| Warning:  Undefined variable $zfal in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
 
 Deprecated:  str_replace(): Passing null to parameter #3 ($subject) of type array|string is deprecated in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
 
  
 Warning:  Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 530
 
 Warning:  Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 531
 
 Warning:  file_get_contents(http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=19829057&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
 in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 445
 
   English Wikipedia
 
 Nephropedia Template TP (
 
 Twit Text
 
 
 DeepDyve
 Pubget Overpricing
 | lüll   
 
 Autophagy eliminates a specific species of misfolded procollagen and plays a  protective role in cell survival against ER stress Ishida Y; Nagata KAutophagy  2009[Nov]; 5 (8): 1217-9Type I collagen is one of the most abundant proteins in the human body and is  essential for tissue formation. Mutations in collagen cause severe abnormalities  in bone formation, including osteogenesis imperfecta. Although the mutant  collagens are retained in the endoplasmic reticulum (ER) and are toxic to the  cell, little is known about how they are removed from the ER. Using two  independent cell lines that produce misfolded collagens, we recently demonstrated  that procollagen, which is misfolded and accumulated as trimers, is eliminated  through the autophagy-lysosomal pathway, not through the ER-associated  degradation (ERAD) pathway. In contrast, misfolded procollagen monomer is  degraded via ERAD. Moreover, autophagic elimination and ERAD occur independently  and exert protective roles and promote cell survival. Thus, autophagy and ERAD,  in concert, contribute to eliminating toxic species of misfolded and accumulated  proteins from the ER.|*Autophagy[MESH]|*Cytoprotection[MESH]|*Protein Folding[MESH]|*Stress, Physiological[MESH]|Cell Survival[MESH]|Endoplasmic Reticulum/*metabolism/*pathology[MESH]|HSP47 Heat-Shock Proteins/metabolism[MESH]|Humans[MESH]|Models, Biological[MESH]|Mutant Proteins/metabolism[MESH]|Procollagen/*metabolism[MESH]
 |