High-level secretion of native recombinant human calreticulin in yeast.

ABSTRACT:

Background

Calreticulin (CRT) resides in the endoplasmic reticulum (ER) and functions to chaperone proteins, ensuring proper folding, and intracellular Ca(2+) homeostasis. Emerging evidence shows that CRT is a multifunctional protein with significant roles in physiological and pathological processes with presence both inside and outside of the ER, including the cell surface and extracellular space. These recent findings suggest the possible use of this ER chaperone in development of new therapeutic pharmaceuticals. Our study was focused on human CRT production in two yeast species, Saccharomyces cerevisiae and Pichia pastoris.

Results

Expression of a full-length human CRT precursor including its native signal sequence resulted in high-level secretion of mature recombinant pr

SUBMITTER: Ciplys E 

PROVIDER: S-EPMC4608220 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature