Disease relevance of Pdia4

• The amount of CaBP2 in H-35 Reuber hepatoma cells increases in parallel with that of immunoglobin heavy-chain-binding protein under conditions which lead to impaired glycosylation, while the amount of calreticulin, another KDEL-containing glycoprotein, remains almost unchanged [1].
• Erp72 expression activated by transient cerebral ischemia or disturbance of neuronal endoplasmic reticulum calcium stores [2].

High impact information on Pdia4

• Furthermore, coimmunoprecipitation studies after antimycin A treatment demonstrated that Tg stably associates with BiP, grp94, and ERp72 [3].
• Likewise, when cellular ATP was depleted to less than 10% of control with antimycin A, mRNA levels of BiP, ERp72, and grp94 were increased in kidney and thyroid epithelial cell culture models [3].
• Analysis of proteins in the d < 1.006 g/ml fraction after ultracentrifugation of the luminal content of the cells identified five chaperone proteins: binding protein, protein disulfide isomerase, calcium-binding protein 2, calreticulin, and glucose regulatory protein 94 [4].
• Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation [5].
• Three of these proteins, CaBP1, CaBP2, and protein disulfide isomerase, have been purified from rat microsomes and analyzed biochemically [6].

Anatomical context of Pdia4

• The expression pattern was like that of the endoplasmic reticulum chaperone, Erp72, but not that of the cytosol chaperone, hsp72 [7].

Associations of Pdia4 with chemical compounds

• Ca-binding protein 2 (CaBP2) has been described previously as an intracisternal calcium-binding microsomal glycoprotein [1].
• Analysis of uncross-linked and cross-linked samples by sucrose density gradient centrifugation confirmed that Tg, BiP, grp94, and ERp72 are present together in high molecular weight complexes only after treatment of cells with cross-linking reagent [5].

Physical interactions of Pdia4

• In contrast, after cross-linking, there was a large increase in the amount of ERp72 and grp94 that coimmunoprecipitated with anti-Tg antibodies, although there was only a slight increase in BiP [5].

References