Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0729233 (Thoracic)
 6,478 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human arterial endothelial cells were cultured in vitro for up to 40 cumulative population doublings. Culture conditions similar to those required for long-term propagation of human umbilical vein endothelial cells were employed. These included fibronectin-coated culture vessels, 5 to 20% fetal bovine serum, endothelial cell growth factor, and heparin. Thoracic aorta endothelial cells were larger than iliac artery endothelial cells. Both cell types stained positively for Factor VIII antigen by immunofluorescence. A decrease in confluent density as a function of population doubling level was correlated with the appearance of large, senescent cells in the cultures. Serum growth factors to which the arterial endothelial cells responded included insulin, transferrin, epidermal growth factor, thrombin, and somatomedins. The effect of thrombin did not require the availability of the active site of the protease. The effect of the somatomedins was only seen in the presence of heparin. Neither platelet-derived growth factor nor hydrocortisone induced arterial endothelial cell proliferation. These growth factor responses were also observed on the part of human umbilical vein endothelial cells.
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PMID:Growth factor responses of human arterial endothelial cells in vitro. 375 96

Cellular interactions control lymphocyte localization within salivary gland tissues and contribute to the immune defense of oral surfaces. We examined lymphocyte adherence to cultured parotid cells using an in vitro assay and found good correlation with previously reported binding to parotid gland frozen sections. Thoracic duct lymphocytes (TDL) bound to parotid cells in greater numbers than thymocytes (74 vs 11 cells/mm2). B cells showed preferential adherence compared to T cells (75% vs 28%). TDL binding was inhibited by sodium azide or cytochalasin B (60% and 80%, respectively). EDTA inhibition (63%) was restored by replacing calcium (9%) but not magnesium (65%). Binding was inhibited by fucoidin or phosphomannan (approximately 70%). Fibronectin peptides had no effect. Culture supernatants were inhibitory for TDL adherence (60%), suggesting that molecules involved in lymphocyte localization may be shed and that parotid cell cultures will be useful for ligand isolation and characterization.
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PMID:Lymphocyte adhesive interactions with cultured parotid salivary gland epithelial cells from rats. 902 60

Aortic distensability is the key to normal aortic function and relates to the lamellar unit in the media. However, the organization of the extracellular matrix components in these lamellar units, which are largely responsible for the distensability, is insufficiently known, especially in the human. We therefore performed a detailed ultrastructural analysis of these components. Thoracic aortas of 56 individuals (age 45-74 years), none of whom suffered from aortic disease, were studied by immunoelectron microscopy of elastin, collagen types I, III, IV, V, and VI, fibronectin, and fibrillin-1, and by ultrastructural histochemistry of proteoglycans, which were further characterized by enzymatic digestion. The elastic lamellae were closely associated with thick collagen fibers containing types I, III, and V collagen. Between these collagen fibers, numerous complex, circumferentially oriented streaks of elastin protruded from the lamellae. In contrast to what is usually reported in the aortas of experimental animals, the smooth muscle cells preferentially adhered to these ill-defined streaks rather than directly to the solid lamellae. Fibrillin-1- and type VI collagen-containing bundles of microfibrils (oxytalan fibers) were also involved in the smooth muscle cell-elastin contact. The smooth muscle cells were invested by basal lamina-like layers connecting them to each other as well as to the oxytalan fibers. Unexpectedly, these layers were abundantly labeled by anti-fibronectin, whereas type IV collagen, a specific basement membrane component, was mainly found in larger, flocculent deposits. The proteoglycans present were collagen-associated dermatan sulfate proteoglycan, cell-associated heparan sulfate proteoglycan, and interstitial chondroitin sulfate proteoglycan. Our observations demonstrate that the extracellular matrix in the human aorta is extremely complex and therefore differs from most descriptions based on experimental animals. They serve as reference for future studies on aortic diseases, such as aneurysmas and dissections.
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PMID:Extracellular matrix of the human aortic media: an ultrastructural histochemical and immunohistochemical study of the adult aortic media. 1060 43