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MTJ1

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https://www.readbyqxmd.com/read/24772975/effect-of-dexamethasone-on-unfolded-protein-response-genes-mtj1-grp78-grp94-chop-hmox-1-in-hep2-cell-line
#1
Aynur Duzgun, Abdulkerim Bedir, Tulay Ozdemir, Rukiye Nar, Veli Kilinc, Osman Salis, Hasan Alacam, Sedat Gulten
The endoplasmic reticulum (ER) is related to the various signal routes that are activated in unfolded protein response (UPR). The Grp78, Grp94, CHOP, MTJ1 and HMOX1 genes expressions demonstrate UPR activity. In this study, we investigated the UPR gene expressions in larynx epidermoid carcinoma (HEp2) to which dexamethasone (dex) was applied. HEp2 cells were administered for 48 h with different combinations using 0.1 microM and 1 microM dex, 1 mM phenyl butyric acid (PBA) and 100 ng/ml lipopolysaccharide (LPS)...
December 2013: Indian Journal of Biochemistry & Biophysics
https://www.readbyqxmd.com/read/21503958/loss-of-cell-surface-tfii-i-promotes-apoptosis-in-prostate-cancer-cells-stimulated-with-activated-%C3%AE-%C3%A2-macroglobulin
#2
U K Misra, Y M Mowery, G Gawdi, S V Pizzo
Receptor-recognized forms of α₂ -macroglobulin (α₂ M) bind to cell surface-associated GRP78 and initiate pro-proliferative and anti-apoptotic signaling. Ligation of GRP78 with α₂ M also upregulates TFII-I, which binds to the GRP78 promoter and enhances GRP78 synthesis. In addition to its transcriptional functions, cytosolic TFII-I regulates agonist-induced Ca(2+) entry. In this study we show that down regulation of TFII-I gene expression by RNAi profoundly impairs its cell surface expression and anti-apoptotic signaling as measured by significant reduction of GRP78, Bcl-2, and cyclin D1 in 1-Ln and DU-145 human prostate cancer cells stimulated with α₂ M...
June 2011: Journal of Cellular Biochemistry
https://www.readbyqxmd.com/read/19838160/patterns-of-grp78-and-mtj1-expression-in-primary-cutaneous-malignant-melanoma
#3
John A Papalas, Robin T Vollmer, Mario Gonzalez-Gronow, Salvatore V Pizzo, James Burchette, Kenneth E Youens, Krystal B Johnson, Maria A Selim
Cell surface expression of glucose-regulated protein 78 (GRP78) occurs in several types of cancer; however, its role in the behavior of primary cutaneous melanoma is not well studied. The association of cell surface GRP78 with other proteins such as MTJ1 stimulates cell proliferation. In this study, we characterized the pattern of expression of GRP78 and MTJ1 in invasive primary cutaneous melanomas and analyzed the relationships between the pattern of expression and various clinicopathological parameters. We found two patterns of GRP78 expression in invasive primary cutaneous melanoma...
January 2010: Modern Pathology: An Official Journal of the United States and Canadian Academy of Pathology, Inc
https://www.readbyqxmd.com/read/16271702/bip-co-chaperone-mtj1-erdj1-interacts-with-inter-alpha-trypsin-inhibitor-heavy-chain-4
#4
Barbara Kroczynska, LaShaunda King-Simmons, Leonor Alloza, Maria A Alava, Ebrahim C Elguindi, Sylvie Y Blond
MTJ1/ERdj1 and its human homologue HTJ1 are membrane proteins that interact with the molecular chaperone BiP through their J-domain. HTJ1 also contains a C-terminal cytosolic region of unknown function that consists of two SANT domains separated by a spacer region. We recently showed that the second SANT domain of HTJ1 (SANT2) binds to alpha1-antichymotrypsin and alters its serpin activity [B. Kroczynska, C.M. Evangelista, S.S. Samant, E.C. Elguindi, S.Y. Blond, The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity, J...
December 23, 2005: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/14668352/the-sant2-domain-of-the-murine-tumor-cell-dnaj-like-protein-1-human-homologue-interacts-with-alpha1-antichymotrypsin-and-kinetically-interferes-with-its-serpin-inhibitory-activity
#5
Barbara Kroczynska, Christina M Evangelista, Shalaka S Samant, Ebrahim C Elguindi, Sylvie Y Blond
The murine tumor cell DnaJ-like protein 1 or MTJ1/ERdj1 is a membrane J-domain protein enriched in microsomal and nuclear fractions. We previously showed that its lumenal J-domain stimulates the ATPase activity of the molecular chaperone BiP/GRP78 (Chevalier, M., Rhee, H., Elguindi, E. C., and Blond, S. Y. (2000) J. Biol. Chem. 275, 19620-19627). MTJ1/ERdj1 also contains a large carboxyl-terminal cytosolic extension composed of two tryptophan-mediated repeats or SANT domains for which the function(s) is unknown...
March 19, 2004: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/11790253/computational-prediction-of-membrane-tethered-transcription-factors
#6
J Zupicich, S E Brenner, W C Skarnes
BACKGROUND: Sequestration of transcription factors in the membrane is emerging as an important mechanism for the regulation of gene expression. A handful of membrane-spanning transcription factors has been previously identified whose access to the nucleus is regulated by proteolytic cleavage from the membrane. To investigate the existence of other transmembrane transcription factors, we analyzed computationally all proteins in SWISS-PROT/TrEMBL for the combined presence of a DNA-binding domain and a transmembrane segment...
2001: Genome Biology
https://www.readbyqxmd.com/read/11388813/isolation-expression-and-characterization-of-fully-functional-nontoxic-bip-grp78-mutants
#7
L S King, M Berg, M Chevalier, A Carey, E C Elguindi, S Y Blond
Mammalian BiP/GRP78 and Escherichia coli DnaK belong to the highly conserved hsp70 family and function as molecular chaperones in the endoplasmic reticulum or the cytosol, respectively. Induction of murine BiP/GRP78 expression in E. coli leads to growth arrest and cell death, independent of the bacterial strain and vector used. Analysis of various BiP constructs and mutants shows that the dominant-lethal phenotype is induced specifically by the expression of the 13.7-kDa C-terminal domain and abolished by a single substitution in that region...
June 2001: Protein Expression and Purification
https://www.readbyqxmd.com/read/10777498/interaction-of-murine-bip-grp78-with-the-dnaj-homologue-mtj1
#8
M Chevalier, H Rhee, E C Elguindi, S Y Blond
The activity of Hsp70 proteins is regulated by accessory proteins, among which the most studied are the members of the DnaJ-like protein family. BiP/GRP78 chaperones the translocation and maturation of secreted and membrane proteins in the endoplasmic reticulum. No DnaJ-like partner has been described so far to regulate the function of mammalian BiP/GRP78. We show here that murine BiP/GRP78 interacts with the lumenal J domain of the murine transmembrane protein MTJ1 (J-MTJ1). J-MTJ1 stimulates the ATPase activity of BiP/GRP78 at stoichiometric concentrations...
June 30, 2000: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/7875597/isolation-of-a-mouse-cdna-encoding-mtj1-a-new-murine-member-of-the-dnaj-family-of-proteins
#9
S E Brightman, G L Blatch, B R Zetter
We report the isolation and sequencing of MTJ1, a 1792-bp cDNA from an M27 murine lung carcinoma cell line. The largest ORF within MTJ1 encodes a 63,869-Da protein, containing a 73-amino-acid (aa) sequence (the J domain) that is conserved in proteins of the DnaJ family of chaperonins. The J domain of MTJ1 is bracketed by potential transmembrane domains in a similar configuration to the J domain of the yeast DnaJ-like protein, SEC63. Polyclonal antibodies raised against deduced aa sequences within MTJ1 recognized antigens of 62, 42 and 41 kDa that were enriched in the nuclear and heavy microsome subcellular fractions of murine tumor cells...
February 14, 1995: Gene
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