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- W2013293359 abstract "Calreticulin (CRT) is a calcium-binding protein that participates in several cellular processes including the control of protein folding and homeostasis of Ca2+. Its folding, stability and functions are strongly controlled by the presence of Ca2+. The oligomerization state of CRT is also relevant for its functions. We studied the thermal transitions of monomers and oligomers of CRT by differential scanning calorimetry (DSC), circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) in the presence and absence of Ca2+. We found three and two components for the calorimetric transition in the presence and absence of Ca2+ respectively. The presence of several components was also supported by CD and FTIR spectra acquired as a function of the temperature. The difference between the heat capacity of the native and the unfolded state strongly suggests that interactions between protein domains also contribute to the heat uptake in a calorimetry experiment. We found that once unfolded at high temperature the process is reversible and the native state can be recovered upon cooling only in the absence of Ca2+. We also propose a new simple method to obtain pure CRT oligomers." @default.
- W2013293359 created "2016-06-24" @default.
- W2013293359 creator A5026004030 @default.
- W2013293359 date "1994-07-01" @default.
- W2013293359 modified "2023-10-17" @default.
- W2013293359 title "Novel functions for calreticulin: interaction with integrins and modulation of gene expression?" @default.
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- W2013293359 doi "https://doi.org/10.1016/0968-0004(94)90001-9" @default.
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