Functional Coupling between the Unfolded Protein Response and Endoplasmic Reticulum/Golgi Ca-ATPases Promotes Stress Tolerance, Cell Wall Biosynthesis, and Virulence of Aspergillus fumigatus.

Many species of pathogenic fungi deploy the unfolded protein response (UPR) to expand the folding capacity of the endoplasmic reticulum (ER) in proportion to the demand for virulence-related proteins that traffic through the secretory pathway. Although Ca plays a pivotal role in ER function, the mechanism by which transcriptional upregulation of the protein folding machinery is coordinated with Ca homeostasis is incompletely understood. In this study, we investigated the link between the UPR and genes encoding P-type Ca-ATPases in the human-pathogenic mold We demonstrate that acute ER stress increases transcription of the gene, encoding a member of the sarco/endoplasmic reticulum Ca-ATPase (SERCA) family, as well as that of , encoding a secretory pathway Ca-ATPase (SPCA) in the Golgi membrane.

The early signaling pathway of live yeast cell derivative in THP-1 monocytes.

Live yeast cell derivative (LYCD) is a medicinal yeast extract that has been used in the treatment of burns, wounds and hemorrhoids for over 70 years. It has been shown to enhance the closure of skin wounds in diabetic mice by increasing inflammation, angiogenesis, formation of granulation tissue and epithelial migration. An active fraction of LYCD has been identified as a mixture of peptides ranging in size from 5 kDA to 17 kDA.

Midgestational lethality in mice lacking the parathyroid hormone (PTH)/PTH-related peptide receptor is associated with abrupt cardiomyocyte death.

PTHrP is a key developmental regulatory protein and a potent vasoactive agent. Previous studies have shown that mice lacking either the Pthrp or the PTH type 1 receptor (Pth1r) gene exhibit severe chondrodysplasia. In addition, in most genetic backgrounds, the receptor null mice die prenatally at midgestation, but the cause of death remains elusive.

Nuclear CaMKII inhibits neuronal differentiation of PC12 cells without affecting MAPK or CREB activation.

Ca(2+)/calmodulin-regulated protein kinase II (CaMKII) mediates many cellular events. The four CaMKII isoforms have numerous splice variants, three of which contain nuclear localization signals. Little is known about the role of nuclear localized CaMKII in neuronal development.