Document Detail


Purification of catalytically active caspase-12 and its biochemical characterization.
MedLine Citation:
PMID:  20646990     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Caspase-12, mainly detected in endoplasmic reticulum (ER), has been suggested to play a role in ER-mediated apoptosis and inflammatory caspase activation pathway. Cleavage of the prodomain by caspase-3/-7 at the carboxyl terminus of Asp94 or m-calpain at the carboxyl terminus of Lys158 was reported to be a part of caspase-12-involved apoptosis. We biochemically characterized the prodomain-free forms of caspase-12 and the equivalent enzymes; Deltapro1(G95-D419), rev-Deltapro1[(T319-N419)-(G95-D318), a reverse form of Deltapro1] and rev-Deltapro2[(T319-N419)-(T159-D318)]. The three variants showed comparable activities which were dependent on salt concentration and pH. Auto-proteolytic cleavage was observed at two sites (carboxyl termini of Asp318 and Asp320) in Deltapro1. Constitutively active forms of caspase-12 (rev-Deltapro1 and rev-Deltapro2) could induce cell death in cells transfected with the corresponding expression vectors, but no cleavage of caspase-3, DFF45 or Bid was observed, indicating caspase-12 may mediate a distinct apoptotic pathway rather than caspase-8 or -9-mediated cell death.
Authors:
Hyun-Jung Lee; Sung Haeng Lee; Sung-Hee Park; M Golam Sharoar; Song Yub Shin; Jung Sup Lee; Byungyun Cho; Il-Seon Park
Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-07-18
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  502     ISSN:  1096-0384     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  2010 Oct 
Date Detail:
Created Date:  2010-08-31     Completed Date:  2010-09-20     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  United States    
Other Details:
Languages:  eng     Pagination:  68-73     Citation Subset:  IM    
Copyright Information:
Copyright 2010 Elsevier Inc. All rights reserved.
Affiliation:
Department of Biology, Ewha Womans University, Seoul, Republic of Korea.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Apoptosis / physiology
Base Sequence
Binding Sites
Caspase 12 / chemistry,  genetics,  isolation & purification*,  metabolism
Caspase 7 / genetics,  isolation & purification,  metabolism
Cell Line
DNA Primers / genetics
Genetic Variation
Humans
Hydrogen-Ion Concentration
Osmolar Concentration
Protein Structure, Tertiary
Recombinant Proteins / genetics,  isolation & purification,  metabolism
Transfection
Chemical
Reg. No./Substance:
0/CASP12 protein, human; 0/DNA Primers; 0/Recombinant Proteins; EC 3.4.22.-/CASP7 protein, human; EC 3.4.22.-/Caspase 12; EC 3.4.22.-/Caspase 7

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Berberine ameliorates renal injury in diabetic C57BL/6 mice: Involvement of suppression of SphK-S1P ...
Next Document:  Characterization of two tropomyosin isoforms from the fast skeletal muscle of bluefin tuna Thunnus t...