Cation-dependent interactions of calreticulin with denatured and native proteins.
Calreticulin has sequence homology with the molecular chaperone calnexin, which is known to control folding and assembly of nascent proteins in the endoplasmic reticulum in a calcium-dependent manner. We have investigated the interaction between human placental calreticulin and denatured placental and serum proteins under various incubation conditions. The interactions with denatured proteins differed significantly from the interactions with native proteins. The interactions were highly dependent on divalent metal ions or polyamines, but were not influenced by detergent and sulfhydryl agents. Our results indicate that calreticulin might have a similar role in protein folding as the chaperone calnexin.
Wiuff
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C
Statens Seruminstitut, Copenhagen S, Denmark.
Houen
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G
D001710:Biotin; D001798:Blood Proteins / Q000737:chemistry; D015153:Blotting, Western; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D037282:Calreticulin; D002412:Cations; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003101:Collodion; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry*; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000737:chemistry; D011485:Protein Binding; D011489:Protein Denaturation; D012261:Ribonucleoproteins / Q000737:chemistry*
D001798:Blood Proteins; D002135:Calcium-Binding Proteins; D037282:Calreticulin; D002412:Cations; D018832:Molecular Chaperones; D011257:Pregnancy Proteins; D012261:Ribonucleoproteins; D001710:Biotin; D003101:Collodion