scholarly journals Concerted Upregulation of CLP36 and Smooth Muscle Actin Protein Expression in Human Endometrium during Decidualization

2005 ◽  
Vol 179 (3) ◽  
pp. 109-114 ◽  
Author(s):  
Ulrich Miehe ◽  
Peruka Neumaier-Wagner ◽  
Mamed Kadyrov ◽  
Pankaj Goyal ◽  
Joachim Alfer ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Expression ◽  
Smooth Muscle Actin ◽  
Human Endometrium ◽  
Muscle Actin ◽  
Actin Protein

Regulation of airway smooth muscle α-actin expression by glucocorticoids

2007 ◽  
Vol 292 (1) ◽  
pp. L99-L106 ◽  
Author(s):  
Adam M. Goldsmith ◽  
Marc B. Hershenson ◽  
Miguel P. Wolbert ◽  
J. Kelley Bentley
Keyword(s):  
Smooth Muscle ◽  
Protein Expression ◽  
Airway Smooth Muscle ◽  
Contractile Function ◽  
Smooth Muscle Actin ◽  
Mrna Translation ◽  
Contractile Protein ◽  
Muscle Actin ◽  
Actin Expression ◽  
Actin Protein

Airway smooth muscle hypertrophy appears to be present in severe asthma. However, the effect of corticosteroids on airway smooth muscle cell size or contractile protein expression has not been studied. We examined the effects of dexamethasone, fluticasone, and salmeterol on contractile protein expression in transforming growth factor (TGF)-β-treated primary bronchial smooth muscle cells. Dexamethasone and fluticasone, but not salmeterol, each reduced expression of α-smooth muscle actin and the short isoform of myosin light chain kinase. Steady-state α-actin mRNA level and stability were unchanged, consistent with posttranscriptional control. Fluticasone significantly decreased α-actin protein synthesis following treatment with the transcriptional inhibitor actinomycin D, indicative of an inhibitory effect on mRNA translation. Fluticasone also significantly increased α-actin protein turnover. Finally, fluticasone reduced TGF-β-induced incorporation of α-actin into filamentous actin, cell length, and cell shortening in response to ACh and KCl. We conclude that glucocorticoids reduce human airway smooth muscle α-smooth muscle actin expression and incorporation into contractile filaments, as well as contractile function, in part by attenuation of mRNA translation and enhancement of protein degradation.

scholarly journals Relationship Between the Immunodetection of Alpha-Smooth Muscle Actin and the Aggressiveness of Mammary Papillar Tumors in Female Dog

2019 ◽  
Vol 2 (1) ◽  
pp. 11-15
Author(s):  
Mayara Caroline Rosolem ◽  
Pamela Rodrigues Reina Moreira ◽  
Fábio Nelson Gava ◽  
Diego Felipe Alves Batista ◽  
Paulo Henrique Leal Bertolo ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Actin ◽  
Biological Behavior ◽  
Muscle Actin ◽  
Alpha Smooth Muscle Actin ◽  
Hematoxylin And Eosin ◽  
Hematoxylin And Eosin Staining ◽  
Actin Protein ◽  
Veterinary Hospital ◽  
Mammary Neoplasia

Papillary carcinoma is a mammary neoplasia of women and female dogs characterized by papillary fibrovascular projections lined by epithelial cells. Evaluation on the biology of these tumors can be done by immunohistochemistry through detection of alpha-smooth muscle actin protein in the papillary myoepithelium, which lacks such a molecule during malignant proliferations. Thus, this study aimed at determining the malignancy degree of papillary mammary tumors of female dogs by immunohistochemistry. Twenty samples of mammary neoplastic tissues collected from female dogs treated in the Veterinary Hospital at FCAV were evaluated by Hematoxylin and Eosin staining (H&E) and tumor cells were immunolabelled with monoclonal antibody to alpha-smooth muscle actin (α-SMA). Five out of 20 cases showed positive immunolabeling greater than 10% of the total immunolabeling. The remaining fourteen cases presented immunostaining lesser than 10% showing decrease or absence of α-SMA labeling in the myoepithelium of the papilla tumors. All those cases in which immunostained cell was over 10% of the neoplasm (5 immunostains of 20 total cases) were classified as benign whereas those below 10% of immunostained in the slid were considered as malignant. Therefore, immunohistochemistry played an essential role in differentiating benign and malignant papillary tumors of bitches as already described for female. Tumor classification by conventional methods, such as H&E staining, can lead to erroneous interpretations on the real biological behavior of the papillary mammary tumor.

Lässt sich die Expression von EZM-Proteinen durch Kompression beeinflussen?

Phlebologie ◽  
2012 ◽  
Vol 41 (03) ◽  
pp. 121-127
Author(s):  
J. Brinckmann ◽  
D. Zillikens ◽  
B. Kahle ◽  
O. Gerdes
Keyword(s):  
Smooth Muscle ◽  
Protein Expression ◽  
Smooth Muscle Actin ◽  
Muscle Actin ◽  
Tenascin C ◽  
Klasse Ii

ZusammenfassungHintergrund: In den fortgeschrittenen Stadien der chronischen venösen Insuffizienz (CVI) werden die Proteine Tenascin C, Fibrillin 2 und α-smooth muscle Actin (αSMA) vermehrt ex-primiert. Diese Proteine der Extrazellularmatrix werden im Rahmen der Wundheilung und in hypertrophen Narben verstärkt gebildet. Die pathologische Expression in hypertrophen Narben kann durch Kompression normalisiert werden.Fragestellung: Wird die Expression der Proteine Tenascin C, Fibrillin 2 und αSMA im Stadium C2 und C4 der CVI durch Kompression be-einflusst?Methode: Untersucht wurden 23 Patienten mit CVI (12 Stadium C2, 11 Stadium C4) ohne bisherige Kompressionstherapie. Sie erhielten für 2 bzw. 4 Wochen einen medizinischen Kompressionsstrumpf (Klasse II oder Klasse III). An Tag 1, 14 und 28 wurde jeweils eine Hautprobe am Innenknöchel entnommen.Ergebnisse: Im Stadium C2 liegt ein Expressionsmuster wie in normaler Haut vor. Im Stadium C4 variiert die Expression je nach kli-nischem Erscheinungsbild. Bei Dermatoliposklerose zeigt sich in der gesamten Dermis eine vermehrte Expression von Fibrillin 2 und Tenascin C. Bei Hyperpigmentierung oder Stauungsekzem zeigt sich in wenigen Fällen eine vermehrte Expression in der Tiefe bzw. entlang der Basalmembran. αSMA lässt sich nur in den Wänden der dermalen Gefäße darstellen. Die Kompressionstherapie bewirkt in dem Untersuchungszeitraum keine Änderung der Protein-expression.Schlussfolgerung: Fibrillin 2 und Tenascin C zei-gen sich erst im Falle einer bestehenden Sklerose. Ein potenzieller Einfluss von Kompression auf die Expression dieser Parameter muss in weiteren Studien untersucht werden.

scholarly journals Cytotoxic Influence of Khat (Catha edulis (Vahl) Forssk. ex Endl) on Oral Fibroblasts, Squamous Carcinoma Cells, and Expression of α Smooth Muscle Actin

2021 ◽  
Vol 11 (8) ◽  
pp. 3524
Author(s):  
Azeem Ul Yaqin Syed ◽  
Muhammad A. Ahmed ◽  
Eman I. AlSagob ◽  
Mansour Al-Askar ◽  
Abdulrahman M. AlMubarak ◽  
...  
Keyword(s):  
Cell Death ◽  
Smooth Muscle ◽  
Smooth Muscle Actin ◽  
Control Cell ◽  
Squamous Carcinoma ◽  
Carcinoma Cells ◽  
Muscle Actin ◽  
Catha Edulis ◽  
Squamous Carcinoma Cells ◽  
Dose Dependent

The aim was to determine the cytotoxicity of Khat (Catha edulis (Vahl) Forssk. ex Endl) on normal oral fibroblasts (NOFs) and SCC4 (squamous carcinoma cells) along with expression of α-smooth muscle actin (α-SMA) in fibroblasts. Khat filtrate was prepared to obtain a concentrated viscous solution. NOFs and SCC4 cells were cultured in biological cabinets and were grown in Dulbeccos’ modified Eagles medium. Frozen cells were thawed at 37 °C and cell seeding was performed. NOFs and SCC4 cells were seeded on 96 well plates and allowed to attach. The medium was removed and a fresh medium containing different concentrations of Khat was added. The group without Khat served as a negative control and 4% paraformaldehyde as the positive control. Cell viability was assessed using the MTT assay and effect of Khat on fibroblast and SCC4 phenotypes was evaluated by immunostaining. Analysis of variance was used to assess data (p < 0.05). NOF 316 showed cell death in response to 4% paraformaldehyde, 12.5, 6.25, and 3.12 mg/mL of Khat. The highest concentration of Khat (25 mg/mL) failed to cause cytotoxicity of NOF 316. NOF 319 and NOF 26 displayed cell death at all concentrations of Khat, however, cytotoxicity was not dose dependent. NOF 18 and SCC4 cells showed dose-dependent cell death. NOF 316 showed α-SMA expression after 1 mg/mL of Khat exposure. Not all fibroblasts were α-SMA-positive, suggesting specific activation of a subset of fibroblasts. Khat is cytotoxic to NOF and SCC4 cells. Furthermore, it can also cause activation and phenotypic changes in oral fibroblasts, indicating a potential role in progression of oral squamous cell carcinoma.

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