Synthesis of crosslinked elastin by an endothelial cell culture

Cantor, Jerome O.; Keller, Stephen; Parshley, Mary S.; Darnule, Tukaram V.; Darnule, A. T.; Cerreta, Joseph M.; Turino, Gerard M.; Mandl, Ines

doi:10.1016/s0006-291x(80)80050-7

Cited by 45 publications

(11 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…2). The ability of endothelial cells to produce elastin suggests that they contribute to the formation of the IEL (25, 26, 46), perhaps in response to a signal from medial cells (186). The subendothelial matrix is normally acellular in smaller animals but contains a population of SMCs in humans and in other larger animals (244, 245).…”

Section: Arterial Wall Structurementioning

confidence: 99%

Vascular Extracellular Matrix and Arterial Mechanics

Wagenseil

Mecham²

2009

Physiological Reviews

840

815

View full text Add to dashboard Cite

An important factor in the transition from an open to a closed circulatory system was a change in vessel wall structure and composition that enabled the large arteries to store and release energy during the cardiac cycle. The component of the arterial wall in vertebrates that accounts for these properties is the elastic fiber network organized by medial smooth muscle. Beginning with the onset of pulsatile blood flow in the developing aorta, smooth muscle cells in the vessel wall produce a complex extracellular matrix (ECM) that will ultimately define the mechanical properties that are critical for proper function of the adult vascular system. This review discusses the structural ECM proteins in the vertebrate aortic wall and will explore how the choice of ECM components has changed through evolution as the cardiovascular system became more advanced and pulse pressure increased. By correlating vessel mechanics with physiological blood pressure across animal species and in mice with altered vessel compliance, we show that cardiac and vascular development are physiologically coupled, and we provide evidence for a universal elastic modulus that controls the parameters of ECM deposition in vessel wall development. We also discuss mechanical models that can be used to design better tissue-engineered vessels and to test the efficacy of clinical treatments.

show abstract

Section: Arterial Wall Structurementioning

confidence: 99%

Vascular Extracellular Matrix and Arterial Mechanics

Wagenseil

Mecham²

2009

Physiological Reviews

840

815

View full text Add to dashboard Cite

show abstract

“…Kantor et al. (51) have reported the synthesis of elastin by lung endothelial cells in culture. Elastin was suggested as a product of protein synthesis from cloned rat lung endothelial cells based on the presence of crosslinking amino acids common to elastin in protein secreted by the cells and immunofluorescence following incubation of cell matrix with fluorescent-labeled rat lung elastin antibody preparations.…”

Section: Components Of Elastic Fiber: Isolation and Composition Of Elmentioning

confidence: 99%

Elastin metabolism and chemistry: potential roles in lung development and structure.

Rucker¹,

Dubick²

1984

Environ Health Perspect

View full text Add to dashboard Cite

Elastic fibers are important for elasticity and extensibility of lung tissue. In the developing lung, elastic fibers appear in greatest numbers during the process or period of alveolarization. A variety of mesenchymal cells in lung appear responsible for elastin synthesis. Elastin is a novel protein both from the standpoint of its processing into elastic fibers and chemical properties. For example, elastin undergoes posttranslational modification before its assembly into fibers. These steps include limited proteolysis, hydroxylation of prolyl residues and the oxidative deamination of lysyl residues prior to their incorporation into the crosslinks that covalently bond together polypeptide chains of elastin. The crosslinking amino acids include lysinonorleucine, merodesmosine and desmosine isomers. A key enzyme that controls this process is lysyl oxidase. Lysyl oxidase is a copper metalloprotein whose activity is responsive to and modulated by environmental insults, nutrition deficiencies and the administration of various pharmacological agents. Regarding chemical properties, elastin is one of the most apolar proteins secreted by mammalian cells. Moreover, elastin is one of the most long-lived proteins secreted into the extracellular matrix. In relationship to its processing into elastic fibers and chemical properties, details related to major aspects of elastin metabolism as well as speculation on its potential as a factor in lung development and disease are discussed.

show abstract

“…However, no insoluble elastin was detected in the cell layers nor was the authenticity of tropoelastin established by amino acid analysis or immunological identity. In other studies, Cantor et al (1980) identified desmosine and isodesmosine in an established clone of rat lung endothelial cells. However, since immunofluorescent staining with antibody elicited against rat lung elastin localized to cell bodies with no staining of the extracellular matrix, the presence of extracellular insoluble elastin is unclear.…”

mentioning

confidence: 75%

Elastin production by cultured calf pulmonary artery endothelial cells

Mecham

Madaras

McDonald

et al. 1983

Journal Cellular Physiology

View full text Add to dashboard Cite

Calf pulmonary artery (CPA) endothelial cells synthesize and secrete soluble elastin when incubated in medium conditioned by arterial smooth muscle cells. Endothelial cell tropoelastin cross-reacts with antiserum to bovine ligamentum nuchae elastin and comigrates on SDS-PAGE with tropoelastins from fetal bovine ligamentum nuchae fibroblasts, aortic smooth muscle cells, and ear chondroblasts at an apparent molecular weight of 70,000. Endothelial cells synthesize only one-third as much elastin as these other cell types, however. Approximately 80% of the elastin synthesized by endothelial cells in confluent culture is released into the culture medium. The remaining 20% remains associated with the cell layer and is readily extractable with dilute acetic acid as un-cross-linked, 70,000-dalton tropoelastin. The addition of beta-aminopropionitrile to culture medium did not alter the ratio of tropoelastin in the medium and cell layer, suggesting that cross-linking of tropoelastin does not occur in culture. Immunofluorescent staining of confluent endothelial cell cultures with antielastin serum demonstrated elastin occurring as a web-like network of fine filaments extending throughout the extracellular space. The fibrous elastin was different in organization and distribution from fibers stained with antifibronectin serum, which were localized primarily beneath the cell layer and in regions of cell-cell contact. Extracellular matrix remaining after solubilization of cellular material with Triton X-100 stained positive for fibronectin, but not for elastin.

show abstract

Synthesis of crosslinked elastin by an endothelial cell culture

Cited by 45 publications

References 11 publications

Vascular Extracellular Matrix and Arterial Mechanics

Vascular Extracellular Matrix and Arterial Mechanics

Elastin metabolism and chemistry: potential roles in lung development and structure.

Elastin production by cultured calf pulmonary artery endothelial cells

Contact Info

Product

Resources

About