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Researchers from Children's Hospital provide details of new studies and findings in the area of science

Published in Hospital Law Weekly, December 3rd, 2009

"Plasma cells can synthesize and secrete thousands of Ig molecules per second, which are folded and assembled in the endoplasmic reticulum (ER) and are likely to place unusually high demands on the resident chaperones and folding enzymes. We have discovered a new resident ER protein (pERp1) that is a component of the BiP chaperone complex," scientists in the United States report.

"PERp1 is substantially up-regulated during B to plasma cell differentiation and can be induced in B cell lines by some UPR activators, arguing that it represents a potentially new class of conditional UPR targets. In LPS-stimulated murine splenocytes, pERp1 interacted covalently via a...

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