucidating biological functions of peptidases. This can be achieved by refined methodology as will be demonstrated herein for the cysteine cathepsins. Besides localisation, it is now feasible to study in situ enzymatic activity at the various levels of subcellular compartments, cells, tissues, and even whole organisms including mouse.
authors: School of Engineering and Science, Jacobs University Bremen, 28759 Bremen, Germany.
authors: Maria
authors: M
authors: Arampatzidou
authors: Maren
authors: M
authors: Rehders
authors: Stephanie
authors: S
authors: Dauth
authors: Denise M T
authors: DM
authors: Yu
authors: Sofia
authors: S
authors: Tedelind
authors: Klaudia
authors: K
authors: Brix
mesh_terms: D000818:Animals; D002403:Cathepsins / Q000737:chemistry / Q000502:physiology*; D057056:Cysteine Proteases / Q000737:chemistry / Q000502:physiology*; D004847:Epithelial Cells / Q000201:enzymology* / Q000648:ultrastructure; D006801:Humans; D008247:Lysosomes / Q000201:enzymology / Q000648:ultrastructure; D008854:Microscopy, Electron / Q000295:instrumentation / Q000379:methods / Q000639:trends; D008856:Microscopy, Fluorescence / Q000295:instrumentation / Q000379:methods / Q000639:trends; D021381:Protein Transport / Q000502:physiology; D014018:Tissue Distribution / Q000502:physiology
chemical_list: D002403:Cathepsins; D057056:Cysteine Proteases