Document Detail


Sec61alpha synthesis is enhanced during translocation of nascent chains of collagen type IV in F9 teratocarcinoma cells after retinoic acid treatment.
MedLine Citation:
PMID:  12532224     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Nascent procollagen peptides and other secretory proteins are transported across the endoplasmic reticulum (ER) membrane through a protein-conducting channel called translocon. Sec61alpha, a multispanning membrane translocon protein, has been implicated as being essential for translocation of polypeptide chains into the cisterns of the ER. Sec61alpha forms a protein complex with collagen and Hsp47, an ER-resident heat shock protein that binds specifically to collagen. However, it is not known whether Sec61alpha is ubiquitously produced in collagen-producing F9 teratocarcinoma cells or under heat shock treatment. Furthermore, the production and utilization of Sec61alpha may depend on the stage of cell differentiation. Cultured F9 teratocarcinoma cells are capable of differentiation in response to low concentrations of retinoic acid. This differentiation results in loss of tumorigenicity. Mouse F9 cells were grown in culture medium at 37 degrees C and 43 degrees C (heat shock treatment) treated or not with retinoic acid, and labeled in certain instances with 35S-methionine. Membrane-bound polysomes of procollagen IV were then isolated. Immunoprecipitation and Western blot analysis were performed using polyclonal antibodies against collagen IV, Hsp47 and Sec61alpha. Under retinoic acid-untreated conditions, F9 cells produced undetectable amounts of Sec61alpha. Sec61alpha, Hsp47 and type IV collagen levels were increased after retinoic acid treatment. Heat shock treatment did not alter Sec61alpha levels, suggesting that Sec61alpha production is probably not affected by heat shock. These data indicate that the enhanced production of Sec61alpha in retinoic acid-induced F9 teratocarcinoma cells parallels the increased synthesis of Hsp47 and collagen type IV.
Authors:
L R Ferreira; C E E Velano; E C Braga; C C Paula; H Marteli; J J Sauk
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Brazilian journal of medical and biological research = Revista brasileira de pesquisas médicas e biológicas / Sociedade Brasileira de Biofísica ... [et al.]     Volume:  36     ISSN:  0100-879X     ISO Abbreviation:  Braz. J. Med. Biol. Res.     Publication Date:  2003 Jan 
Date Detail:
Created Date:  2003-01-17     Completed Date:  2003-05-15     Revised Date:  2005-11-17    
Medline Journal Info:
Nlm Unique ID:  8112917     Medline TA:  Braz J Med Biol Res     Country:  Brazil    
Other Details:
Languages:  eng     Pagination:  29-37     Citation Subset:  IM    
Affiliation:
Grupo de Pesquisa em Biomedicina, Departamento de Ciências Morfológicas, Pontifícia Universidade Católica de Minas Gerais, Poços de Caldas, MG, Brasil. resende@pucpcaldas.br
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MeSH Terms
Descriptor/Qualifier:
Animals
Antineoplastic Agents / pharmacology*
Blotting, Western
Cell Differentiation / drug effects
Chemiluminescent Measurements
Collagen Type IV / drug effects,  metabolism*
Electrophoresis, Polyacrylamide Gel
HSP47 Heat-Shock Proteins
Heat-Shock Proteins / biosynthesis*,  drug effects
Membrane Proteins / biosynthesis*,  drug effects
Mice
Teratocarcinoma / metabolism
Tretinoin / pharmacology*
Tumor Cells, Cultured / drug effects*
Chemical
Reg. No./Substance:
0/Antineoplastic Agents; 0/Collagen Type IV; 0/HSP47 Heat-Shock Proteins; 0/Heat-Shock Proteins; 0/Membrane Proteins; 0/SEC61 protein; 0/Serpinh1 protein, mouse; 302-79-4/Tretinoin

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