Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Anna M. Castle"'
Publikováno v:
PLoS ONE, Vol 13, Iss 9, p e0198383 (2018)
The ABC transporter ABCG1 contributes to the regulation of cholesterol efflux from cells and to the distribution of cholesterol within cells. We showed previously that ABCG1 deficiency inhibits insulin secretion by pancreatic beta cells and, based on
Externí odkaz:
https://doaj.org/article/25219964486640e486b5f912fbb680b6
Autor:
Syed Saad Hussain, Anna M. Castle, Peter Arvan, Catherine A. Doyle, Megan T. Harris, J. David Castle, Candice M Inouye, Alex J. B. Kreutzberger
Publikováno v:
Molecular Biology of the Cell
In pancreatic β-cells, insulin granule membranes are enriched in cholesterol and are both recycled and newly generated. Cholesterol’s role in supporting granule membrane formation and function is poorly understood. ATP binding cassette transporter
Autor:
Raghavendra G. Mirmira, Anna M. Castle, Laura C. Page, Catherine C. Hedrick, Anthony P. Trace, John S. Parks, Carmella Evans-Molina, Jeffrey M. Sturek, J. David Castle
Publikováno v:
Journal of Clinical Investigation. 120:2575-2589
Cholesterol is a critical component of cell membranes, and cellular cholesterol levels and distribution are tightly regulated in mammals. Recent evidence has revealed a critical role for pancreatic beta cell-specific cholesterol homeostasis in insuli
Publikováno v:
Molecular Biology of the Cell. 13:4266-4278
In secretory carrier membrane proteins (SCAMPs), the most conserved structural segment is between transmembrane spans 2 and 3, facing the cytosol. A synthetic peptide, CWYRPIYKAFR (E peptide), from this segment of SCAMP2 potently inhibits exocytosis
Autor:
Anna M. Castle, J. David Castle
Publikováno v:
Molecular Biology of the Cell. 9:575-583
We have used coexpression of a salivary basic proline-rich protein (PRP) along with a proline-rich proteoglycan (PRPg) in pituitary AtT-20 cells to examine the regulation of glycosaminoglycan (GAG) biosynthesis and the storage of these secretory prod
Publikováno v:
Journal of Cell Science. 109:1637-1645
When expressed in pituitary AtT-20 cells, parotid proline-rich proteins enter the regulated pathway. Because the short N-terminal domain of a basic proline-rich protein is necessary for efficient export from the ER, it has not been possible to evalua
Autor:
Anna M. Castle, J D Castle
Publikováno v:
Journal of Biological Chemistry. 268:20490-20496
We have isolated two cDNAs that encode backbones of proline-rich proteoglycans identified previously in parotids of isoproterenol-treated rats (Blair, A. E., Castle, A. M., and Castle, J. D. (1991) Am. J. Physiol. 30, C897-C905). The sequences and do
Publikováno v:
Journal of Biological Chemistry. 267:13093-13100
We have investigated the role of different domains of a salivary basic proline-rich protein in intracellular transport and sorting of proline-rich proteins to the secretory granules. We have cloned a full-length cDNA of a basic proline-rich protein f
Publikováno v:
Molecular biology of the cell. 20(6)
The epidermal growth factor receptor (EGFR) is targeted for lysosomal degradation by ubiquitin-mediated interactions with the ESCRTs (endosomal-sorting complexes required for transport) in multivesicular bodies (MVBs). We show that secretory carrier
Publikováno v:
The Journal of biological chemistry. 276(25)
Resting secretion of salivary proteins by the parotid gland is sustained in situ between periods of eating by parasympathetic stimulation and has been assumed to involve low level granule exocytosis. By using parotid lobules from ad libitum fed rats