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Journal articles on the topic 'Human Aortic Smooth Muscle Cell'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Belkin, V. M., A. M. Belkin, and V. E. Koteliansky. "Human smooth muscle VLA-1 integrin: purification, substrate specificity, localization in aorta, and expression during development." Journal of Cell Biology 111, no. 5 (November 1, 1990): 2159–70. http://dx.doi.org/10.1083/jcb.111.5.2159.

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A membrane glycoprotein complex was isolated and purified from human smooth muscle by detergent solubilization and affinity chromatography on collagen-Sepharose. The complex was identified as VLA-1 integrin and consisted of two subunits of 195 and 130 kD in SDS-PAGE. Liposomes containing the VLA-1 integrin adhered to surfaces coated with type I, II, III, and IV collagens, Clq subcomponent of the first component of the complement, and laminin. The liposomes specifically adhered to these proteins in a Ca2+, Mg2(+)-dependent manner, but did not bind to gelatin, fibronectin, and thrombospondin substrates. The expression of VLA-1 integrin in different human tissues and cell types, and during aorta smooth muscle development was studied by SDS-PAGE, and subsequent quantitative immunoblotting was performed with antibodies recognizing alpha 1 and beta 1 subunits of the VLA-1 integrin. A high level of VLA-1 integrin expression was an exceptional feature of smooth muscles. Fibroblasts, endothelial cells, keratinocytes, striated muscles, and platelets contained trace amounts of VLA-1 integrin. In the 10-wk-old human fetal aorta, VLA-1 integrin was found only in smooth muscle cells whereas mesenchymal cells, surrounding aortic smooth muscle cells, were VLA-1 integrin negative. By the 24th wk of gestation, the amount of VLA-1 integrin was significantly reduced in the aortic media (4.3-fold for alpha 1 subunit and 2.5-fold for beta 1 subunit) compared with that in the 10-wk-old aortic smooth muscle cells. After birth, the expression of VLA-1 integrin increased and in the 1.5-yr-old child aorta the VLA-1 integrin level was almost the same as in adult aortic media. Smooth muscle cells from intimal thickening of adult aorta express five times less alpha 1 subunit of VLA integrin that smooth muscle cells from adult aortic media. In primary culture of aortic smooth muscle cells, the content of the VLA-1 integrin was dramatically reduced and subcultured cells did not contain VLA-1 integrin at all.

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2

Glukhova, M. A., S. P. Domogatskii, A. E. Kabakov, V. R. Muzykantov, O. I. Ornatskaya, D. V. Sakharov, and M. G. Frid. "Red blood cell targeting to human aortic smooth muscle cells." Bulletin of Experimental Biology and Medicine 102, no. 5 (November 1986): 1550–52. http://dx.doi.org/10.1007/bf00854687.

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3

Chotani, Maqsood A., Srabani Mitra, Baogen Y. Su, Sheila Flavahan, Ali H. Eid, K. Reed Clark, Christine R. Montague, Hervé Paris, Diane E. Handy, and Nicholas A. Flavahan. "Regulation of α2-adrenoceptors in human vascular smooth muscle cells." American Journal of Physiology-Heart and Circulatory Physiology 286, no. 1 (January 2004): H59—H67. http://dx.doi.org/10.1152/ajpheart.00268.2003.

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This study analyzed the regulation of α2-adrenoceptors (α2-ARs) in human vascular smooth muscle cells (VSMs). Saphenous veins and dermal arterioles or VSMs cultured from them expressed high levels of α2-ARs (α2C > α2A, via RNase protection assay) and responded to α2-AR stimulation [5-bromo- N-(4,5-dihydro-1 H-imidazol-2-yl)-6-quinoxalinamine (UK-14,304, 1 μM)] with constriction or calcium mobilization. In contrast, VSMs cultured from aorta did not express α2-ARs and neither cultured cells nor intact aorta responded to UK-14,304. Although α2-ARs (α2C >> α2A) were detected in aortas, α2C-ARs were localized by immunohistochemistry to VSMs of adventitial arterioles and not aortic media. In contrast with aortas, aortic arterioles constricted in response to α2-AR stimulation. Reporter constructs demonstrated higher activities for α2A- and α2C-AR gene promoters in arteriolar compared with aortic VSMs. In arteriolar VSMs, serum increased expression of α2C-AR mRNA and protein but decreased expression of α2A-ARs. Serum induction of α2C-ARs was reduced by inhibition of p38 mitogen-activated protein kinase (MAPK) with 2 μM SB-202190 or dominant-negative p38 MAPK. UK-14,304 (1 μM) caused calcium mobilization in control and serum-stimulated cells: in control VSMs, the response was inhibited by the α2A-AR antagonist BRL-44408 (100 nM) but not by the α2C-AR antagonist MK-912 (1 nM), whereas after serum stimulation, MK-912 (1 nM) but not BRL-44408 (100 nM) inhibited the response. These results demonstrate site-specific expression of α2-ARs in human VSMs that reflects differential activity of α2-AR gene promoters; namely, high expression and function in venous and arteriolar VSMs but no detectable expression or function in aortic VSMs. We found that α2C-ARs can be dramatically and selectively induced via a p38 MAPK-dependent pathway. Therefore, altered expression of α2C-ARs may contribute to pathological changes in vascular function.

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4

Gown, A. M., A. M. Vogel, D. Gordon, and P. L. Lu. "A smooth muscle-specific monoclonal antibody recognizes smooth muscle actin isozymes." Journal of Cell Biology 100, no. 3 (March 1, 1985): 807–13. http://dx.doi.org/10.1083/jcb.100.3.807.

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Injection of chicken gizzard actin into BALB/c mice resulted in the isolation of a smooth muscle-specific monoclonal antibody designated CGA7. When assayed on methanol-Carnoy's fixed, paraffin-embedded tissue, it bound to smooth muscle cells and myoepithelial cells, but failed to decorate striated muscle, endothelium, connective tissue, epithelium, or nerve. CGA7 recognized microfilament bundles in early passage cultures of rat aortic smooth muscle cells and human leiomyosarcoma cells but did not react with human fibroblasts. In Western blot experiments, CGA7 detected actin from chicken gizzard and monkey ileum, but not skeletal muscle or fibroblast actin. Immunoblots performed on two-dimensional gels demonstrated that CGA7 recognizes gamma-actin from chicken gizzard and alpha- and gamma-actin from rat colon muscularis. This antibody was an excellent tissue-specific smooth muscle marker.

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5

Tang, Yangfeng, Shangyi Yu, Yang Liu, Jiajun Zhang, Lin Han, and Zhiyun Xu. "MicroRNA-124 controls human vascular smooth muscle cell phenotypic switch via Sp1." American Journal of Physiology-Heart and Circulatory Physiology 313, no. 3 (September 1, 2017): H641—H649. http://dx.doi.org/10.1152/ajpheart.00660.2016.

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Phenotypic switch of vascular smooth muscle cells (VSMCs) plays an important role in the pathogenesis of atherosclerosis and aortic dissection. However, the mechanisms of phenotypic modulation are still unclear. MicroRNAs have emerged as important regulators of VSMC function. We recently found that microRNA-124 (miR-124) was downregulated in proliferative vascular diseases that were characterized by a VSMC phenotypic switch. Therefore, we speculated that the aberrant expression of miR-124 might play a critical role in human aortic VSMC phenotypic switch. Using quantitative RT-PCR, we found that miR-124 was dramatically downregulated in the aortic media of clinical specimens of the dissected aorta and correlated with molecular markers of the contractile VSMC phenotype. Overexpression of miR-124 by mimicking transfection significantly attenuated platelet-derived growth factor-BB-induced human aortic VSMC proliferation and phenotypic switch. Furthermore, we identified specificity protein 1 (Sp1) as the downstream target of miR-124. A luciferase reporter assay was used to confirm direct miR-124 targeting of the 3′-untranslated region of the Sp1 gene and repression of Sp1 expression in human aortic VSMCs. Furthermore, constitutively active Sp1 in miR-124-overexpressing VSMCs reversed the antiproliferative effects of miR-124. These results demonstrated a novel mechanism of miR-124 modulation of VSMC phenotypic switch by targeting Sp1 expression. NEW & NOTEWORTHY Previous studies have demonstrated that miR-124 is involved in the proliferation of a variety of cell types. However, miRNAs are expressed in a tissue-specific manner. We first identified miR-124 as a critical regulator in human aortic vascular smooth muscle cell differentiation, proliferation, and phenotype switch by targeting the 3′-untranslated region of specificity protein 1.

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6

Pedroza, Albert J., Yasushi Tashima, Rohan Shad, Paul Cheng, Robert Wirka, Samantha Churovich, Ken Nakamura, et al. "Single-Cell Transcriptomic Profiling of Vascular Smooth Muscle Cell Phenotype Modulation in Marfan Syndrome Aortic Aneurysm." Arteriosclerosis, Thrombosis, and Vascular Biology 40, no. 9 (September 2020): 2195–211. http://dx.doi.org/10.1161/atvbaha.120.314670.

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Objective: To delineate temporal and spatial dynamics of vascular smooth muscle cell (SMC) transcriptomic changes during aortic aneurysm development in Marfan syndrome (MFS). Approach and Results: We performed single-cell RNA sequencing to study aortic root/ascending aneurysm tissue from Fbn1 C1041G/ + (MFS) mice and healthy controls, identifying all aortic cell types. A distinct cluster of transcriptomically modulated SMCs (modSMCs) was identified in adult Fbn1 C1041G/ + mouse aortic aneurysm tissue only. Comparison with atherosclerotic aortic data (ApoE −/− mice) revealed similar patterns of SMC modulation but identified an MFS-specific gene signature, including plasminogen activator inhibitor-1 ( Serpine1 ) and Kruppel-like factor 4 ( Klf4 ). We identified 481 differentially expressed genes between modSMC and SMC subsets; functional annotation highlighted extracellular matrix modulation, collagen synthesis, adhesion, and proliferation. Pseudotime trajectory analysis of Fbn1 C1041G/ + SMC/modSMC transcriptomes identified genes activated differentially throughout the course of phenotype modulation. While modSMCs were not present in young Fbn1 C1041G/ + mouse aortas despite small aortic aneurysm, multiple early modSMCs marker genes were enriched, suggesting activation of phenotype modulation. modSMCs were not found in nondilated adult Fbn1 C1041G/ + descending thoracic aortas. Single-cell RNA sequencing from human MFS aortic root aneurysm tissue confirmed analogous SMC modulation in clinical disease. Enhanced expression of TGF-β (transforming growth factor beta)-responsive genes correlated with SMC modulation in mouse and human data sets. Conclusions: Dynamic SMC phenotype modulation promotes extracellular matrix substrate modulation and aortic aneurysm progression in MFS. We characterize the disease-specific signature of modSMCs and provide temporal, transcriptomic context to the current understanding of the role TGF-β plays in MFS aortopathy. Collectively, single-cell RNA sequencing implicates TGF-β signaling and Klf4 overexpression as potential upstream drivers of SMC modulation.

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7

Ferri, Nicola, Federica Panariti, Chiara Ricci, Giuseppe Maiocchi, and Alberto Corsini. "Aliskiren inhibits prorenin-induced human aortic smooth muscle cell migration." Journal of the Renin-Angiotensin-Aldosterone System 16, no. 2 (July 27, 2014): 284–91. http://dx.doi.org/10.1177/1470320314528364.

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8

Wiskirchen, Jakub, Helmut Dittmann, Rainer Kehlbach, Jens Vogel-Claussen, Regina Gebert, Bernhard M. Dohmen, Wolfgang Schöber, et al. "Rhenium-188 for inhibition of human aortic smooth muscle cell proliferation." International Journal of Radiation Oncology*Biology*Physics 49, no. 3 (March 2001): 809–15. http://dx.doi.org/10.1016/s0360-3016(00)01452-8.

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9

Huang, Hayden, Roger D. Kamm, Peter T. C. So, and Richard T. Lee. "Receptor-Based Differences in Human Aortic Smooth Muscle Cell Membrane Stiffness." Hypertension 38, no. 5 (November 2001): 1158–61. http://dx.doi.org/10.1161/hy1101.096456.

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10

Govatati, Suresh, Prahalathan Pichavaram, Jagadeesh Janjanam, Liang Guo, Renu Virmani, and Gadiparthi N. Rao. "Myristoylation of LMCD1 Leads to Its Species-Specific Derepression of E2F1 and NFATc1 in the Modulation of CDC6 and IL-33 Expression During Development of Vascular Lesions." Arteriosclerosis, Thrombosis, and Vascular Biology 40, no. 5 (May 2020): 1256–74. http://dx.doi.org/10.1161/atvbaha.120.314147.

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Objective: In view of our previous observations on differential expression of LMCD1 (LIM and cysteine-rich domains 1) in human versus rodents, we asked the question whether LMCD1 plays a species-specific role in the development of vascular lesions. Approach and Results: A combination of genetic, molecular, cellular, and disease models were used to test species-specific role of LMCD1 in the pathogenesis of vascular lesions. Here, we report species-specific regulation of LMCD1 expression in mediating vascular smooth muscle cell proliferation and migration during vascular wall remodeling in humans versus mice. Thrombin induced LMCD1 expression in human aortic smooth muscle cells but not mouse aortic smooth muscle cells via activation of Par1 (protease-activated receptor 1)-Gαq/11 (Gα protein q/11)-PLCβ3 (phospholipase Cβ3)-NFATc1 (nuclear factor of activated T cells 1) signaling. Furthermore, although LMCD1 mediates thrombin-induced proliferation and migration of both human aortic smooth muscle cells and mouse aortic smooth muscle cells via influencing E2F1 (E2F transcription factor 1)-mediated CDC6 (cell division cycle 6) expression and NFATc1-mediated IL (interleukin)-33 expression, respectively, in humans, it acts as an activator, and in mice, it acts as a repressor of these transcriptional factors. Interestingly, LMCD1 repressor activity was nullified by N-myristoyltransferase 2–mediated myristoylation in mouse. Besides, we found increased expression of LMCD1 in human stenotic arteries as compared to nonstenotic arteries. On the other hand, LMCD1 expression was decreased in neointimal lesions of mouse injured arteries as compared to noninjured arteries. Conclusions: Together, these observations reveal that LMCD1 acts as an activator and repressor of E2F1 and NFATc1 in humans and mice, respectively, in the induction of CDC6 and IL-33 expression during development of vascular lesions. Based on these findings, LMCD could be a potential target for drug development against restenosis and atherosclerosis in humans.

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11

Ivanov, V., S. Ivanova, A. Niedzwiecki, and M. Rath. "Fat-Soluble Vitamins Affect Composition of Extracellular Matrix Deposited by Human Aortic Smooth Muscle and Endothelial Cells In Vitro." Current Topics in Nutraceutical Research 19, no. 1 (July 6, 2020): 36–45. http://dx.doi.org/10.37290/ctnr2641-452x.19:36-45.

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Atherosclerotic cardiovascular disease is accompanied by changes in arterial connective tissue. We evaluated the effects of fat-soluble vitamins A, D, and E individually and in combinations on the composition of extracellular matrix produced and deposited by arterial wall cells, human aortic smooth muscle cells, and endothelial cells. Individually, vitamins D and E stimulated collagen type I extracellular matrix deposition in human aortic smooth muscle cell cultures. However, vitamins A, D, and E reduced collagen type IV deposition by human aortic smooth muscle cell, counteracting the stimulatory effects of vitamin C. The extracellular matrix deposition of heparan sulfate by human aortic smooth muscle cells increased by vitamin C and its combination (C+D+E). β-carotene + D + C induced the extracellular matrix deposition of collagen I by endothelial cells. Vitamin E with other vitamins resulted in either induction (E+C+A) or inhibition (E+D). The extracellular matrix deposition of type IV collagen and elastin by human aortic endothelial cells was not affected by test vitamins, except the extracellular matrix type IV collagen decrease by combinations (A+E), (A+D+E), and (C+D+E). The extracellular matrix deposition of all tested glycosaminoglycans was reduced by vitamin A and its combination (A+C+D+E). Therefore, the fat-soluble vitamins applied individually or in combination—both with each other or with ascorbic acid—can affect extracellular matrix deposition of type I and IV collagens, and key glycosaminoglycans by cultured human aortic arterial wall cells.

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12

Naseem, Syed M., and Felix P. Heald. "Sex mediated lipid metabolism in human aortic smooth muscle cells." Biochemical and Biophysical Research Communications 144, no. 1 (April 1987): 284–91. http://dx.doi.org/10.1016/s0006-291x(87)80508-9.

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13

Word, R. A., M. L. Casey, K. E. Kamm, and J. T. Stull. "Effects of cGMP on [Ca2+]i, myosin light chain phosphorylation, and contraction in human myometrium." American Journal of Physiology-Cell Physiology 260, no. 4 (April 1, 1991): C861—C867. http://dx.doi.org/10.1152/ajpcell.1991.260.4.c861.

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Adenosine 3',5'-cyclic monophosphate (cAMP) is believed to be an important mediator of myometrial relaxation, and there is evidence to suggest that guanosine 3',5'-cyclic monophosphate (cGMP) is a mediator of smooth muscle relaxation in vascular and probably nonvascular tissues. To investigate the biochemical mechanisms involved in regulation of human myometrial contractility, we studied the effects of analogues of cAMP and cGMP, as well as activators of adenylate and guanylate cyclases, on uterine smooth muscle contractile activity. We found that myometrial smooth muscle cells in culture respond to analogues of cGMP and cAMP, as well as activators of guanylate cyclase, with a significant decrease in the resting and endothelin-induced increase in [Ca2+]i. Treatment of human uterine smooth muscle strips with sodium nitroprusside or isoproterenol results in diminished force and frequency of contraction as well as a decrease in the rate and extent of myosin light chain phosphorylation in spontaneous contractions of human myometrium. cGMP did not effect relaxation of endothelin-stimulated contractions of human myometrium, but the relaxation effects of cGMP were dramatic in precontracted bovine tracheal and human fetal aortic smooth muscles. Whereas cGMP and cAMP act to promote a decrease in the force and frequency of spontaneous contractions in human myometrium, this tissue is not as responsive to the actions of cyclic nucleotides as are other types of smooth muscle.

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14

Iizuka, Kenji, Noriteru Morita, Takeshi Murakami, and Hideaki Kawaguchi. "Nipradilol inhibits atmospheric pressure-induced cell proliferation in human aortic smooth muscle cells." Pharmacological Research 49, no. 3 (March 2004): 217–25. http://dx.doi.org/10.1016/j.phrs.2003.09.011.

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15

Miyamoto, Tetsuya, Yasuyuki Sasaguri, Takakazu Sasaguri, Shiroh Azakami, Hideo Yasukawa, Seiya Kato, Nobuyuki Arima, Kazushige Sugama, and Minoru Morimatsu. "Expression of stem cell factor in human aortic endothelial and smooth muscle cells." Atherosclerosis 129, no. 2 (March 1997): 207–13. http://dx.doi.org/10.1016/s0021-9150(96)06043-1.

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16

Yoshida, Shunsuke, Christoph S. Nabzdyk, Leena Pradhan, and Frank W. LoGerfo. "Thrombospondin-2 Gene Silencing in Human Aortic Smooth Muscle Cells Improves Cell Attachment." Journal of the American College of Surgeons 213, no. 5 (November 2011): 668–76. http://dx.doi.org/10.1016/j.jamcollsurg.2011.07.006.

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17

Assoian, R. K., and M. B. Sporn. "Type beta transforming growth factor in human platelets: release during platelet degranulation and action on vascular smooth muscle cells." Journal of Cell Biology 102, no. 4 (April 1, 1986): 1217–23. http://dx.doi.org/10.1083/jcb.102.4.1217.

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A specific radioimmunoassay for type beta transforming growth factor (TGF-beta) was developed and used to show that human platelets treated with thrombin release TGF-beta as a consequence of degranulation. The thrombin concentrations required to induce release of TGF-beta parallel those concentrations that release the alpha-granule marker, beta-thromboglobulin. Related studies showed that TGF-beta acts on early passage, explant cultures of bovine aortic smooth muscle cells by inhibiting the effect of mitogens on proliferation of subconfluent cell monolayers yet synergizing with mitogens to stimulate growth of the same cells when cultured in soft agar. The results show that primary cultures of bovine aortic smooth muscle cells and established normal rat kidney cells behave similarly with regard to TGF-beta action. Moreover, the data suggest that platelet-mediated proliferation of aortic smooth muscle cells in vivo may not result solely from the stimulatory effect of platelet-derived growth factor (PDGF), but rather from an interaction of platelet factors which has the intrinsic ability to limit as well as stimulate mitosis.

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18

HOLMES, DENNIS R., ANGEL LÓPEZ-CANDALES, SHIXIONG LIAO, and ROBERT W. THOMPSON. "Smooth Muscle Cell Apoptosis and p53 Expression in Human Abdominal Aortic Aneurysms." Annals of the New York Academy of Sciences 800, no. 1 The Abdominal (November 1996): 286–87. http://dx.doi.org/10.1111/j.1749-6632.1996.tb33334.x.

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19

Yin, Chi-Chao, Tin-Kwang Lin, and Kuang-Tse Huang. "Superoxide counteracts low-density lipoprotein-induced human aortic smooth muscle cell proliferation." Journal of Bioscience and Bioengineering 104, no. 3 (September 2007): 157–62. http://dx.doi.org/10.1263/jbb.104.157.

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20

Ray, Julie Basu, Sara Arab, Peter Liu, and Michael Ward. "OXYGEN REGULATION OF HUMAN AORTIC SMOOTH MUSCLE CELL CYCLE ASSOCIATED GENE EXPRESSION." Cardiovascular Pathology 13, no. 3 (May 2004): 139. http://dx.doi.org/10.1016/j.carpath.2004.03.417.

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21

Glukhova, Marina A., Boris V. Shekhonin, Howard Kruth, and Victor E. Koteliansky. "Expression of cytokeratin 8 in human aortic smooth muscle cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 261, no. 4 (October 1, 1991): L72—L77. http://dx.doi.org/10.1152/ajplung.1991.261.4.l72.

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An immunofluorescence method was used to study the expression of cytokeratin 8 in human aortic smooth muscle cells (SMCs) during prenatal development and in atherosclerotic plaques. Aortic SMCs from a 10-wk-old fetus contained cytokeratin 8 in additional to vimentin and a small amount of desmin, whereas, in the cells from a 25-wk-old fetus, cytokeratin 8 was not detected. Cytokeratin 8 was found in the SMCs from intimal thickenings, fatty streaks, and atherosclerotic fibrous plaques. Clusters of cytokeratin 8-positive cells were more abundant in rather advanced lesions (fibrous plaques) that contained at least some amount of lipid. Expression of cytokeratin 8 in the cells of human atherosclerotic lesions probably reflects general rearrangement of gene expression in the intimal cells. cytodifferentiation; fetal phenotype; lipid accumulation

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Glukhova, Marina A., Boris V. Shekhonin, Howard Kruth, and Victor E. Koteliansky. "Expression of cytokeratin 8 in human aortic smooth muscle cells." American Journal of Physiology-Heart and Circulatory Physiology 261, no. 4 (October 1, 1991): 72–77. http://dx.doi.org/10.1152/ajpheart.1991.261.4.72.

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An immunofluorescence method was used to study the expression of cytokeratin 8 in human aortic smooth muscle cells (SMCs) during prenatal development and in atherosclerotic plaques. Aortic SMCs from a 10-wk-old fetus contained cytokeratin 8 in additional to vimentin and a small amount of desmin, whereas, in the cells from a 25-wk-old fetus, cytokeratin 8 was not detected. Cytokeratin 8 was found in the SMCs from intimal thickenings, fatty streaks, and atherosclerotic fibrous plaques. Clusters of cytokeratin 8-positive cells were more abundant in rather advanced lesions (fibrous plaques) that contained at least some amount of lipid. Expression of cytokeratin 8 in the cells of human atherosclerotic lesions probably reflects general rearrangement of gene expression in the intimal cells. cytodifferentiation; fetal phenotype; lipid accumulation

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23

Glukhova, M. A., M. G. Frid, B. V. Shekhonin, T. D. Vasilevskaya, J. Grunwald, M. Saginati, and V. E. Koteliansky. "Expression of extra domain A fibronectin sequence in vascular smooth muscle cells is phenotype dependent." Journal of Cell Biology 109, no. 1 (July 1, 1989): 357–66. http://dx.doi.org/10.1083/jcb.109.1.357.

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Different fibronectin (FN) variants arise from the single gene transcript alternatively spliced in a tissue-specific manner (Hynes, R. O. 1985. Annu. Rev. Cell Biol. 1:67-90; Owens, R. J., A. R. Kornblihtt, and F. E. Baralle. 1986. Oxf. Surv. Eurcaryotic Genes. 3:141-160). We used mAb IST-9, specific for extra domain A (ED-A) FN sequence, and cDNA probe to ED-A exon to determine whether ED-A is present in FN synthesized by vascular smooth muscle cells (SMCs) and, if so, whether expression of ED-A is SMC phenotype dependent. ED-A-containing FN (A-FN) was not revealed in tunica media of human arteries and normal rat aorta by immunofluorescence and immunoblotting techniques. A cDNA probe to ED-A exon did not hybridize with RNA isolated from human aortic media. A positive reaction with IST-9 was observed in (a) diffuse intimal thickening and atherosclerotic plaque from human arteries; (b) experimentally induced intimal thickening in rat aorta; and (c) cultured vascular SMCs. A-FN mRNA was present in the RNA preparation from human aortic intima as judged by hybridization with cDNA probe to ED-A. On the other hand, an mAb interacting with an epitope common for all FN variants revealed FN in both intima and media of human arteries and in the normal rat aorta. A cDNA probe to a sequence shared by all FN variants hybridized with RNA from both intima and media of human aorta, though the level of expression was higher in intima. The data suggest that ED-A exon is omitted during splicing of the FN mRNA precursor in medial SMCs while the expression of A-FN is characteristic of "modulated" SMCs--those of intimal thickenings, of atherosclerotic lesions, and growing in culture.

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André, Dominique E., Urs Arnet, Zhihong Yang, and Thomas F. Lüscher. "Nebivolol Inhibits Human Aortic Smooth Muscle Cell Growth: Effects on Cell Cycle Regulatory Proteins." Journal of Cardiovascular Pharmacology 35, no. 6 (June 2000): 845–48. http://dx.doi.org/10.1097/00005344-200006000-00003.

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25

Sivaraman, Srikanth, Jackson Hedrick, Samia Ismail, Chris Slavin, and Raj R. Rao. "Generation and Characterization of Human Mesenchymal Stem Cell-Derived Smooth Muscle Cells." International Journal of Molecular Sciences 22, no. 19 (September 25, 2021): 10335. http://dx.doi.org/10.3390/ijms221910335.

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Cardiovascular diseases are the leading cause of death worldwide. A completely autologous treatment can be achieved by using elastogenic mesenchymal stem cell (MSC)-derived smooth muscle cells (SMC) at the affected tissue site of vascular diseases such as abdominal aortic aneurysms (AAA). Thus, our work focused on evaluating the efficacy of (a) the combination of various growth factors, (b) different time periods and (c) different MSC lines to determine the treatment combination that generated SMCs that exhibited the greatest elastogenicity among the tested groups using Western blotting and flow cytometry. Additionally, total RNA sequencing was used to confirm that post-differentiation cells were upregulating SMC-specific gene markers. Results indicated that MSCs cultured for four days in PDGF + TGFβ1 (PT)-infused differentiation medium showed significant increases in SMC markers and decreases in MSC markers compared to MSCs cultured without differentiation factors. RNA Seq analysis confirmed the presence of vascular smooth muscle formation in MSCs differentiated in PT medium over a seven-day period. Overall, our results indicated that origin, growth factor treatment and culture period played a major role in influencing MSC differentiation to SMCs.

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Birukov, K. G., O. V. Stepanova, A. K. Nanaev, and V. P. Shirinsky. "Expression of calponin in rabbit and human aortic smooth muscle cells." Cell and Tissue Research 266, no. 3 (December 1991): 579–84. http://dx.doi.org/10.1007/bf00318599.

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27

Gurung, Rijan, Andrew Mark Choong, Chin Cheng Woo, Roger Foo, and Vitaly Sorokin. "Genetic and Epigenetic Mechanisms Underlying Vascular Smooth Muscle Cell Phenotypic Modulation in Abdominal Aortic Aneurysm." International Journal of Molecular Sciences 21, no. 17 (August 31, 2020): 6334. http://dx.doi.org/10.3390/ijms21176334.

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Abdominal aortic aneurysm (AAA) refers to the localized dilatation of the infra-renal aorta, in which the diameter exceeds 3.0 cm. Loss of vascular smooth muscle cells, degradation of the extracellular matrix (ECM), vascular inflammation, and oxidative stress are hallmarks of AAA pathogenesis and contribute to the progressive thinning of the media and adventitia of the aortic wall. With increasing AAA diameter, and left untreated, aortic rupture ensues with high mortality. Collective evidence of recent genetic and epigenetic studies has shown that phenotypic modulation of smooth muscle cells (SMCs) towards dedifferentiation and proliferative state, which associate with the ECM remodeling of the vascular wall and accompanied with increased cell senescence and inflammation, is seen in in vitro and in vivo models of the disease. This review critically analyses existing publications on the genetic and epigenetic mechanisms implicated in the complex role of SMCs within the aortic wall in AAA formation and reflects the importance of SMCs plasticity in AAA formation. Although evidence from the wide variety of mouse models is convincing, how this knowledge is applied to human biology needs to be addressed urgently leveraging modern in vitro and in vivo experimental technology.

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Belkin, A. M., O. I. Ornatsky, M. A. Glukhova, and V. E. Koteliansky. "Immunolocalization of meta-vinculin in human smooth and cardiac muscles." Journal of Cell Biology 107, no. 2 (August 1, 1988): 545–53. http://dx.doi.org/10.1083/jcb.107.2.545.

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Meta-vinculin, a vinculin-related protein, has been isolated from human uterus smooth muscle. Specific antibodies to meta-vinculin, which distinguish between meta-vinculin and vinculin, were prepared by absorption of anti-meta-vinculin serum on vinculin coupled to nitrocellulose. Meta-vinculin specific antibody demonstrates only smooth and cardiac muscle specificity and is able to cross-react with a small 21-kD fragment of the meta-vinculin polypeptide chain. This antibody does not interact with protease resistant 95-kD core shared by vinculin and meta-vinculin. Meta-vinculin specific antibody was used for the localization of meta-vinculin in smooth and cardiac muscles by the indirect immunofluorescence method. At the light microscopy resolution level it was found that meta-vinculin and vinculin are localized in the same cellular adhesive structures. Meta-vinculin is present in membrane-associated microfilament-bound plaques of smooth muscle, in intercalated discs and costameres of cardiac muscle. In primary culture of smooth muscle cells from human aorta, meta-vinculin and vinculin were found to be present in focal contacts of the cells. During the cultivation of smooth muscle cells, the quantity of meta-vinculin decreased progressively and finally meta-vinculin completely disappeared from the focal contacts. The data show that in smooth and cardiac muscles meta-vinculin could be a structural component of microfilament-membrane attachment sites, defined earlier by the localization of vinculin.

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29

Kirschenlohr, H. L., J. C. Metcalfe, P. L. Weissberg, and D. J. Grainger. "Adult human aortic smooth muscle cells in culture produce active TGF-beta." American Journal of Physiology-Cell Physiology 265, no. 2 (August 1, 1993): C571—C576. http://dx.doi.org/10.1152/ajpcell.1993.265.2.c571.

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Vascular smooth muscle cells (VSMC) from adult human aortas proliferated in culture in response to fetal calf serum (FCS) with a population doubling time of 70-85 h compared with 35 +/- 5 h for VSMC derived from adult rat aortas. Medium conditioned on cultures prepared from aortas from three different donors and mixed 1:1 with fresh Dulbecco's modified Eagle's medium plus 20% FCS [human conditioned medium (HCM)] reduced the rate of proliferation of rat VSMC by 46 +/- 6% (n = 3) after 48 h compared with cells in fresh medium. HCM did not reduce the proportion (> 65%) of rat VSMC that entered DNA synthesis but delayed entry into mitosis by at least 18 h. This effect was similar to previous observations of the action of transforming growth factor-beta (TGF-beta) on rat VSMC (G. K. Owens, A. A. Geisterfer, Y. W. Yang, and A. Komoriya. J. Cell Biol. 107: 771-780, 1988). A TGF-beta assay using DNA synthesis in mink lung epithelial cells confirmed that human, but not rat, VSMC in culture secrete active TGF-beta. Addition of a neutralizing antibody to TGF-beta to human VSMC in the presence of 20% FCS decreased the population doubling time from 74 +/- 3 to 46 +/- 6 h (n = 3). These observations demonstrate that the long population doubling time of human VSMC is due to the production of active TGF-beta and to an inhibitory autocrine loop.

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30

Lee, Tae-Hee, Sun-Hwa Song, Koung Li Kim, Ji-Yeun Yi, Ga-Hee Shin, Ji Yeon Kim, Jihoon Kim, et al. "Functional Recapitulation of Smooth Muscle Cells Via Induced Pluripotent Stem Cells From Human Aortic Smooth Muscle Cells." Circulation Research 106, no. 1 (January 8, 2010): 120–28. http://dx.doi.org/10.1161/circresaha.109.207902.

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31

Carpenter, Keri L. H., Simon J. Hardwick, Valentina Albarani, and Malcolm J. Mitchinson. "Carotenoids inhibit DNA synthesis in human aortic smooth muscle cells." FEBS Letters 447, no. 1 (March 19, 1999): 17–20. http://dx.doi.org/10.1016/s0014-5793(99)00252-5.

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32

Grange, Janet J., Lisa M. Baca-Regen, Alisa J. Nollendorfs, Yuri Persidsky, Debra L. Sudan, and B. Timothy Baxter. "Protein kinase C isoforms in human aortic smooth muscle cells." Journal of Vascular Surgery 27, no. 5 (May 1998): 919–27. http://dx.doi.org/10.1016/s0741-5214(98)70273-3.

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33

Cox, R. H., Z. Zhou, and T. N. Tulenko. "Voltage-Gated Sodium Channels in Human Aortic Smooth Muscle Cells." Journal of Vascular Research 35, no. 5 (1998): 310–17. http://dx.doi.org/10.1159/000025600.

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34

Peiró, Concepción, Susana Vallejo, Elena Cercas, José Luis Llergo, Nuria Lafuente, Nuria Matesanz, Leocadio Rodríguez-Mañas, and Carlos F. Sánchez-Ferrer. "Thapsigargin Induces Apoptosis in Cultured Human Aortic Smooth Muscle Cells." Journal of Cardiovascular Pharmacology 36, no. 5 (November 2000): 676–80. http://dx.doi.org/10.1097/00005344-200011000-00018.

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35

Seeger, H., A. O. Mueck, C. Bartsch, and T. H. Lippert. "Effect of Melatonin on Depolarized Human Aortic Smooth Muscle Cells." Menopause 2, no. 4 (1995): 261. http://dx.doi.org/10.1097/00042192-199502040-00073.

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36

Ares, Mikko P. S., M. Isabella Pörn, Johan Thyberg, Ulf Diczfalusy, Bengt Kallin, Ingemar Björkhem, Sten Orrenius, and Jan Nilsson. "25-HYDROXYCHOLESTEROL INDUCES APOPTOSIS IN HUMAN AORTIC SMOOTH MUSCLE CELLS." Biochemical Society Transactions 24, no. 4 (November 1, 1996): 616S. http://dx.doi.org/10.1042/bst024616sb.

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37

Oikawa, Koji, Kenji Iizuka, Takeshi Murakami, Tatsuya Nagai, Koichi Okita, Kazuya Yonezawa, Akira Kitabatake, and Hideaki Kawaguchi. "Pure pressure stress increased monocarboxylate transporter in human aortic smooth muscle cell membrane." Molecular and Cellular Biochemistry 259, no. 1/2 (April 2004): 151–56. http://dx.doi.org/10.1023/b:mcbi.0000021366.62189.9d.

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38

Vigetti, Davide, Manuela Viola, Eugenia Karousou, Manuela Rizzi, Paola Moretto, Anna Genasetti, Moira Clerici, Vincent C. Hascall, Giancarlo De Luca, and Alberto Passi. "Hyaluronan-CD44-ERK1/2 Regulate Human Aortic Smooth Muscle Cell Motility during Aging." Journal of Biological Chemistry 283, no. 7 (December 12, 2007): 4448–58. http://dx.doi.org/10.1074/jbc.m709051200.

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39

Alfieri, V., F. Saporiti, F. Ferrari, L. Piacentini, M. Chiesa, and G. I. Colombo. "MC1R regulates P38 MAPK pathway to reduce human aortic smooth muscle cell migration." Atherosclerosis 275 (August 2018): e127-e128. http://dx.doi.org/10.1016/j.atherosclerosis.2018.06.368.

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40

Muteliefu, Gulinuer, Hidehisa Shimizu, Atsushi Enomoto, Fuyuhiko Nishijima, Masahide Takahashi, and Toshimitsu Niwa. "Indoxyl sulfate promotes vascular smooth muscle cell senescence with upregulation of p53, p21, and prelamin A through oxidative stress." American Journal of Physiology-Cell Physiology 303, no. 2 (July 15, 2012): C126—C134. http://dx.doi.org/10.1152/ajpcell.00329.2011.

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We previously demonstrated that indoxyl sulfate (IS), a uremic toxin, induces aortic calcification in hypertensive rats and induces oxidative stress and the expression of osteoblast-specific proteins in vascular smooth muscle cells. This study aimed to clarify whether IS stimulates senescence of cultured human aortic smooth muscle cells (HASMCs) and aorta in Dahl salt-sensitive hypertensive rats and whether AST-120, an oral sorbent, prevents senescence of aorta in subtotally nephrectomized uremic rats. IS increased the mRNA expression of p53 and p21 in HASMCs, whereas it did not change that of p16 and retinoblastoma protein (pRb). The IS-induced expression of p53 and p21 was suppressed by N-acetylcysteine, an antioxidant. IS promoted protein expression of p53, p21, and senescence-associated β-galactosidase (SA-β-gal) activity in HASMCs, and N-acetylcysteine and pifithrin-α, p-nitro, a p53 inhibitor, blocked these effects. IS upregulated prelamin A, a hallmark of vascular smooth muscle cell senescence, and downregulated FACE1/Zempste24 protein expression in HASMCs, and N-acetylcysteine suppressed these effects. Administration of IS to hypertensive rats increased expression of SA-β-gal, p53, p21, prelamin A, and oxidative stress markers such as 8-hydroxyl-2′-deoxyguanosine (8-OHdG) and malondialdehyde (MDA) in the cells embedded in the calcification area of arcuate aorta. Further, the uremic rat model showed positive staining for SA-β-gal, p53, p21, prelamin A, 8-OHdG, and MDA in the cells embedded in the calcification area of arcuate aorta, whereas AST-120 reduced the expression of these biomarkers. Taken together, IS accelerates vascular smooth muscle cell senescence with upregulation of p53, p21, and prelamin A and downregulation of FACE1 through oxidative stress.

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41

Bayston, T., S. Ramessur, J. Reise, K. G. Jones, and J. T. Powell. "Prostaglandin e2 receptors in abdominal aortic aneurysm and human aortic smooth muscle cells." Journal of Vascular Surgery 38, no. 2 (August 2003): 354–59. http://dx.doi.org/10.1016/s0741-5214(03)00339-2.

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42

Glukhova, Marina A., Maria G. Frid, and Victor E. Koteliansky. "Phenotypic changes of human aortic smooth muscle cells during development and in the adult vessel." American Journal of Physiology-Heart and Circulatory Physiology 261, no. 4 (October 1, 1991): 78–80. http://dx.doi.org/10.1152/ajpheart.1991.261.4.78.

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To characterize phenotypic expression of human aortic smooth muscle cells (SMCs), we have studied the content of cytodifferentiation-related cytoskeletal proteins, and of fibronectin (FN) variants in the samples of media from the fetal, child, and adult aorta and in the subendothelial intima of the normal and atherosclerotic aorta. Mature SMCs from the adult aortic media contained high amounts of -SM-actin, SM-myosin heavy chains, meta-vinculin, and 150 kDa caldesmon. Cytokeratin 8 and extra domain-containing variants of FN (A-FN and B-FN) were not found in these cells. The SMCs from the aortic media of 10-wk-old fetus contained low amounts of the SM markers, expressed cytokeratin 8, A-FN, and B-FN. In 25-wk-old fetus, as well as in 2- and 6-mo-old child, aortic medial SMCs expressed an intermediate phenotype, and only in 18-mo-old child were the cells found to be similar to those from adult media. SMCs from the normal adult subendothelial intima contained reduced amounts of meta-vinculin and of 150 kDa caldesmon, and they expressed A-FN. In addition, the SMCs from atherosclerotic fibrous plaque contained a decreased proportion of -SM-actin and of SM-myosin heavy chains, whereas cytokeratin 8 was found. Therefore we conclude that the SMCs from intimal thickenings appear to express a less mature phenotype than that of the medial cells from adult aorta. Rather, these SMCs contain reduced amounts of the SM markers and express proteins typical of the fetal SMC phenotype, A-FN and cytokeratin 8. cytodifferentiation; cytoskeletal proteins; fibronectin variant forms

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43

Wong, Gail A., Vincent Tang, Faten El-Sabeawy, and Robert H. Weiss. "BMP-2 inhibits proliferation of human aortic smooth muscle cells via p21Cip1/Waf1." American Journal of Physiology-Endocrinology and Metabolism 284, no. 5 (May 1, 2003): E972—E979. http://dx.doi.org/10.1152/ajpendo.00385.2002.

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Bone-morphogenetic proteins (BMP)-2 and -7, multifunctional members of the transforming growth factor (TGF)-β superfamily with powerful osteoinductive effects, cause cell cycle arrest in a variety of transformed cell lines by activating signaling cascades that involve several cyclin-dependent kinase inhibitors (CDKIs). CDKIs in the cip/kip family, p21Cip1/Waf1and p27Kip1, have been shown to negatively regulate the G1 cyclins and their partner cyclin-dependent kinase proteins, resulting in BMP-mediated growth arrest. Bone morphogens have also been associated with antiproliferative effects in vascular tissue by unknown mechanisms. We now show that BMP-2-mediated inhibition of platelet-derived growth factor (PDGF)-stimulated human aortic smooth muscle cell (HASMC) proliferation is accompanied by increased levels of p21 protein. Antisense oligodeoxynucleotides specific for p21 attenuate BMP-2-induced inhibition of proliferation when transfected into HASMCs, demonstrating that BMP-2 inhibits PDGF-stimulated proliferation of HASMCs through induction of p21. Whether p21-mediated induction of cell cycle arrest by BMP-2 sets the stage for osteogenic differentiation of vascular smooth muscle cells, ultimately leading to vascular mineralization, remains to be investigated.

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44

Hatzi, Elissavet, Yann Bassaglia, and Josette Badet. "Internalization and Processing of Human Angiogenin by Cultured Aortic Smooth Muscle Cells." Biochemical and Biophysical Research Communications 267, no. 3 (January 2000): 719–25. http://dx.doi.org/10.1006/bbrc.1999.2015.

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45

BONO, Françoise, Patrice RIGON, Isabelle LAMARCHE, Pierre SAVI, Véronique SALEL, and Jean-Marc HERBERT. "Heparin inhibits the binding of basic fibroblast growth factor to cultured human aortic smooth-muscle cells." Biochemical Journal 326, no. 3 (September 15, 1997): 661–68. http://dx.doi.org/10.1042/bj3260661.

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Basic fibroblast growth factor (bFGF) and its specific receptors have diverse roles on a variety of cell types, such as the induction of vascular smooth-muscle cell proliferation which contributes to restenosis after coronary balloon angioplasty. bFGF is also known to interact with heparan sulphate proteoglycans present on the cell surface or in the extracellular matrix. In this study, the binding of 125I-bFGF to human aortic smooth-muscle cells was investigated. 125I-bFGF binding to these cells was reversible and saturable. Scatchard analysis revealed the presence of two distinct binding sites: a high-affinity receptor (Kd = 38±7 pM; 1480±220 sites/cell) and a low-affinity non-saturable binding site (Kd= 8.0±2.0 nM). Pretreatment of the cells with heparinase resulted in a large reduction of 125I-bFGF binding to its low-affinity receptors, suggesting that they are heparin-like molecules. The specificity of the low- and high-affinity binding sites for bFGF was determined with acidic FGF, platelet-derived growth factor-BB and epidermal growth factor, which did not compete for 125I-bFGF binding. Expression of FGF receptor isoforms analysed by reverse transcriptase-PCR revealed the presence of only the type-1 receptor. Binding to low-affinity binding sites was antagonized by heparin, suramin, protamine sulphate and platelet factor 4. Unexpectedly, these molecules also reduced the binding of 125I-bFGF to its high-affinity sites. Consistent with these results, heparin, suramin, protamine sulphate and platelet factor 4 inhibited bFGF-induced proliferation of human aortic smooth-muscle cells. Heparin abrogated bFGF-induced release of tissue-type plasminogen activator by these cells. These observations suggest that the interaction of bFGF with human aortic smooth-muscle cells is different from that described for other cells such as endothelial cells, in which heparin acts as a potentiating factor of the mitogenic activity of bFGF.

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46

Sumi, Yukio, Hisako Muramatsu, Yoshifumi Takei, Ken-Ichiro Hata, Minoru Ueda, and Takashi Muramatsu. "Midkine, a heparin-binding growth factor, promotes growth and glycosaminoglycan synthesis of endothelial cells through its action on smooth muscle cells in an artificial blood vessel model." Journal of Cell Science 115, no. 13 (July 1, 2002): 2659–67. http://dx.doi.org/10.1242/jcs.115.13.2659.

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To study the interactions between smooth muscle cells and endothelial cells in vitro, we developed an artificial blood vessel model, which consisted of collagen gel containing human aortic smooth muscle cells and human umbilical vein endothelial cells grown on the gel. The blood vessel model was utilized to investigate the role of midkine, a heparin-binding growth factor, in the intercellular interactions that are important in angiogenesis. In the blood vessel model, midkine induced stratification of the endothelial cells and increased their proliferation and glycosaminoglycan synthesis. However,midkine had no effect on the smooth muscle cells or endothelial cells when they were cultured separately. Increased proliferation of the endothelial cells was also attained by coculturing them with smooth muscle cells in the presence of midkine or culturing endothelial cells with the conditioned medium of the smooth muscle cells, which had been treated with midkine. These experiments indicate that the target of midkine was smooth muscle cells, which secreted factor(s) acting on the endothelial cells. We identified interleukin-8 as one such factor; the synthesis of interleukin-8 by the smooth muscle cells was increased by exposure to midkine, and anti-interleukin-8 inhibited the midkine action. Furthermore, interleukin-8 caused stratification of the endothelial cells in the blood vessel model. These results provided evidence that midkine is one of the factors involved in epithelial-mesenchymal interactions.

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47

Glukhova, Marina A., Maria G. Frid, and Victor E. Koteliansky. "Phenotypic changes of human aortic smooth muscle cells during development and in the adult vessel." American Journal of Physiology-Lung Cellular and Molecular Physiology 261, no. 4 (October 1, 1991): L78—L80. http://dx.doi.org/10.1152/ajplung.1991.261.4.l78.

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To characterize phenotypic expression of human aortic smooth muscle cells (SMCs), we have studied the content of cytodifferentiation-related cytoskeletal proteins, and of fibronectin (FN) variants in the samples of media from the fetal, child, and adult aorta and in the subendothelial intima of the normal and atherosclerotic aorta. Mature SMCs from the adult aortic media contained high amounts of agr-SM-actin, SM-myosin heavy chains, meta-vinculin, and 150 kDa caldesmon. Cytokeratin 8 and extra domain-containing variants of FN (A-FN and B-FN) were not found in these cells. The SMCs from the aortic media of 10-wk-old fetus contained low amounts of the SM markers, expressed cytokeratin 8, A-FN, and B-FN. In 25-wk-old fetus, as well as in 2- and 6-mo-old child, aortic medial SMCs expressed an intermediate phenotype, and only in 18-mo-old child were the cells found to be similar to those from adult media. SMCs from the normal adult subendothelial intima contained reduced amounts of meta-vinculin and of 150 kDa caldesmon, and they expressed A-FN. In addition, the SMCs from atherosclerotic fibrous plaque contained a decreased proportion of agr-SM-actin and of SM-myosin heavy chains, whereas cytokeratin 8 was found. Therefore we conclude that the SMCs from intimal thickenings appear to express a less mature phenotype than that of the medial cells from adult aorta. Rather, these SMCs contain reduced amounts of the SM markers and express proteins typical of the fetal SMC phenotype, A-FN and cytokeratin 8. cytodifferentiation; cytoskeletal proteins; fibronectin variant forms

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48

Robinson, William P., Christelle D. Douillet, Peter M. Milano, Richard C. Boucher, Cam Patterson, and Preston B. Rich. "ATP stimulates MMP-2 release from human aortic smooth muscle cells via JNK signaling pathway." American Journal of Physiology-Heart and Circulatory Physiology 290, no. 5 (May 2006): H1988—H1996. http://dx.doi.org/10.1152/ajpheart.00344.2005.

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Aortic smooth muscle cell release of matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of metalloproteinase-2 (TIMP-2) has been implicated in aortic aneurysm pathogenesis, but proximal modulation of release is poorly understood. Extracellular nucleotides regulate vascular smooth muscle cell metabolism in response to physiochemical stresses, but nucleotide modulation of MMP and/or TIMP release has not been reported. We hypothesized that nucleotides modulate MMP-2 and TIMP-2 release from human aortic smooth muscle cells (HASMCs) via distinct purinergic receptors and signaling pathways. We exposed HASMCs to exogenous ATP and other nucleotides with and without interleukin-1β (IL-1β). HASMCs were pretreated in some experiments with apyrase, which degrades ATP, and inhibitors of ERK1/2, JNK, and p38 MAPK. MMP-2 and TIMP-2 released into supernatant were assessed using ELISA and Western blotting. ATP, adenosine, and UTP significantly stimulated MMP-2 release in the presence of IL-1β (300 nM ATP: 181 ± 22%, P = 0.003; 30 μm adenosine: 244 ± 150%, P = 0.001; and 200 μm UTP: 153 ± 40%, P = 0.015; vs. 100% constitutive). ATP also stimulated MMP-2 release in the absence of IL-1β (100 μm ATP: 148 ± 38% vs. 100% constitutive). Apyrase significantly reduced ATP-stimulated MMP-2 release (apyrase + 500 nM ATP: 59 ± 3% vs. 124 ± 7% with 500 nM ATP). Rank-order agonist potency for MMP-2 release was consistent with ATP activation of PAY and PAY receptors. ATP induced phosphorylation of intracellular JNK, and inhibition of the JNK pathway blocked ATP-stimulated MMP-2 release, indicating signaling via this pathway. Nucleotides are thus novel stimulants of MMP-2 release from HASMCs and may provide a mechanistic link between physiochemical stress in the aorta and aneurysms, especially in the context of inflammation.

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49

Degraeve, Frédéric, Manlio Bolla, Stéphanie Blaie, Christophe Créminon, Isabelle Quéré, Patrice Boquet, Sylviane Lévy-Toledano, Jacques Bertoglio, and Aı̈da Habib. "Modulation of COX-2 Expression by Statins in Human Aortic Smooth Muscle Cells." Journal of Biological Chemistry 276, no. 50 (October 8, 2001): 46849–55. http://dx.doi.org/10.1074/jbc.m104197200.

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Cyclooxygenase (COX)-2 and COX-1 play an important role in prostacyclin production in vessels and participate in maintaining vascular homeostasis. Statins are inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) reductase, which is crucial in cholesterol biosynthesis. Recently, cholesterol-independent effects of statins have been described. In this study, we evaluated the effect of two inhibitors of HMG CoA reductase, mevastatin and lovastatin, on the production of prostacyclin and the expression of COX in human aortic smooth muscle cells. Treatment of cells with 25 μmmevastatin or lovastatin resulted in the induction of COX-2 and increase in prostacyclin production. Mevalonate, the direct metabolite of HMG CoA reductase, and geranylgeranyl-pyrophosphate reversed this effect. GGTI-286, a selective inhibitor of geranylgeranyltransferases, increased COX-2 expression and prostacyclin formation, thus indicating the involvement of geranylgeranylated proteins in the down-regulation of COX-2. Furthermore,Clostridium difficiletoxin B, an inhibitor of the Rho GTP-binding protein family, the Rho selective inhibitor C3 transferase, and Y-27632, a selective inhibitor of the Rho-associated kinases, targets of Rho A, increased COX-2 expression whereas the activator of the Rho GTPase, the cytotoxic necrotizing factor 1, blocked interlukin-1α-dependent COX-2 induction. These results demonstrate that statins up-regulate COX-2 expression and subsequent prostacyclin formation in human aortic smooth muscle cells in part through inhibition of Rho.

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50

Miwa, T., Y. Manabe, K. Kurokawa, S. Kamada, N. Kanda, G. Bruns, H. Ueyama, and T. Kakunaga. "Structure, chromosome location, and expression of the human smooth muscle (enteric type) gamma-actin gene: evolution of six human actin genes." Molecular and Cellular Biology 11, no. 6 (June 1991): 3296–306. http://dx.doi.org/10.1128/mcb.11.6.3296-3306.1991.

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Recombinant phages that carry the human smooth muscle (enteric type) gamma-actin gene were isolated from human genomic DNA libraries. The amino acid sequence deduced from the nucleotide sequence matches those of cDNAs but differs from the protein sequence previously reported at one amino acid position, codon 359. The gene containing one 5' untranslated exon and eight coding exons extends for 27 kb on human chromosome 2. The intron between codons 84 and 85 (site 3) is unique to the two smooth muscle actin genes. In the 5' flanking region, there are several CArG boxes and E boxes, which are regulatory elements in some muscle-specific genes. Hybridization with the 3' untranslated region, which is specific for the human smooth muscle gamma-actin gene, suggests the single gene in the human genome and specific expressions in enteric and aortic tissues. From characterized molecular structures of the six human actin isoform genes, we propose a hypothesis of evolutionary pathway of the actin gene family. A presumed ancestral actin gene had introns at least sites 1, 2, and 4 through 8. Cytoplasmic actin genes may have directly evolved from it through loss of introns at sites 5 and 6. However, through duplication of the ancestral actin gene with substitutions of many amino acids, a prototype of muscle actin genes had been created. Subsequently, striated muscle actin and smooth muscle actin genes may have evolved from this prototype by loss of an intron at site 4 and acquisition of a new intron at site 3, respectively.

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