Document Detail


Imaging of protease functions--current guide to spotting cysteine cathepsins in classical and novel scenes of action in mammalian epithelial cells and tissues.
MedLine Citation:
PMID:  21898969     Owner:  NLM     Status:  In-Process    
Abstract/OtherAbstract:
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:
Maria Arampatzidou; Maren Rehders; Stephanie Dauth; Denise M T Yu; Sofia Tedelind; Klaudia Brix
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Italian journal of anatomy and embryology = Archivio italiano di anatomia ed embriologia     Volume:  116     ISSN:  1122-6714     ISO Abbreviation:  Ital J Anat Embryol     Publication Date:  2011  
Date Detail:
Created Date:  2011-09-08     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9612303     Medline TA:  Ital J Anat Embryol     Country:  Italy    
Other Details:
Languages:  eng     Pagination:  1-19     Citation Subset:  IM    
Affiliation:
School of Engineering and Science, Jacobs University Bremen, 28759 Bremen, Germany.
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