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Chaperone‐like function of lipocortin 1
Author(s) -
Kim GeumYi,
Lee HeeBong,
Lee Soo Ok,
Rhee Hae Jin,
Na Doe Sun
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700204321
Subject(s) - circular dichroism , annexin a1 , chemistry , lactate dehydrogenase , annexin , glutamate dehydrogenase , biochemistry , microbiology and biotechnology , enzyme , apoptosis , biology , glutamate receptor , receptor
Abstract Lipocortin 1 (LC1) is a 37 kDa member of the annexin family of proteins. It has been proposed to act as a mediator of some of the actions of glucocorticoids in anti‐inflammatory and immune suppressive functions. LC1 has been shown to play a role in cell proliferation, apoptosis, and differentiation. However, the exact biological functions of LC1 still remain obscure. Here it is shown that LC1 displays a chaperone‐like function. Stoichiometric amounts of LC1 suppressed thermally induced inactivation and aggregation of the test enzymes citrate synthase and glutamate dehydrogenase. LC1 was also effective in refolding guanine hydrochloride‐denatured glutamate dehydrogenase, as judged by circular dichroism spectroscopy.