Haptoglobin is degraded by iron in C57BL/6 mice: A possible link with endoplasmic reticulum stress

Blood Cells, Molecules, and Diseases

Volumn 39, Issue 3, 2007, Pages 229-237

  Faye, Audrey ^a,b   Ramey, Guillemette ^a,b   Foretz, Marc ^a,b   Vaulont, Sophie ^a,b  

^a INSTITUT COCHIN   (France)

^b INSERM   (France)

Author keywords

Chaperone GRP78; Endoplasmic reticulum; Haptoglobin; Iron; Stress

Indexed keywords

CHAPERONE; GLUCOSE REGULATED PROTEIN 78; HAPTOGLOBIN; IRON; MESSENGER RNA;

129SV PAS MOUSE; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; C57BL 6 MOUSE; ENDOPLASMIC RETICULUM STRESS; EXPERIMENTAL ANIMAL; GENETIC LINKAGE; GLYCOSYLATION; LIVER; MALE; MOUSE; NONHUMAN; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BLOOD LEVEL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN SYNTHESIS;

ANIMALS; CELLS, CULTURED; ENDOPLASMIC RETICULUM; GLYCOSYLATION; HAPTOGLOBINS; HEAT-SHOCK PROTEINS; HEMOGLOBINS; HEPATOCYTES; IRON; IRON OVERLOAD; LIVER; MALE; MICE; MICE, INBRED C57BL; MOLECULAR CHAPERONES; OXIDATIVE STRESS; PROTEIN PROCESSING, POST-TRANSLATIONAL; TUNICAMYCIN;

MUS;

EID: 34748824925     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcmd.2007.05.008     Document Type: Article

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