Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 17 de 17
Filter
1.
Journal of Southern Medical University ; (12): 893-898, 2020.
Article in Chinese | WPRIM | ID: wpr-828897

ABSTRACT

OBJECTIVE@#To analyze the association of integrinα5 (ITGA5) with grading of liver cancer and the overall patient survival and investigate the effects of integrin α5 (ITGA5) silencing on the proliferation, invasion and migration abilities of human liver cancer Bel-7404 cells.@*METHODS@#UALCAN was used to analyze the expression of ITGA5 in liver cancer tissues and normal tissues, and expression in different grades of liver cancer tissues. GEPIA was used to analyze the relationship between ITGA5 expression and the survival of liver cancer patients through.The ITGA5 shRNA lentiviral vector was used to infect Bel-7404 cells to establish a cell line with stable ITGA5 silencing verified by Western blotting. Plate clone formation assay and Transwell assay were used to detect the proliferation, invasion and migration of Bel-7404 cells. The correlation between ITGA5 and PI3K in liver cancer tissues and control tissues was analyzed using Oncomine cancer specimen database.@*RESULTS@#The expression of ITGA5 was significantly higher in liver cancer than in normal tissues ( < 0.05). The expression of ITGA5 was significantly lower in grade 1 than in grade 2 liver cancer, and also lower in grade 2 than in grade 3 liver cancer ( < 0.05). The patients with high ITGA5 expression had a significantly lower overall survival rate than those with low ITGA5 expression ( < 0.05). Plate clone formation assay showed that the clone formation rate was significantly lowered in Bel-7404 cells with ITGA5 silencing compared with the blank and negative control cells ( < 0.05). ITGA5 silencing significantly attenuated the migration of Bel-7404 cells as shown by Transwell assay ( < 0.05). ITGA5 and PI3K were both highly expressed and showed a positive correlation in liver cancer tissues ( < 0.05).@*CONCLUSIONS@#ITGA5 is closely related to the progression of liver cancer and the patients' prognosis. ITGA5 silencing inhibits the proliferation, invasion and migration of liver cancer cells. ITGA5 promotes the liver cancer growth and metastasis possibly by regulating the PI3K signaling pathway.


Subject(s)
Humans , Cell Line, Tumor , Cell Movement , Cell Proliferation , Gene Expression Regulation, Neoplastic , Integrin alpha5 , Liver Neoplasms , Neoplasm Invasiveness , Phosphatidylinositol 3-Kinases
2.
Biomolecules & Therapeutics ; : 62-66, 2016.
Article in English | WPRIM | ID: wpr-20737

ABSTRACT

Amygdalin, D-mandelonitrile-beta-D-glucoside-6-beta-glucoside, belongs to aromatic cyanogenic glycoside group derived from rosaceous plant seed. Mounting evidence has supported the anti-cancer effects of amygdalin. However, whether amygdalin indeed acts as an anti-tumor agent against breast cancer cells is not clear. The present study aimed to investigate the effect of amygdalin on the proliferation of human breast cancer cells. Here, we show that amygdalin exerted cytotoxic activities on estrogen receptors (ER)-positive MCF7 cells, and MDA-MB-231 and Hs578T triple-negative breast cancer (TNBC) cells. Amygdalin induced apoptosis of Hs578T TNBC cells. Amygdalin downregulated B-cell lymphoma 2 (Bcl-2), upregulated Bcl-2-associated X protein (Bax), activated of caspase-3 and cleaved poly ADP-ribose polymerase (PARP). Amygdalin activated a pro-apoptotic signaling molecule p38 mitogen-activated protein kinases (p38 MAPK) in Hs578T cells. Treatment of amygdalin significantly inhibited the adhesion of Hs578T cells, in which integrin alpha5 may be involved. Taken together, this study demonstrates that amygdalin induces apoptosis and inhibits adhesion of breast cancer cells. The results suggest a potential application of amygdalin as a chemopreventive agent to prevent or alleviate progression of breast cancer, especially TNBC.


Subject(s)
Humans , Adenosine Diphosphate Ribose , Amygdalin , Apoptosis , bcl-2-Associated X Protein , Breast Neoplasms , Caspase 3 , Integrin alpha5 , Lymphoma, B-Cell , MCF-7 Cells , p38 Mitogen-Activated Protein Kinases , Plants , Receptors, Estrogen , Triple Negative Breast Neoplasms
3.
Chinese journal of integrative medicine ; (12): 438-444, 2014.
Article in English | WPRIM | ID: wpr-267210

ABSTRACT

<p><b>OBJECTIVE</b>To investigate the effect of Ganfukang (GFK) on connective tissue growth factor (CTGF) and focal adhesion kinase (FAK)/protein kinase B (PKB or Akt) signal pathway in a hepatic fibrosis rat model and to explore the underlying therapeutic molecular mechanisms of GFK.</p><p><b>METHODS</b>Fifty SD rats were randomly divided into five groups as follows: the control group, the model group (repeated subcutaneous injection of CCl4), and the three GFK treatment groups (31.25, 312.5, and 3125 mg/kg, intragastric administration). Reverse transcriptase-polymerase chain reaction (RT-PCR), Western blotting, and immunohistochemistry were used to examine the expression of CTGF, integrin α5, integrin β1, FAK/Akt signal pathway, cyclinD1, and collagen in the different-treated rats.</p><p><b>RESULTS</b>GFK attenuated the up-regulation of CTGF, integrin α5, and integrin β1 in hepatic fibrosis rats and suppressed both the phosphorylation of FAK and the phosphorylation of Akt simultaneously (P<0.01). At the same time, the expression of cyclinD1, collagen I, and collagen III was decreased by GFK significantly (P<0.01).</p><p><b>CONCLUSIONS</b>CTGF and FAK/Akt signal pathway were activated in the CCl4-induced hepatic fibrosis rats, which contribute to increased expression of cyclinD1 and collagen genes. The mechanisms of the anti-fibrosis activity of GFK may be due to its effects against CTGF and FAk/Akt signal pathway.</p>


Subject(s)
Animals , Female , Male , Collagen , Genetics , Metabolism , Connective Tissue Growth Factor , Genetics , Metabolism , Cyclin D1 , Genetics , Metabolism , Drugs, Chinese Herbal , Pharmacology , Therapeutic Uses , Focal Adhesion Protein-Tyrosine Kinases , Metabolism , Gene Expression Regulation , Integrin alpha5 , Genetics , Metabolism , Integrin beta1 , Genetics , Metabolism , Liver , Pathology , Liver Cirrhosis , Drug Therapy , Genetics , Pathology , Phosphorylation , Proto-Oncogene Proteins c-akt , Metabolism , Rats, Sprague-Dawley , Signal Transduction
4.
IJRM-Iranian Journal of Reproductive Medicine. 2014; 12 (10): 687-694
in English | IMEMR | ID: emr-148984

ABSTRACT

Endometrial integrin expression changes might be a reason for implantation failure in polycystic ovarian syndromes [PCOS]. Assessment of integrin genes and proteins expression upon endometrium in the PCOS experimental mouse model was the main goal of this study. 30 NMRI female mice were equally divided into control, experimental [PCOS; received estradiol valerate [40 mg/kg]] and sham group [received; olive oil]. After 8 weeks, each group was hyper stimulated by 7 IU PMSG and then, after 48hrs, 7 IU HCG was injected. Vaginal plaque was checked. After 5 days, Progesterone and estradiol levels and endometrial tissues were investigated to evaluate of alpha4, alphav, beta1 and beta3 integrins gene and protein by qPCR method and immunohistochemistry, respectively. Tissue samples were assessed and showed that level of progesterone was significantly decreased in PCOS group. Results of molecular part in the amount of alphav, beta3, beta1 and alpha4 gene expressions showed a great difference in beta3 and alphav genes expressions between experimental groups, alphav, beta3, alpha4 and beta1 proteins in the endometrial stroma in the control group were expressed, but they were not detected in PCOS group. According to the results, integrins had different expression patterns in different areas of the endometrium; such as epithelial and stromal. It seems that in PCOS, this pattern has changed and the results might have a great influence on implantation failure. Therefore, this study suggests that a great attention to this problem may be essential in patients who are involved


Subject(s)
Animals, Laboratory , Integrin alpha4 , Integrin alpha5 , Integrin beta3 , Integrin beta1 , Integrins , Endometrium , Mice , Gene Expression , Embryo Implantation
5.
Chinese Medical Journal ; (24): 3443-3448, 2014.
Article in English | WPRIM | ID: wpr-240148

ABSTRACT

<p><b>BACKGROUND</b>The initial osteoblastic adhesion to materials characterizes the first phase of cell-material interactions and influences all the events leading to the formation of new bone. In a previous work, we developed a novel amorphous calcium phosphate (ACP)/poly(L-lactic acid) (PLLA) material that demonstrated morphologic variations in its microstructure. The aim of this study was to investigate the initial interaction between this material and osteoblastic cells. Cellular attachment and the corresponding signal transduction pathways were investigated.</p><p><b>METHODS</b>A porous ACP/PLLA composite and PLLA scaffold (as a control) were incubated in fetal bovine serum (FBS) containing phosphate-buffered saline (PBS), and the protein adsorption was determined. Osteoblastic MG63 cells were seeded on the materials and cultured for 1, 4, 8, or 24 hours. Cell attachment was evaluated using the MTS method. Cell morphology was examined using scanning electron microscopy (SEM). The expression levels of the genes encoding integrin subunits α1, α5, αv, β1, focal adhesion kinase (FAK), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were determined using real-time reverse transcription polymerase chain reaction (RT-PCR).</p><p><b>RESULTS</b>The ACP/PLLA material significantly increased the protein adsorption by 6.4-fold at 1 hour and 2.4-fold at 24 hours, compared with the pure PLLA scaffold. The attachment of osteoblastic cells to the ACP/PLLA was significantly higher than that on the PLLA scaffold. The SEM observation revealed a polygonal spread shape of cells on the ACP/ PLLA, with the filopodia adhered to the scaffold surface. In contrast, the cells on the PLLA scaffold exhibited a spherical or polygonal morphology. Additionally, real-time RT-PCR showed that the genes encoding the integrin subunits α1, αv, β1, and FAK were expressed at higher levels on the ACP/PLLA composite.</p><p><b>CONCLUSIONS</b>The ACP/PLLA composite promoted protein adsorption and osteoblastic adhesion. The enhanced cell adhesion may be mediated by the binding of integrin subunits α1, αv, and β1, and subsequently may be regulated through the FAK signal transduction pathways.</p>


Subject(s)
Humans , Biocompatible Materials , Chemistry , Calcium Phosphates , Chemistry , Cell Adhesion , Physiology , Cells, Cultured , Focal Adhesion Protein-Tyrosine Kinases , Metabolism , Integrin alpha1 , Metabolism , Integrin alpha5 , Metabolism , Integrin alphaV , Metabolism , Integrin beta1 , Metabolism , Integrins , Genetics , Metabolism , Lactic Acid , Chemistry , Osteoblasts , Cell Biology , Porosity , Tissue Engineering , Methods
6.
Chinese Journal of Stomatology ; (12): 653-659, 2013.
Article in Chinese | WPRIM | ID: wpr-274164

ABSTRACT

<p><b>OBJECTIVE</b>To investigate the regulatory mechanisms of integrin α5 and β1 in osteoblast in the process of gingipains-induced apoptosis.</p><p><b>METHODS</b>Gingipains were isolated and purified from supernatants of Porphyromonas gingivalis W83 which was cultured under standard anaerobic conditions. MC3T3-E1 was challenged with or without 8.3480 U/L gingipains for 48 h and apoptosis was examined by transferase-mediated deoxyuridine triphosphate-biotin nick end labeling-(4-Amidinophenyl)-6-indolecarbamidine dihydrochloride (TUNEL-DAPI) staining. The expression of integrin α5 and β1 was analyzed by Western blotting after MC3T3-E1 was treated under different conditions.</p><p><b>RESULTS</b>Arginine-specific proteinases(Rgp) activity was (41.74 ± 2.11) U/L and lysine-specific proteinase(Kgp) was (1.02 ± 0.25) U/L.Gingipains induced MC3T3-E1 cells apoptosis after 48 h. Compared with control group, expression of integrin α5 and β1 was down-regulated by gingipains in a time-dependent manner within short periods ( ≤ 72 h), integrin α5 and β1 relative expression was (0.485 ± 0.039),(0.504 ± 0.002) at 48 h,(0.398 ± 0.058),(0.179 ± 0.001) at 72 h respectively (P < 0.05). After 72 h, integrin α5 expression in MC3T3-E1 cells was stable compared with control group while integrin β1 was still lower(control group:1.000 ± 0.000, 96 h:0.604 ± 0.003, 120 h: 0.357 ± 0.002) (P < 0.05). Proteinase inhibitor tosyl- L- lysine-chloromethyl-ketone(TLCK) effectively blocked the activity of gingipain and inhibited down-regulation of integrin α5 and β1 induced by gingipains from (0.398 ± 0.058,0.179 ± 0.001 ) to (0.781 ± 0.012, 0.857 ± 0.060) (P < 0.05). TLCK alone did not have any effect on integrin α5 and β1(P > 0.05). Gingipains also decreased integrin α5 and β1 in a dose-dependent manner.When cells were treated with 20.8700 U/L gingipains, integrin α5 and β1 relative expression reached to the lowest(0.105 ± 0.004,0.020 ± 0.000) (P < 0.05).</p><p><b>CONCLUSIONS</b>Gingipains inhibited the expression of integrin α5 and β1 in a time- and dose- dependent manner in osteoblasts in the process of apoptosis, which may not be mediated by direct proteolytic effect.</p>


Subject(s)
Animals , Mice , Adhesins, Bacterial , Pharmacology , Apoptosis , Cysteine Endopeptidases , Pharmacology , Dose-Response Relationship, Drug , Down-Regulation , Integrin alpha5 , Metabolism , Integrin beta1 , Metabolism , Osteoblasts , Cell Biology , Metabolism , Porphyromonas gingivalis , Chemistry , Serine Proteinase Inhibitors , Pharmacology , Time Factors , Tosyllysine Chloromethyl Ketone , Pharmacology
7.
Chinese Journal of Industrial Hygiene and Occupational Diseases ; (12): 341-346, 2013.
Article in Chinese | WPRIM | ID: wpr-343669

ABSTRACT

<p><b>OBJECTIVE</b>To observe the expressions of α-SMA, integrin α5 and fibronectin (Fn) in acute paraquat poisoned rats and the effect of PDTC. To investigate the mechanism of paraquat-induced pulmonary fibrosis.</p><p><b>METHODS</b>Sprague-Dawley rats were randomly divided into three experimental groups: Control group (6 rats), PQ group (36 rats) and PQ+PDTC group (36 rats). On the 1st, 3rd, the 7th, the 14th, the 28th and the 56th day after exposure, the protein expression of α smooth muscle actin (α-SMA) was evaluated by western blot. The mRNA levels of integrin α5 and fibronectin (Fn) were analyzed with real-time quantitative PCR (RT-PCR). Meanwhile, the lung pathological changes were observed and semi-quantified.</p><p><b>RESULTS</b>T With the time passing, the expression of α-SMA in PQ group increased gradually compared with control group (P < 0.05 or P < 0.01). The increasing extent was gently on the 3 rd, the 7 th day. While increasing extent was rapidly from the 28 th to the 56 th day. RT-PCR showed PQ significantly increased Fn mRNA level on all time points and increased integrin α5 mRNA level from the 7 rd to 56 th day compared with control group (P < 0.05 or P < 0.01). PDTC treatment significantly deceased α-SMA, Fn, and integrin α5 levels compared with PQ group in corresponding time points (P < 0.05 or P < 0.01) Noteworthy, in PQ+PDTC group, the occurrence of pathological changes were drastically attenuated and pathologic score significantly decreased (P < 0.05 or P < 0.01).</p><p><b>CONCLUSIONS</b>α-SMA, integrin α5 and fibronectin could play an important role in the development of pulmonary fibrosis caused by paraquat poisoning. PDTC, asa strong NF-κB inhibitor, may inhibit NF-κB activity and further significantly decreased expressions of α-SMA, integrin α5 and fibronectin which were important part of ECM, leading to drastically attenuated pulmonary fibrosis. However, the mechanisms of PDTC intervention still remains to be explored.</p>


Subject(s)
Animals , Male , Rats , Actins , Metabolism , Disease Models, Animal , Fibronectins , Metabolism , Integrin alpha5 , Metabolism , Paraquat , Poisoning , Pulmonary Fibrosis , Metabolism , Pyrrolidines , Pharmacology , Rats, Sprague-Dawley , Thiocarbamates , Pharmacology
8.
Experimental & Molecular Medicine ; : 166-174, 2010.
Article in English | WPRIM | ID: wpr-203596

ABSTRACT

Melanoma inhibiting activity/cartilage-derived retinoic acid-sensitive protein (MIA/CD-RAP) is a small soluble protein secreted from malignant melanoma cells and from chondrocytes. Recently, we revealed that MIA/CD-RAP can modulate bone morphogenetic protein (BMP)2-induced osteogenic differentiation into a chondrogenic direction. In the current study we aimed to find the molecular details of this MIA/CD-RAP function. Direct influence of MIA on BMP2 by protein-protein-interaction or modulating SMAD signaling was ruled out experimentally. Instead, we revealed inhibition of ERK signaling by MIA/CD-RAP. This inhibition is regulated via binding of MIA/CD-RAP to integrin alpha5 and abolishing its activity. Active ERK signaling is known to block chondrogenic differentiation and we revealed induction of aggrecan expression in chondrocytes by treatment with MIA/CD-RAP or PD098059, an ERK inhibitor. In in vivo models we could support the role of MIA/CD-RAP in influencing osteogenic differentiation negatively. Further, MIA/CD-RAP-deficient mice revealed an enhanced calcified cartilage layer of the articular cartilage of the knee joint and disordered arrangement of chondrocytes. Taken together, our data indicate that MIA/CD-RAP stabilizes cartilage differentiation and inhibits differentiation into bone potentially by regulating signaling processes during differentiation.


Subject(s)
Animals , Humans , Mice , Bone Morphogenetic Proteins/metabolism , Cartilage/cytology , Cell Differentiation , Chondrocytes/cytology , Extracellular Matrix Proteins/deficiency , Extracellular Signal-Regulated MAP Kinases/metabolism , Integrin alpha5/metabolism , Mesenchymal Stem Cells/cytology , Neoplasm Proteins/deficiency , Osteogenesis , Protein Binding , Signal Transduction , Smad Proteins/metabolism
9.
Chinese Journal of Oncology ; (12): 885-889, 2009.
Article in Chinese | WPRIM | ID: wpr-295213

ABSTRACT

<p><b>OBJECTIVE</b>To investigate the effects of PPARgamma ligand (rosiglitazone, RGZ) as well as combined with all trans-retinoic acid (ATRA) on human myeloma cells and try to explore the possible mechanism.</p><p><b>METHODS</b>Human myeloma cell lines U266 and RPMI-8226 cells were treated with RGZ in the presence or absence of ATRA. Cell proliferation was evaluated by [(3)H] thymidine incorporation, cell cycle distribution and CD49e expression were analyzed by flow cytometry, morphology changes were evaluated by Wright-Giemsa staining, and p27(Kip1) and p21(Waf1) expression was detected by Western blotting.</p><p><b>RESULTS</b>The exposure to RGZ induced proliferation inhibition in both cell lines in a dose-dependent manner. After cultured with 5 micromol/L RGZ, the proportion of U266 and RPMI-8226 cells in phase G(0)/G(1) was (45.2 +/- 6.7)% and (40.3 +/- 7.3)%, respectively (P < 0.05). The proportion of the cells in phase G(2)/M and S was (52.2 +/- 7.4)% and (57.4 +/- 9.5)%, respectively (P < 0.05). These changes were more evident when the RGZ concentration was increased to 10 micromol/L. A combination of RGZ with ATRA enhanced the growth inhibition and cell cycle arrest effects of RGZ. The RGZ-treated myeloma cells displayed morphological characteristics of cell differentiation, and more evident signs of differentiation were observed when RGZ was combined with ATRA. These changes were confirmed by the detection of CD49e expression. The expression of p27(Kip1) and p21(Waf1) in myeloma cells was up-regulated by RGZ and this change was more apparent when RGZ was used in combination with ATRA.</p><p><b>CONCLUSION</b>RGZ can induce cell cycle arrest and cell differentiation in myeloma cells which maybe caused by up-regulation of p27(Kip1) and p21(Waf1) expression. ATRA can enhance these effects of RGZ on multiple myeloma cells and combined use of these two drugs may show a synergistic effect on myeloma cells.</p>


Subject(s)
Humans , Cell Cycle , Cell Line, Tumor , Cell Proliferation , Cyclin-Dependent Kinase Inhibitor p21 , Metabolism , Cyclin-Dependent Kinase Inhibitor p27 , Dose-Response Relationship, Drug , Drug Synergism , Integrin alpha5 , Metabolism , Intracellular Signaling Peptides and Proteins , Metabolism , Multiple Myeloma , Metabolism , Pathology , PPAR gamma , Thiazolidinediones , Pharmacology , Tretinoin , Pharmacology , Up-Regulation
10.
The Journal of Korean Academy of Prosthodontics ; : 375-381, 2007.
Article in English | WPRIM | ID: wpr-25858

ABSTRACT

STATEMENT OF PROBLEM: Prior to determining an optimal width of micropatterned grooves provided on titanium substrata, we have done a pilot study using surface topographies in combined microm and submicrom levels. PURPOSE: The purpose of this study was twofold 1) to assess the proliferation and 2) to analyze the expression of genes encoding the intracellular signaling proteins involved in cell-substratum adhesions and adhesion-dependent G1 phase cell cycle progression of human gingival fibroblasts plated on smooth and microgrooved/acid-etched titanium substrata. MATERIAL AND METHODS: Three groups of titanium discs as NE0 (smooth Ti substrata), E15 (Ti substrata with microgrooves of 15 micrometer of spacing and 3.5 micrometer in depth and with further acidetching), and E30 (Ti substrata with microgrooves of 30 micrometer spacing and 3.5 micrometer in depth and with further acid-etching) served as the human gingival fibroblasts' substrata. Viability and proliferation of fibroblasts were determined using an XTT assay. Gene expressions of fibronectin, alpha5 integrin, CDK4, and p27(kip) were analyzed in RT-PCR. Cell-substratum interactions were analyzed in SEM. RESULTS: From the XTT assay at 24 h incubation, the mean optical density (OD) value of E15 was significantly greater than the values of E30 and NE0. At 48 and 96 h however, the mean OD values of E30 were significantly greater than the values of E15 and NE0. No differences in the expression of PCR transcripts at 96 h incubations were noted between groups, whereas at 48 h, an unexpected increase in the expression of all the transcripts were noted in E15 compared with other two groups. Fibroblasts were observed to orient and adhere inside the microgrooves. CONCLUSION: Micropatterned grooves and acid-etching on Ti substrata alter viability and gene expression of adhered human gingival fibroblasts.


Subject(s)
Humans , Cell Cycle , Fibroblasts , Fibronectins , G1 Phase , Gene Expression , Integrin alpha5 , Intracellular Signaling Peptides and Proteins , Pilot Projects , Polymerase Chain Reaction , Titanium
11.
National Journal of Andrology ; (12): 148-150, 2006.
Article in Chinese | WPRIM | ID: wpr-338344

ABSTRACT

<p><b>OBJECTIVE</b>To explore the correlation between the expression of integrin subunits alpha5 and beta1 in prostate cancer (PCa) and its clinicopathological data including tumor grade and clinical stage.</p><p><b>METHODS</b>Expressions of integrin subunits alpha5 and beta1 were examined in 30 cases of PCa and 30 cases of normal prostatic tissues by immunohistochemical assay.</p><p><b>RESULTS</b>Expressions of integrin subunits alpha5 and beta1 in PCa were lower than those in normal prostatic tissues (P <0.05) respectively.</p><p><b>CONCLUSION</b>Compared with normal prostatic tissues, expressions of integrin subunits alpha5 and beta1 in PCa were rather weaker or even faded. Expressions of integrin subunits alpha5 and beta1 revealed an positive correlation with tumor's Gleason grade and negative with clinical TNM stage. The results indicate that integrin subunits alpha5 and beta1 have potential values in the diagnosis and are predictable indices in the proliferation of PCa.</p>


Subject(s)
Aged , Aged, 80 and over , Animals , Humans , Male , Mice , Middle Aged , Integrin alpha5 , Integrin alpha5beta1 , Neoplasm Staging , Prostatic Hyperplasia , Metabolism , Prostatic Neoplasms , Metabolism , Pathology
12.
Chinese Journal of Hematology ; (12): 240-243, 2006.
Article in Chinese | WPRIM | ID: wpr-243966

ABSTRACT

<p><b>OBJECTIVE</b>To investigate the biological behavior of stromal cell-derived factor-1 (SDF-1) on multiple myeloma (MM) cell migration and adhesion and it related signaling pathways.</p><p><b>METHODS</b>Expression of adhesion molecules on MM cells of RPMI8226, XG-1 and XG-7 cells was analysed by flow cytometry, the influence of SDF-1 on CD29 and CD49e distribution by immunofluorescence, the effect of SDF-1 on chemotaxis of MM cells by transwell assay. Activation of phosphoinositide-3 kinase (PI3K) in MM cells treated with SDF-1 and by immunoblotting.</p><p><b>RESULTS</b>3 strains of MM cell line expressed many adhesion molecule. RPMI8226, XG-7 cells were all high level of expression of CD29 (> 70%). XG-1, XG-7 cells were all high level of expression of CD44 (> 80%), and XG-7 cells was of CD49d (> 90%). In all of 3 strains, the levels of expression of CD49e were low (< 30%). SDF-1 could not upregulate their expression, but could trigger the establishment of polarized morphology of MM cells and the redistribution of CD29 and CD49e. SDF-1 promoted MM cells adhesion to endothelial cells, stimulated phosphorylation of P85 subunit of PI3K in MM cells and induced MM cells migration, which were inhibited by G protein inhibitor PTX and PI3K inhibitor wortmannin.</p><p><b>CONCLUSION</b>SDF-1 can promote MM cell adhesion to endothelial cells, trigger establishment of a polarized morphology of MM cells and redistribution of adhesion molecules and induce MM cells migration via PI3K signaling pathway.</p>


Subject(s)
Humans , Blotting, Western , Cell Adhesion , Physiology , Cell Adhesion Molecules , Metabolism , Cell Line, Tumor , Cell Movement , Physiology , Chemokine CXCL12 , Pharmacology , Physiology , Enzyme Activation , Flow Cytometry , Fluorescent Antibody Technique , Integrin alpha4 , Metabolism , Integrin alpha5 , Metabolism , Integrin beta1 , Metabolism , Multiple Myeloma , Metabolism , Pathology , Phosphatidylinositol 3-Kinases , Metabolism , Signal Transduction , Physiology
13.
Journal of Experimental Hematology ; (6): 582-586, 2006.
Article in Chinese | WPRIM | ID: wpr-233541

ABSTRACT

The aim of this study was to evaluate the homing capabilities of hematopoietic stem/progenitor cells (HSPCs) derived from human placenta tissues (PT). Single cell suspension of human PT was prepared by mechanical method. The expression levels of homing-related adhesion molecules (HRAM) including CD11a, CD49d, CD44, CD49e, CD62L and CD54 on CD34(+) cells and the percentages of CD34(+) cells and their subpopulations in nucleated cells (NC) from fresh human PT, umbilical cord arterial blood (UCAB) and umbilical cord venous blood (UCVB) were detected by using flow cytometry. The results showed that the percentage of CD34(+) cells and CD34(+)CD38(-) cells in placenta were higher than those in UCAB and UCVB. There were no significant difference in percentage of HSPC between UCAB and UCVB. Placenta-derived CD34(+) cells strongly expressed CD11a, CD49d, CD44, CD49e and CD54, among which expression levels of CD49e and CD54 on placenta-derived CD34(+) cells were significantly higher than those on UCAB and UCVB-derived CD34(+) cells. While the percentage of CD34(+)CD62L(+) cells in placenta was only lower than that in UCVB. It is concluded that human placenta is rich in HSPC. Moreover, the expression levels of most HRAM in CD34(+) cells from PT are higher than those from UCAB and UCVB or are close to them. It suggested that HSPCs derived from PT might have stronger homing capabilities than those from UCB.


Subject(s)
Humans , Antigens, CD34 , Cell Adhesion Molecules , Fetal Blood , Cell Biology , Hematopoietic Stem Cells , Metabolism , Hyaluronan Receptors , Integrin alpha5 , Intercellular Adhesion Molecule-1 , Placenta , Cell Biology
14.
Chinese Journal of Oncology ; (12): 253-256, 2006.
Article in Chinese | WPRIM | ID: wpr-236993

ABSTRACT

<p><b>OBJECTIVE</b>To analyze the drug-sensitivity-related genes to anti-tumor drugs navalbine (NVB) and docetaxel (Doc) in four SCLC and six NSCLC cell lines.</p><p><b>METHODS</b>The sensitivity of 4 SCLC lines and 6 NSCLC lines to NVB and to Doc was determined with MTT test. The expression of 1291 anti-tumor drug sensitivity-related genes in the 10 cell lines was assayed by cDNA macroarray technique, and cluster analysis was performed to find the relationship between the results obtained by the above mentioned two measurements.</p><p><b>RESULTS</b>(1) The anti-tumor effect of NVB on the 10 cell lines was apparently better than that of Doc. (2) The drug sensitivity-related genes in these 10 cell lines showed a more close positive correlation with Doc than that with NVB, whereas more genes showed negative correlation with NVB than that with Doc. But in 6 NSCLC cell lines, more genes showed the same positive or negative correlation with the two drugs. (3) 51 genes in the 10 cell lines showed correlation with Doc or NVB. 13 of them had negative correlation with Doc, 11 of them showed positive correlation. 24 of them showed negative correlation with NVB, 3 of them showed positive correlation. 67 genes in 6 NSCLC cell lines showed a correlation with sensitivity to Doc or NVB, among them 34 had negative correlation with Doc, 4 had positive correlation. 25 genes had negative correlation with NVB, 4 had positive correlation. (4) Rab 1, Rab 3, Rho B, Rho C, Rac 1, Rac 2, Gho GDI beta, CD44, integrin alpha5, integrin alpha6, integrin beta5, vinculin showed to be cytoskeleton-related genes differently expressing in SCLC or NSCLC cell lines.</p><p><b>CONCLUSION</b>There is obvious difference in the drug sensitivity-related genes to NVB or Doc between SCLC and NSCLC cell lines.</p>


Subject(s)
Humans , Antineoplastic Agents , Pharmacology , Cell Line, Tumor , Cluster Analysis , Cytoskeletal Proteins , Metabolism , Cytoskeleton , Genetics , Gene Expression Profiling , Gene Expression Regulation, Neoplastic , Integrin alpha5 , Metabolism , Lung Neoplasms , Genetics , Metabolism , Pathology , Oligonucleotide Array Sequence Analysis , Taxoids , Pharmacology , Vinblastine , Pharmacology , rab1 GTP-Binding Proteins , Metabolism , rac1 GTP-Binding Protein , Metabolism
15.
Korean Journal of Anatomy ; : 527-541, 2005.
Article in Korean | WPRIM | ID: wpr-650368

ABSTRACT

In postmenopausal osteoporosis, estrogen deficiency leads to unbalance of bone metabolism, decreased bone formation and increased bone resorption, and the result is reduced bone mineral density (BMD) and bone stiffness. The processes of bone formation and resorption involves the expression of integrins in anchoragedependent cells, such as osteoblast and osteoclast. The osteoporosis-induced rats frequently demonstrated the loss of trabecular bone volume in the tibia, vertebra and mandible due to estrogen depletion. However, in maxilla, study has been rare because of its anatomical limits. So the objective of this study was to investigate bony change and property of integrin expression in maxilla of osteoporosis-induced rats. 12-week-old female Sprague-Dawley rats were bilaterally ovariectomized (OVX). At 1, 2, 3, 4, 8 and 12 weeks, control and OVX group rats were sacrificed respectively. BMD of maxilla of the rats was measured using dual-energy X-ray absorptiometry (DEXA). And then the histopathologic observation, histomorphometric analysis and immunohistochemistry with CD44, alpha2 integrin, alpha5 integrin, alpha6 integrin, alphav integrin and beta3 integrin were done. BMD of alveolar bone in maxilla was decreased with significance statistically after OVX 4 weeks and was decreased 18.15% at OVX 12 weeks group compared to control group. From OVX 4 to 12 weeks, the thickness of periodontal ligament space was decreased, the number of osteoclast and the size of marrow stroma were increased than control group. By histomorphometric analysis, the size of marrow stroma of alveolar bone in maxilla was increased 86.42% at OVX 12 weeks group compared to control group. CD44 was widely expressed throughout the odontoblast, cementoblast, dental pulp, preiodontal ligament, osteocyte, osteoclast and perivascular tissue at control group, and CD44 immunoreactivity was increased the odontoblast, osteoblast and osteoclast at OVX groups. alpha2 integrin was expressed the odontoblast and osteoblast at control group, but alpha2 integrin immunoreactivity was decreased the osteoblast at OVX 12 weeks group. alpha5 integrin was expressed the cementoblast, osteoblast and osteoclast at control group, and alpha5 integrin immunoreactivity was decreased the osteoblast and was increased the osteoclast from OVX 4 weeks group. alpha6 integrin was weakly expressed the odontoblast, cementoblast, osteoblast and osteoclast at control group, and alpha6 integrin immunoreactivity was weakly increased the osteoclast from OVX 4 weeks. alphav integrin was expressed the odontoblast and osteoclast at control group, and alphav integrin immunoreactivity was strongly increased the osteoclast from OVX 4 weeks. beta3 integrin was expressed the osteocyte and osteoclast at control group, and beta3 integrin immunoreactivity was strongly increased the osteoclast from OVX 4 weeks. From these results, alveolar bone in maxilla of OVX rats was decreased BMD gradually. Moreover, alpha2 and alpha5 integrin expression of osteoblast was decreased, and alpha5, alphav and beta3 integrin expression of osteoclast was increased in OVX rats. Thus, this study indicates that consideration of reduced BMD is necessary in dental procedure of postmenopausal women.


Subject(s)
Animals , Female , Humans , Rats , Absorptiometry, Photon , Bone Density , Bone Marrow , Bone Resorption , Dental Cementum , Dental Pulp , Estrogens , Immunohistochemistry , Integrin alpha2 , Integrin alpha5 , Integrin alpha6 , Integrin alphaV , Integrin beta3 , Integrins , Ligaments , Mandible , Maxilla , Metabolism , Odontoblasts , Osteoblasts , Osteoclasts , Osteocytes , Osteogenesis , Osteoporosis, Postmenopausal , Ovariectomy , Periodontal Ligament , Rats, Sprague-Dawley , Spine , Tibia
16.
Chinese Journal of Surgery ; (12): 1605-1608, 2005.
Article in Chinese | WPRIM | ID: wpr-317217

ABSTRACT

<p><b>OBJECTIVE</b>To investigate the expression of integrin alpha5 and actin in the cells of intervertebral disc under cyclic hydrostatic pressure in vitro.</p><p><b>METHODS</b>The porcine lumbar intervertebral disc cells were isolated and cultured in vitro, and the cells underwent cyclic hydrostatic loading. After that, the expression of integrin alpha5 and actin in intervertebral disc cells were studied by means of morphology observing, Western blot and immunohistochemistry staining.</p><p><b>RESULTS</b>The morphology of intervertebral disc cells were changed into smaller and flatten shape, and the expression of integrin alpha5 and actin were decreased after loading.</p><p><b>CONCLUSIONS</b>The expression of integrin alpha5 decreases under cyclic hydrostatic pressure, and the actin is affected at the same time when signals are transferred into the cells by integrin alpha5. That may be one of the important mechanisms of the mechanotransduction in the cells of intervertebral disc.</p>


Subject(s)
Animals , Actins , Metabolism , Cells, Cultured , Hydrostatic Pressure , Integrin alpha5 , Metabolism , Intervertebral Disc , Cell Biology , Mechanotransduction, Cellular , Swine
17.
Chinese Journal of Hematology ; (12): 197-199, 2005.
Article in Chinese | WPRIM | ID: wpr-229872

ABSTRACT

<p><b>OBJECTIVE</b>To investigate the differentiation induction effect of 2-methoxyestradiol (2ME2), an estrogen derivative on myeloma cell line CZ-1.</p><p><b>METHODS</b>The changes of CZ-1 cells in morphology, expression of surface CD49e and quantity of light chain secretion in the supernatant were observed when treated with 0.1 approximately 0.5 micromol/L 2ME2 for 48 h.</p><p><b>RESULTS</b>2ME2 could induce differentiation of CZ-1 cells. The cells appeared decreased in size of nucleus, increased in cytoplasma, decreased in the ratio of nucleus to plasma, decreased in number or disappearance of nucleolus, and thickness and pyknosis of chromatin. The expression of CD49e was increased from (12.20 +/- 1.57)% to (24.80 +/- 1.26)% (P < 0.05). Light chain secretion in the supernatant was increased from (35.97 +/- 2.60) microg/ml to (79.67 +/- 1.88) microg/ml (P < 0.05).</p><p><b>CONCLUSION</b>Low concentrations of 2ME2 could induce differentiation of myeloma cell line CZ-1.</p>


Subject(s)
Humans , Cell Differentiation , Cell Line, Tumor , Dose-Response Relationship, Drug , Estradiol , Pharmacology , Flow Cytometry , Integrin alpha5 , Multiple Myeloma , Metabolism , Pathology , Tubulin Modulators , Pharmacology
SELECTION OF CITATIONS
SEARCH DETAIL