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

Sear, Christopher H. J.; Grant, Michael E.; Jackson, David S.

doi:10.1042/bj1940587

Cited by 80 publications

(27 citation statements)

References 58 publications

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“…Early studies revealed their anionic staining characteristics and that they comprise collagenase-resistant glycoproteins. A major glycoprotein of apparent M r 300,000, designated microfibrillar protein (MFP) II, was then identified (Sear et al 1978;Sear et al 1981a;Sear et al 1981b). MFPII from microfibrilrich foetal bovine nuchal ligament fibroblast cultures was metabolically labelled, immunoprecipitated with anti-microfibrillar protein serum and analysed by SDS-PAGE and gel filtration.…”

Section: Discoverymentioning

confidence: 99%

Fell‐Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?

2017

Int J Experimental Path

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SummaryFibrillin microfibrils are indispensable structural elements of connective tissues in multicellular organisms from early metazoans to humans. They have an extensible periodic beaded organization, and support dynamic tissues such as ciliary zonules that suspend the lens. In tissues that express elastin, including blood vessels, skin and lungs, microfibrils support elastin deposition and shape the functional architecture of elastic fibres. The vital contribution of microfibrils to tissue form and function is underscored by the heritable fibrillinopathies, especially Marfan syndrome with severe elastic, ocular and skeletal tissue defects. Research since the early 1990s has advanced our knowledge of biology of microfibrils, yet understanding of their mechanical and homeostatic contributions to tissues remains far from complete. This review is a personal reflection on key insights, and puts forward the conceptual hypothesis that microfibrils are structural ‘tensometers’ that direct cells to monitor and respond to altered tissue mechanics.

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Section: Discoverymentioning

confidence: 99%

Fell‐Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?

2017

Int J Experimental Path

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“…Initial attempts to isolate microfibrillar proteins utilised a series of steps which included collagenase digestion and guanidine extraction of tissue in the presence of an agent to reduce the disulphide bonds (Gibson and Cleary, 1983;Kewley et al, 1977;Sear et al, 1978Sear et al, , 1981. In one study, five putative microfibrillar glycoproteins ranging in M r from 340,000 to 25,000 were isolated from reductive saline extracts of foetal bovine nuchal ligament (Gibson et al, 1986).…”

Section: Fibrillin-containing Microfibrilsmentioning

confidence: 99%

Microfibrillar elements of the dermal matrix

Kielty¹,

Shuttleworth²

1997

Microsc. Res. Tech.

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Connective tissue microfibrils are key structural elements of the dermal matrix which play major roles in establishing and maintaining the structural and mechanical integrity of this complex tissue. Type VI collagen microfibrils form extensive microfibrillar networks which intercalate between the major collagen fibrils and are juxtaposed to cellular basement membranes, blood vessels and other interstitial structures. Fibrillin microfibrils define the continuous elastic network of skin, and are present in dermis as microfibril bundles devoid of measureable elastin extending from the dermal‐epithelial junction and as components of the thick elastic fibres present in the deep reticular dermis. Electron microscopic analyses have revealed both classes of microfibrils to have complex ultrastructures. The ability to isolate intact native microfibrils from skin has enabled a combination of high resolution and biochemical techniques to be applied to elucidate their structure:function relationships. These approaches have generated new information about their molecular organisation and physiological interactions in health and disease. Microsc. Res. Tech. 38:413–427, 1997. © 1997 Wiley‐Liss, Inc.

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“…Perhaps basotubules share some, but not all, components with microfibrils. Breathnach et al (30) have proposed that the amyloid P component is associated with MFP I, one of the two glycoproteins extracted from microfibrils by Sear et al (42).…”

Section: Network Of Cordsmentioning

confidence: 99%

Ultrastructure of Reichert's membrane, a multilayered basement membrane in the parietal wall of the rat yolk sac.

Inoué¹,

Leblond²,

Laurie³

1983

The Journal of Cell Biology

126

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The ultrastructure of Reichert's membrane, a thick basement membrane in the parietal wall of the yolk sac, has been examined in 13-14-d pregnant rats. This membrane is composed of more or less distinct parallel layers, each one of which resembles a common basement membrane. After routine fixation in glutaraldehyde followed by osmium tetroxide, the layers appear to be mainly composed of 3-8-nm thick cords arranged in a threedimensional network. Loosely scattered among the cords are unbranched, straight tubular structures with a diameter of 7-10 nm, which mainly run parallel to the surface and to one another; they are referred to as basotubules. Permanganate fixation emphasizes the presence of a thick feltwork of irregular material around basotubules. Finally, minute dot-like structures measuring 3.5 nm and referred to as double pegs are present within the meshes of the cord network.Reichert's membranes have been treated for 2-48 h at 25°C with plasmin, a proteolytic enzyme known to rapidly digest laminin and fibronectin. After a 2-h treatment, most of the substance of the cords is digested away leaving a three-dimensional network of 1.5-2.0-nm thick filaments. The interpretation is that the cords are formed of a plasmin-resistant core filament and a plasmin-extractable sheath. When plasmin treatment is prolonged for 15 h or longer, the filaments are dissociated and disappear, while basotubules are maintained. Plasmin digestion also reveals that basotubules are composed of two parts: a ribbon-like helical wrapping and tubule proper. Further changes in the tubule under plasmin influence are interpreted as a dissociation into pentagonal units suggestive of the presence of the amyloid P component. After 48 h of plasmin treatment, basotubules are further disaggregated and dispersed, leaving only linearly arranged double pegs.Reichert's membranes with or without a 2-hr plasmin treatment have been immunostained by exposure to antibodies against either laminin or type IV collagen with the help of peroxidase markers. The results indicate that the sheath of the cords contains laminin antigenicity, while the core filament contains type IV collagen antigenicity.It is proposed that Reichert's membrane consists mainly of a three-dimensional network of cords composed of a type IV collagen filament enclosed within a laminin-containing sheath. Also present are basotubules--which may contain the amyloid P component--and double pegs whose nature is unknown.

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

Cited by 80 publications

References 58 publications

Fell‐Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?

Fell‐Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?

Microfibrillar elements of the dermal matrix

Ultrastructure of Reichert's membrane, a multilayered basement membrane in the parietal wall of the rat yolk sac.

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