Glucose Regulated protein 94 (GRP94), is an endoplasmic reticulum-resident member of the heat shock protein90 (HSP90). It plays a crucial role in regulating biological functions. This includes chaperoning cellular protein in the ER lumen and maintaining calcium homeostasis.
Recent reports have highlighted the clinical and functional relevance of GRP94 expression in the progression and metastasis of a variety of cancers. The current review focuses on GRP94's physiological as well as pathophysiological functions in cancer cells. You can know more about grp94 antibody from https://www.bosterbio.com/anti-grp94-antibody-pa1340-boster.html.
Many studies have demonstrated that under stress conditions, GRP94 assists in the folding of newly synthesized polypeptides and prevents the aggregation of unfolded or misfolded proteins in the ER lumen. GRP94 was first identified as a cell protein strongly upregulated in response to glucose starvation in the ER.
GRP94 can also be upregulated in normal cells by a variety of stress conditions, such as oxidative stress, ER calcium loss, misfolded protein accumulation, and glucose starvation. GRP94 shares many biochemical features, such as domain structure and ATPase activity, with other HSP90 family members.
Numerous studies have shown that GRP94 can play multiple functions in physiological conditions. GRP94 mRNA has been shown to be upregulated in many types of cancer tissues including liver, esophageal, esophageal, and glioma tissue. Furthermore, several immune histochemical studies have revealed that GRP94 protein is highly overexpressed in various cancers, like lung, colorectal, oral, esophageal, and gastric.