Stress Chaperone GRP-78 Functions in Mineralized Matrix Formation
نویسندگان
چکیده
منابع مشابه
Endoplasmic reticulum chaperone protein GRP-78 mediates endocytosis of dentin matrix protein 1.
Dentin matrix protein 1 (DMP1), a phosphorylated protein present in the mineral phase of both vertebrates and invertebrates, is a key regulatory protein during biogenic formation of mineral deposits. Previously we showed that DMP1 is localized in the nuclear compartment of preosteoblasts and preodontoblasts. In the nucleus DMP1 might play an important role in the regulation of genes that contro...
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Schmidt, Bela Z., and David H. Perlmutter. Grp78, Grp94, and Grp170 interact with 1-antitrypsin mutants that are retained in the endoplasmic reticulum. Am J Physiol Gastrointest Liver Physiol 289: G444–G445, 2005. First published April 25, 2005; doi:10.1152/ajpgi.00237.2004.—In 1-antitrypsin ( 1-AT) deficiency, a mutant form of 1-AT polymerizes in the endoplasmic reticulum (ER) of liver cells r...
متن کاملGRP-78 secreted by tumor cells blocks the antiangiogenic activity of bortezomib.
Antiangiogenic effects of the proteasome inhibitor bortezomib were analyzed on tumor xenografts in vivo. Bortezomib strongly inhibited angiogenesis and vascularization in the chicken chorioallantoic membrane. Bortezomib's inhibitory effects on chorioallantoic membrane vascularization were abrogated in the presence of distinct tumor xenografts, thanks to a soluble factor secreted by tumor cells....
متن کاملLommel Matrix Functions
The main objective of this work is to develop a pair of Lommel matrix functions suggested by the hypergeometric matrix functions and some of their properties are studied. Some properties of the hypergeometric and Bessel matrix functions are obtained.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2011
ISSN: 0021-9258
DOI: 10.1074/jbc.m110.179341