The identification of glycoproteins associated with elastic-tissue microfibrils

Sear, Christopher H. J.; Kewley, Michael A.; Jones, Carolyn J.P.; Grant, Michael E.; Jackson, David S.

doi:10.1042/bj1700715

Cited by 76 publications

(31 citation statements)

References 11 publications

(11 reference statements)

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“…The preparation and characterization of the rabbit anti-(bovine microfibrillar protein) serum has been described elsewhere (Kewley et al, 1977;Sear et al, 1978). The rabbit anti-(human cold-insoluble globulin) serum, and a similar antiserum preadsorbed with human serum, were generously provided by Dr. A. Vaheri, University of Helsinki, Helsinki, Finland.…”

Section: Experimental Materialsmentioning

confidence: 99%

The nature of the microfibrillar glycoproteins of elastic fibres. A biosynthetic study

Sear¹,

Grant²,

Jackson³

1981

Biochemical Journal

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Section: Experimental Materialsmentioning

confidence: 99%

The nature of the microfibrillar glycoproteins of elastic fibres. A biosynthetic study

Sear¹,

Grant²,

Jackson³

1981

Biochemical Journal

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“…At the ultrastructural level elastic matrices consist of large tracts of amorphous material containing peripherally associated microfibrils 10-12 nm in diameter (Ross and Bornstein, 1969;Sear et al, 1978;. In most vertebrates elastin is the basic component of the amorphous material in elastic matrices (Sage and Gray, 1979).…”

Section: Introductionmentioning

confidence: 99%

Elastic extracellular matrix of the embryonic chick heart: An immunohistological study using laser confocal microscopy

Hurlé

Kitten

Sakai

et al. 1994

Developmental Dynamics

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The "elastic matrix" constitutes a specialized component of the extracellular matrix which confers resiliency to tissues and organs subjected to repeated deformations. The role of the elastic matrix in living organisms appears to be of key importance since diseases characterized by expression of defective inherited genes which encode components of the elastic matrix lead to premature death. While the elastic matrix of adult organs has received a great deal of attention, little is known about when it first appears in embryonic tissues or its possible role in developing organs. In the present study we have performed an immunohistochemical study of the distribution of elastin and three additional components often associated with elastic matrices in adult tissues (i.e., fibrillin, emilin, and type VI collagen) during the development of the chicken embryonic heart. The threedimensional arrangement of these components was established through the observation of wholemount specimens with scanning laser confocal microscopy. Our results revealed three different periods of heart development regarding the composition of the elastic matrix. Prior to stage 21 the embryonic heart lacks elastin but exhibits a matrix scaffold of fibrillin and emilin associated with the endocardium and the developing cardiac jelly. Between stages 22 and 29 the heart shows a transient elastic scaffold in the outflow tract which contains elastin, fibrillin, and emilin. Elastin-positive fibrillar material is also observed during these stages in the base of the atrioventricular cushion adjacent to the myocardial wall. In addition, emilin-positive material appears to be associated with the zones of formation of ventricular trabeculae. Collagen type VI was not detected during these early stages. From stage 30 to stage 40 a progressive modification of the pattern of distribution of elastin, fibrillin, emilin, and collagen type VI is observed in association with the formation of the definitive four-chambered heart. The distribution of the elastic scaffold in the outflow tract appears to be rearranged and becomes restricted to the roots of the main arteries. Each of the components studied here is also deposited at increasing levels in the developing valvular appa-ratus including the valve leaflets and the chordae tendinea. The components are also present in the subendocardial space where they form aligned fibrillar tracts, an arrangement suggestive of a role in ventricular contractile function. The epicardium constitutes an additional region of elastic matrix deposition during these later stages and contains elastic, fibrillin, and collagen type VI. Finally, during the later stages the intramyocardial matrix (''myocardial interstitium") is formed and characterized by an abundance of collagen type VI, emilin, and fibrillin but lacks elastin-positive material. This study suggests that during cardiac development there is not a fixed composition of the so-called "elastic matrix.'' Rather, combinations of the different components of the elastic matrice...

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“…Immature or newly synthesized fibers are rich in an acidic glycoprotein component (19) often designated as microfibrillar protein (17)(18)(19)(20). The microfibrils are found in the interstices and around the peripheries of elastic fibers.…”

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

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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.

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The identification of glycoproteins associated with elastic-tissue microfibrils

Cited by 76 publications

References 11 publications

The nature of the microfibrillar glycoproteins of elastic fibres. A biosynthetic study

The nature of the microfibrillar glycoproteins of elastic fibres. A biosynthetic study

Elastic extracellular matrix of the embryonic chick heart: An immunohistological study using laser confocal microscopy

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

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