Mandibular Appliance Modulates Condylar Growth through Integrins

2008 ◽  
Vol 87 (2) ◽  
pp. 153-158 ◽  
Author(s):  
M. Rubia Marques ◽  
D. Hajjar ◽  
K. Gomes Franchini ◽  
A. Sigari Moriscot ◽  
M. Fagundes Santos
Keyword(s):  
Cell Proliferation ◽  
Cell Binding ◽  
Cartilage Growth ◽  
Condylar Cartilage ◽  
Postural Changes ◽  
Maxilla And Mandible ◽  
Almost All ◽  
Binding Sequence ◽  
Immunohistochemical Analyses

Functional orthopedic therapy corrects growth discrepancies between the maxilla and mandible, possibly through postural changes in the musculature and modulation of the mandibular condylar cartilage growth. Using Wistar rats, we tested the hypothesis that chondrocytes respond to forces generated by a mandibular propulsor appliance by changes in gene expression, and that integrins are important mediators in this response. Immunohistochemical analyses demonstrated that the use of the appliance for different periods of time modulated the expression of fibronectin, α5 and αv integrin subunits, as well as cell proliferation in the cartilage. In vitro, cyclic distension of condylar cartilage-derived cells increased fibronectin mRNA, as well as Insulin-like Growth Factor-I and II mRNA and cell proliferation. A peptide containing the Arginine-Glycine-Asparagine sequence (RGD), the main cell-binding sequence in fibronectin, blocked almost all these effects, confirming that force itself modulates the growth of the rat condylar cartilage, and that RGD-binding integrins participate in mechanotransduction.

Synthesis and Activity of New Epipolythiopiperazine-2,5-dione Compounds. I.

1993 ◽  
Vol 46 (11) ◽  
pp. 1743 ◽  
Author(s):  
H Jiang ◽  
N Newcombe ◽  
P Sutton ◽  
QH Lin ◽  
A Mullbacher ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Biological Activity ◽  
Parent Compound ◽  
Reduced Form ◽  
Fungal Toxin ◽  
Naked Dna ◽  
Almost All ◽  
New Compounds ◽  
Proliferation In Vitro

The new lipophilic epipolythiopiperazine-2,5-diones 1,4-dibutylepidithiopiperazine-2,5-dione. 1,4-dibenzylepidithiopiperazine-2,5-dione, 1-benzyl-4-methylepidithiopiperazine-2,5-dione and 3,3′-dithiobis(1,4-dimethylpiperazine-2,5-dione) were synthesized. Unlike the parent compound, the fungal toxin and immunomodulating agent gliotoxin, these compounds did not affect macrophage adherence and cell proliferation in vitro. Like the reduced form of gliotoxin and other simple analogues, these new compounds induce oxidative damage to naked DNA. We conclude that an increase in lipophilicity plays no part in the biological activity of these compounds and in fact abrogates almost all activity. We also synthesized an intermolecular disulfide analogue which also lacked activity.

Evidence that α5β1 integrins mediate Leydig cell binding to fibronectin and enhance Leydig cell proliferation stimulated by a Sertoli cell-secreted mitogenic factor in vitro

Endocrine ◽  
1996 ◽  
Vol 5 (1) ◽  
pp. 75-83 ◽  
Author(s):  
Naixing Wu ◽  
Eisuke P. Murono ◽  
Wayne E. Carver ◽  
Louis Terracio ◽  
Thierry Bacro
Keyword(s):  
Cell Proliferation ◽  
Sertoli Cell ◽  
Leydig Cell ◽  
Cell Binding ◽  
Mitogenic Factor

Growth hormone stimulates the growth of mouse neonatal condylar cartilage in vitro

1989 ◽  
Vol 120 (4) ◽  
pp. 526-532 ◽  
Author(s):  
Gila Maor ◽  
Zeev Hochberg ◽  
Michael Silbermann
Keyword(s):  
Growth Hormone ◽  
Recombinant Human Growth Hormone ◽  
Human Growth ◽  
Hypertrophic Chondrocytes ◽  
Cartilage Growth ◽  
Condylar Cartilage ◽  
Igf I ◽  
In Vitro Effects ◽  
Vitro Effect

Abstract. This study used an organ culture system of neonatal condylar cartilage to study the in vitro effects of recombinant human growth hormone on the growth of cartilage and its inherent cell populations: progenitor cells, chondroblasts and early hypertrophic chondrocytes. Growth hormone at a dose of 2.5 nmol/l enhanced the overall growth of cartilage explant and stimulated the differentiation of its cells. Hence, growth hormonetreated explants revealed a substantial increase in the number of chondroblasts and young hypertrophic chondrocytes. Along with its effects upon cartilage the hormone also stimulated new bone formation adjacent to mineralized hypertrophic chondrocytes. These results provide support to the notion that growth hormone stimulates cartilage growth which in turn is followed by endochondral ossification. In spite of its in vitro effect it is not as yet clear whether the effect of growth hormone is indeed a direct one or is mediated via the local production of IGF-I.

Domain 5 of high molecular weight kininogen (kininostatin) down-regulates endothelial cell proliferation and migration and inhibits angiogenesis

Blood ◽  
2000 ◽  
Vol 95 (2) ◽  
pp. 543-550 ◽  
Author(s):  
Robert W. Colman ◽  
Bradford A. Jameson ◽  
Yingzhang Lin ◽  
Donald Johnson ◽  
Shaker A. Mousa
Keyword(s):  
Molecular Weight ◽  
Cell Proliferation ◽  
Cell Migration ◽  
Endothelial Cell ◽  
High Molecular Weight ◽  
Endothelial Cell Migration ◽  
Endothelial Cell Proliferation ◽  
High Molecular Weight Kininogen ◽  
Cell Binding

We have demonstrated that high molecular weight kininogen (HK) binds specifically on endothelial cells to domain 2/3 of the urokinase receptor (uPAR). Inhibition by vitronectin suggests that kallikrein-cleaved HK (HKa) is antiadhesive. Plasma kallikrein bound to HK cleaves prourokinase to urokinase, initiating cell-associated fibrinolysis. We postulated that HK cell binding domains would inhibit angiogenesis. We found that recombinant domain 5 (D5) inhibited endothelial cell migration toward vitronectin 85% at 0.27 μM with an IC50 (concentration to yield 50% inhibition) = 0.12 μM. A D5 peptide, G486-K502, showed an IC50 = 0.2 μM, but a 25-mer peptide from a D3 cell binding domain only inhibited migration 10% at 139 μM (IC50 > 50 μM). D6 exhibited weaker inhibitory activity (IC50 = 0.50 μM). D5 also potently inhibited endothelial cell proliferation with an IC50 = 30 nM, while D3 and D6 were inactive. Using deletion mutants of D5, we localized the smallest region for full activity to H441-D474. To further map the active region, we created a molecular homology model of D5 and designed a series of peptides displaying surface loops. Peptide 440-455 was the most potent (IC50 = 100 nM) in inhibiting proliferation but did not inhibit migration. D5 inhibited angiogenesis stimulated by fibroblast growth factor FGF2 (97%) in a chicken chorioallantoic membrane assay at 270 nM, and peptide 400-455 was also inhibitory (79%). HK D5 (for which we suggest the designation, “kininostatin”) is a potent inhibitor of endothelial cell migration and proliferation in vitro and of angiogenesis in vivo.

In Vitro and in Vivo Comparison of Binding of 99m-Tc-Iabeled Anti-CEA MAb F33-104 with 99m-Tc-labeled Anti-CEA MAb BW431/26

1999 ◽  
Vol 38 (04) ◽  
pp. 115-119
Author(s):  
N. Oriuchi ◽  
S. Sugiyama ◽  
M. Kuroki ◽  
Y. Matsuoka ◽  
S. Tanada ◽  
...  
Keyword(s):  
Nude Mice ◽  
Binding Capacity ◽  
Colon Adenocarcinoma ◽  
Human Colon ◽  
Cell Binding ◽  
Vitro Binding ◽  
Labeling Method ◽  
Human Colon Adenocarcinoma

Summary Aim: The purpose of this study was to assess the potential for radioimmunodetection (RAID) of murine anti-carcinoembryonic antigen (CEA) monoclonal antibody (MAb) F33-104 labeled with technetium-99m (99m-Tc) by a reduction-mediated labeling method. Methods: The binding capacity of 99m-Tc-labeled anti-CEA MAb F33-104 with CEA by means of in vitro procedures such as immunoradiometric assay and cell binding assay and the biodistribution of 99m-Tc-labeled anti-CEA MAb F33-104 in normal nude mice and nude mice bearing human colon adenocarcinoma LS180 tumor were investigated and compared with 99m-Tc-labeled anti-CEA MAb BW431/26. Results: The in vitro binding rate of 99m-Tc-labeled anti-CEA MAb F33-104 with CEA in solution and attached to the cell membrane was significantly higher than 99m-Tclabeled anti-CEA MAb BW431/261 (31.4 ± 0.95% vs. 11.9 ± 0.55% at 100 ng/mL of soluble CEA, 83.5 ± 2.84% vs. 54.0 ± 2.54% at 107 of LS 180 cells). In vivo, accumulation of 99m-Tc-labeled anti-CEA MAb F33-104 was higher at 18 h postinjection than 99m-Tc-labeled anti-CEA MAb BW431/26 (20.1 ± 3.50% ID/g vs. 14.4 ± 3.30% ID/g). 99m-Tcactivity in the kidneys of nude mice bearing tumor was higher at 18 h postinjection than at 3 h (12.8 ± 2.10% ID/g vs. 8.01 ± 2.40% ID/g of 99m-Tc-labeled anti-CEA MAb F33-104, 10.7 ± 1.70% ID/g vs. 8.10 ± 1.75% ID/g of 99m-Tc-labeled anti-CEA MAb BW431/26). Conclusion: 99m-Tc-labeled anti-CEA MAb F33-104 is a potential novel agent for RAID of recurrent colorectal cancer.

IN VITRO METHODS FOR THE STUDY OF THE ADENOHYPOPHYSIAL FUNCTIONS TO SECRETE GONADOTROPHIN

1971 ◽  
Vol 68 (1_Suppl) ◽  
pp. S27-S40 ◽  
Author(s):  
T. Kobayashi ◽  
T. Kigawa ◽  
M. Mizuno ◽  
T. Watanabe
Keyword(s):  
Cell Culture ◽  
Organ Culture ◽  
Cultured Cells ◽  
Cell Sheet ◽  
Short Term ◽  
Hypothalamic Extract ◽  
Numerous Cell ◽  
Single Cell Culture ◽  
Almost All

ABSTRACT There are several in vitro methods to analyse the function of the adenohypophysis or the mechanisms of its regulation. The present paper deals with single cell culture, organ culture and short term incubation techniques by which the morphology and gonadotrophin-secreting function of the adenohypophysis were studied. In trypsin-dispersed cell culture, the adenohypophysial cells showed extensive propagation to form numerous cell colonies and finally develop into a confluent monolayer cell sheet covering completely the surface of culture vessels. Almost all of the cultured cells, however, became chromophobic, at least at the end of the first week of cultivation, when gonadotrophin was detectable neither in the culture medium nor in the cells themselves. After the addition of the hypothalamic extract, gonadotrophin became detectable again, and basophilic or PAS-positive granules also reappeared within the cells, suggesting that the gonadotrophs were stimulated by the extract to produce gonadotrophin. In organ culture and short term incubation, the incorporation of [3H] leucine into the adenohypophysial cells in relation to the addition of hypothalamic extract was examined. It was obvious that the ability to incorporate [3H] leucine into the gonadotrophs in vitro was highly dependent upon the presence of the hypothalamic extract.

Role of 4-O Galloylchlorogenic Acid in Lung Cancer- An Insilico Approach

2017 ◽  
Vol 9 (5) ◽  
Author(s):  
Jaynthy C. ◽  
N. Premjanu ◽  
Abhinav Srivastava
Keyword(s):  
Lung Cancer ◽  
Cell Proliferation ◽  
In Silico ◽  
Computational Study ◽  
Regulation Mechanism ◽  
Down Regulation ◽  
Fruit Extract ◽  
In Vitro Techniques ◽  
Discovery Studio

Cancer is a major disease with millions of patients diagnosed each year with high mortality around the world. Various studies are still going on to study the further mechanisms and pathways of the cancer cell proliferation. Fucosylation is one of the most important oligosaccharide modifications involved in cancer and inflammation. In cancer development increased core fucosylation by FUT8 play an important role in cell proliferation. Down regulation of FUT8 expression may help cure lung cancer. Therefore the computational study based on the down regulation mechanism of FUT8 was mechanised. Sapota fruit extract, containing 4-Ogalloylchlorogenic acid was used as the inhibitor against FUT-8 as target and docking was performed using in-silico tool, Accelrys Discovery Studio. There were several conformations of the docked result, and conformation 1 showed 80% dock score between the ligand and the target. Further the amino acids of the inhibitor involved in docking were studied using another tool, Ligplot. Thus, in-silico analysis based on drug designing parameters shows that the fruit extract can be studied further using in-vitro techniques to know its pharmacokinetics.

Age-Related Changes in the Effects of Serum from Lean and Obese Pigs on Myogenic Cell Proliferation in Vitro

1982 ◽  
Vol 54 (4) ◽  
pp. 763-768 ◽  
Author(s):  
Ronald E. Allen ◽  
Gail Robinson ◽  
Matthew J. Parsons ◽  
Robert A. Merkel ◽  
William T. Magee
Keyword(s):  
Cell Proliferation ◽  
Myogenic Cell ◽  
Age Related ◽  
Proliferation In Vitro ◽  
Age Related Changes

Proliferative Effect of Tilapia Fish (Oreochromis niloticus) Lectin on BALB/c Mice Splenocytes

2019 ◽  
Vol 26 (12) ◽  
pp. 887-892
Author(s):  
Cynarha Daysy Cardoso da Silva ◽  
Cristiane Moutinho Lagos de Melo ◽  
Elba Verônica Matoso Maciel Carvalho ◽  
Mércia Andréa Lino da Silva ◽  
Rosiely Félix Bezerra ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Oreochromis Niloticus ◽  
Cytokine Production ◽  
Thymidine Incorporation ◽  
Con A ◽  
Cell Viability Assay ◽  
Proliferative Effect ◽  
Viability Assay ◽  
Apoptosis And Necrosis

Background: Lectins have been studied in recent years due to their immunomodulatory activities. Objective: We purified a lectin named OniL from tilapia fish (Oreochromis niloticus) and here we analyzed the cell proliferation and cytokine production in Balb/c mice splenocytes. Methods: Cells were stimulated in vitro in 24, 48, 72 hours and 6 days with different concentrations of OniL and Con A. Evaluation of cell proliferation was performed through [3H]-thymidine incorporation, cytokines were investigated using ELISA assay and cell viability assay was performed by investigation of damage through signals of apoptosis and necrosis. Results: OniL did not promote significant cell death, induced high mitogenic activity in relation to control and Con A and stimulated the cells to release high IL-2 and IL-6 cytokines. Conclusion: These findings suggest that, like Con A, OniL lectin can be used as a mitogenic agent in immunostimulatory assays.

In Vitro Immunodetection of Prothymosin Alpha in Normal and Pathological Conditions

2020 ◽  
Vol 27 (29) ◽  
pp. 4840-4854 ◽  
Author(s):  
Chrysoula-Evangelia Karachaliou ◽  
Hubert Kalbacher ◽  
Wolfgang Voelter ◽  
Ourania E. Tsitsilonis ◽  
Evangelia Livaniou
Keyword(s):  
Mammalian Cells ◽  
Therapeutic Potential ◽  
Prothymosin Alpha ◽  
Disease States ◽  
Leading Role ◽  
Tissue Extracts ◽  
Biologic Response ◽  
Health And Disease ◽  
Almost All

Prothymosin alpha (ProTα) is a highly acidic polypeptide, ubiquitously expressed in almost all mammalian cells and tissues and consisting of 109 amino acids in humans. ProTα is known to act both, intracellularly, as an anti-apoptotic and proliferation mediator, and extracellularly, as a biologic response modifier mediating immune responses similar to molecules termed as “alarmins”. Antibodies and immunochemical techniques for ProTα have played a leading role in the investigation of the biological role of ProTα, several aspects of which still remain unknown and contributed to unraveling the diagnostic and therapeutic potential of the polypeptide. This review deals with the so far reported antibodies along with the related immunodetection methodology for ProTα (immunoassays as well as immunohistochemical, immunocytological, immunoblotting, and immunoprecipitation techniques) and its application to biological samples of interest (tissue extracts and sections, cells, cell lysates and cell culture supernatants, body fluids), in health and disease states. In this context, literature information is critically discussed, and some concluding remarks are presented.

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