Calreticulin: Roles in Cell-Surface Protein Expression

Calreticulin: Roles in Cell-Surface Protein Expression

In order to perform their designated functions, proteins require precise subcellular localizations. For cell-surface proteins, such as receptors and channels, they are able to transduce signals only when properly targeted to the cell membrane. Calreticulin is a multi-functional chaperone protein involved in protein folding, maturation, and trafficking. However, evidence has been accumulating th...

Functional Roles of Calreticulin in Cancer Biology

Calreticulin is a highly conserved endoplasmic reticulum chaperone protein which participates in various cellular processes. It was first identified as a Ca(2+)-binding protein in 1974. Accumulated evidences indicate that calreticulin has great impacts for the development of different cancers and the effect of calreticulin on tumor formation and progression may depend on cell types and clinical...

Calreticulin modulates cell adhesiveness via regulation of vinculin expression

Calreticulin is an ubiquitous and highly conserved high capacity Ca(2+)-binding protein that plays a major role in Ca2+ storage within the lumen of the ER. Here, using L fibroblast cell lines expressing different levels of calreticulin, we show that calreticulin plays a role in the control of cell adhesiveness via regulation of expression of vinculin, a cytoskeletal protein essential for cell-s...

Anti-DNA Antibodies Receptor Involved in Cell Penetration of Calreticulin, a Potential Cell Surface

applications of autodisplay system for recombinant protein expression on the bacterial cell surface

protein secretory systems are found in all living organisms including gram negative bacteria, and eukaryotic cell’s organelles that are derived from these bacteria. unlike all other living organisms, gram negative bacteria have different protein secretory systems. at least there are four different independent secretory systems, which are responsible to transport the secreted proteins to the mil...