title: Artemin as an efficient molecular chaperone.
abstract: Artemin is an abundant thermostable protein in Artemia encysted embryos under stress. It is considered as a stress protein, as its highly regulated expression is associated with stress resistance in this crustacea. In the present study, artemin has been shown to be a potent molecular chaperone with high efficacy. Artemin is capable of inhibiting the chemical aggregation of proteins such as carbonic anhydrase (CA) and horseradish peroxidase (HRP) at unique molar ratios of chaperone to substrates (1:40 and 1:26 for CA and HRP, respectively). Furthermore, it can also enhance refolding yield of these substrates by nearly 50%. The refolding promotion of CA is checked and verified through a sensitive fluorimetric technique. Based on these experiments, artemin showed higher chaperone activity than other chaperones. The evaluation of artemin surface using ANS showed it to be highly hydrophobic, probably resulting in its high efficacy. These results suggest that artemin can be considered a novel low molecular weight chaperone.
authors: Department of Biology, Faculty of Science, University of Guilan, Rasht, Iran.
authors: S Shirin
authors: SS
authors: Shahangian
authors: Behnam
authors: B
authors: Rasti
authors: Reza H
authors: RH
authors: Sajedi
authors: Reza
authors: R
authors: Khodarahmi
authors: Majid
authors: M
authors: Taghdir
authors: Bijan
authors: B
authors: Ranjbar
mesh_terms: D000818:Animals; D001156:Artemia / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D060829:Arthropod Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D060829:Arthropod Proteins; D018832:Molecular Chaperones