Bladder cancer (BC) is the ninth most common tumors in the world and one of the most common malignant tumor of the urinary system. Several studies have reported that the expression of miR-133b reduced in BC, but whether it plays a role in the development of BC and the mechanism is unclear. microRNAs can be packaged into exosomes to mediate communication between tumor cells, affecting their proliferation and apoptosis.
The purpose of this study was to determine the effect of miR-133b exosomal in BC proliferation and its molecular mechanism. First, the expression of miR-133b was evaluated in BC and adjacent normal tissue, as well as in the patient’s serum exosomes BC and healthy controls. Then the delivery and internalization of exosomes in cell localization was observed through fluorescence. cell viability and apoptosis assessed in cells transfected with imitate BC and incubated with exosomes.
Exosomal the role of miR-133b is also analyzed in nude mice transplanted tumor. Furthermore, miR-133b target genes predicted through bioinformatics. Levels of miR-133b was significantly decreased in the SM network and in exosomes from serum of patients, which correlated with poor overall survival in TCGA. Exosomal miR-133b can be obtained using the cells BC after transfection with miR-133b mimic.
Expression of miR-133b increased after incubation with exosomal miR-133b, which causes inhibition of viability and increased cell apoptosis in BC. Exosomal miR-133b can suppress tumor growth in vivo. In addition, we found that miR-133b exosomal may play a role in suppressing the proliferation by upregulating SM dual-specificity protein phosphatase 1 (DUSP1). These findings may offer promise for new therapeutic directions BC.
Exosome-transmitted microRNA-133b inhibited bladder cancer proliferation by upregulating dual-specificity proteinphosphatase1
Protein phosphatase one 35 regulatory subunit required for ciliogenesis, morphogenesis notochord, and the development of cell-cycle during the development of murine
protein phosphatases regulate a variety of proteins with post-translational modifications and necessary for most intracellular events in eukaryotes. While some of the core components of complex protein phosphatase marked, many large complex subunit remained unstudied. Here we characterize the allele loss-of-function protein phosphatase 1 regulatory subunit 35 (Ppp1r35) gene.
Ppp1r35 homozygous mouse embryos lacking is the development of a delayed start at embryonic day (E) 7.5 and have morphological defects obvious at later stages. Mutant fails to start rotating and not advancing beyond the size or staging normal E8.5 embryos. Consistent with the latest in in vitro studies linking PPP1R35 with microcephaly protein Rotatin and with roles in centrosome formation, we showed that the mutant embryos Ppp1r35 shortage of primary cilia.
Histological and molecular analysis of mutants revealed that the development of the notochord Ppp1r35 irregular and discontinuous, and is consistent with a role in primary cilia, that the floor plate of the neural tube is not specified. Similar to other mutant embryos with defects in the function of centrioles, Ppp1r35 mutant displayed increased cell death that is prevalent in the neural tube and an increasing number of proliferative cells in prometaphase.
Description: A polyclonal antibody against ALPPL2. Recognizes ALPPL2 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC;ELISA:1:2000-1:5000, IHC:1:25-1:100
Description: A polyclonal antibody against ALPP/ALPPL2. Recognizes ALPP/ALPPL2 from Human, Mouse. This antibody is Unconjugated. Tested in the following application: WB, ELISA;WB:1/500-1/2000.ELISA:1/20000
Description: A polyclonal antibody for detection of ALPP/ALPPL2 from Human, Mouse. This ALPP/ALPPL2 antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the N-terminal region of human ALPP/ALPPL2
Description: A polyclonal antibody for detection of ALPP/ALPPL2 from Human, Mouse. This ALPP/ALPPL2 antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the N-terminal region of human ALPP/ALPPL2
Description: A polyclonal antibody for detection of ALPP/ALPPL2 from Human, Mouse. This ALPP/ALPPL2 antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the N-terminal region of human ALPP/ALPPL2
Description: Alkaline phosphatase, placental type encoded by ALPP is an alkaline phosphatase, a metalloenzyme that catalyzes the hydrolysis of phosphoric acid monoesters. It belongs to a multigene family composed of four alkaline phosphatase isoenzymes. The enzyme functions as a homodimer and has a catalytic site containing one magnesium and two zinc ions, which are required for its enzymatic function. The protein is primarily expressed in placental and endometrial tissue; however, strong ectopic expression has been detected in ovarian adenocarcinoma, serous cystadenocarcinoma, and other ovarian cancer cells.
Description: Alkaline phosphatase, placental type encoded by ALPP is an alkaline phosphatase, a metalloenzyme that catalyzes the hydrolysis of phosphoric acid monoesters. It belongs to a multigene family composed of four alkaline phosphatase isoenzymes. The enzyme functions as a homodimer and has a catalytic site containing one magnesium and two zinc ions, which are required for its enzymatic function. The protein is primarily expressed in placental and endometrial tissue; however, strong ectopic expression has been detected in ovarian adenocarcinoma, serous cystadenocarcinoma, and other ovarian cancer cells.
Description: Alkaline phosphatase, placental type encoded by ALPP is an alkaline phosphatase, a metalloenzyme that catalyzes the hydrolysis of phosphoric acid monoesters. It belongs to a multigene family composed of four alkaline phosphatase isoenzymes. The enzyme functions as a homodimer and has a catalytic site containing one magnesium and two zinc ions, which are required for its enzymatic function. The protein is primarily expressed in placental and endometrial tissue; however, strong ectopic expression has been detected in ovarian adenocarcinoma, serous cystadenocarcinoma, and other ovarian cancer cells.
We hypothesize that the loss of homeostasis function abrogates Ppp1r35 centrioles, which resulted in failure to yield the major functional cilia, cell death and cell cycle delay / stalling that leads to the failure of development. Taken together, these results highlight the important function of Ppp1r35 during early mammalian development and involving this gene as a candidate for human microcephaly.
