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Lectin binding to elastic fibres and associated components during development of the human aorta

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Summary

A panel of peroxidase-conjugated lectins was used to stain frozen sections of human foetal, neonatal, infant and adult aortae. Two main distinctive staining patterns were observed at the light microscope level. depending on the lectin employed. Lectins from Concanavalin A,Triticum vulgaris, Arachis hypogaea andGlycine max resulted in staining of the surfaces of aortic elastic lamellae and the interlamellar areas. With lectins fromDolichos biflorus andBandeiraea simplicifolia staining was seen predominantly in the interlamellar areas. The findings indicate the presence of several different glycoconjugates at various sites within the aorta. In addition, there were alterations in the lectin binding affinities of the aortae that were dependent upon age. The findings are interpreted as indicating sequential changes in the composition of glycoprotein or proteoglycan moieties in the development of the human aorta.

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References

  • Bartholomew, J. S. &Anderson, J. C. (1983a) Distribution of proteoglycans and hyaluronic acid in transverse sections of bovine thoracic aorta.Histochem. J. 15, 941–51.

    Google Scholar 

  • Bartholomew, J. S. &Anderson, J. C. (1983b) Investigation of relationships between collagens elastin and proteoglycans in bovine thoracic aorta by immunofluorescence techniques.Histochem. J. 15, 1170–90.

    Google Scholar 

  • Bell, C. J. &Skerrow, C. J. (1984) Factors affecting the binding of lectins to normal human skin.Br. J. Dermat. 111, 517–26.

    Google Scholar 

  • Bhavanandan, V. P. &Katlic, A. W. (1979) The interaction of wheat germ agglutinin with sialoglycoproteins.J. biol. Chem. 254, 4000–8.

    Google Scholar 

  • Birembaut, P., Legrand, Y. J., Bariety, J., Bretton, R., Fauvel, F., Belair, M. F., Pignaud, G. &Caen, J. P. (1982) Histochemical and ultrastructural characterization of subendothelial glycoprotein microfibrils interacting with platelets.J. Histochem. Cytochem. 30, 75–80.

    Google Scholar 

  • Breathnach, S. M., Melrose, S. M., Bhogal, B., De Beer, F. C., Dyck, R. F., Tennent, G., Black, M. M. &Pepys, M. B. (1981) Amyloid P component is located on elastic fibre microfibrils in normal human tissues.Nature, Lond. 293, 652–3.

    Google Scholar 

  • Cleary, E. G. &Gibson, M. A. (1983) Elastin-associated microfibrils and microfibrillar proteins.Int. Rev. Conn. Tiss. Res. 10, 97–209.

    Google Scholar 

  • Coltoff-Schiller, B. &Goldfischer, S. (1981) Glycosaminoglycans in the rat aorta. Ultrastructural localization with toluidine blue O and osmium ferrocyanide procedures.Am. J. Path. 105, 232–40

    Google Scholar 

  • Davies, J. D. &Barnard, K. (1983) The control of elastosis: an hypothesis.J. Path. 139, 504.

    Google Scholar 

  • Davies, J. D., Young, E. W., Mera, S. L. &Barnard, K. (1983) Lysozyme is a component of human vascular elastic fibres.Experientia 39, 382–3.

    Google Scholar 

  • Eisenstein, R. &Kuettner, K. (1976) The ground substance of the arterial wall. Part 2. Electron microscopic studies.Atherosclerosis 27, 37–46.

    Google Scholar 

  • Fahrenbach, W. H., Sandberg, L. B. &Cleary, E. G. (1966) Ultrastructural studies on early elastogenesis.Anat. Rec. 155, 563–76.

    Google Scholar 

  • Fanning, J. C. &Cleary, E. G. (1985) Identification of glycoproteins associated with elastin-associated microfibrils.J. Histochem. Cytochem. 33, 287–94.

    Google Scholar 

  • Fukuda, M. &Hakomori, S. (1979) Carbohydrate structure of galactoprotein, a major transformation sensitive glycoprotein relased from hamster embryo fibroblast.J. biol. Chem. 254, 5451–7.

    Google Scholar 

  • Gibson, M. A. &Cleary, E. G. (1982) A collagen-like glycoprotein from elastic rich tissues.Biochem. Biophys. Res. Commun. 105, 1288–95.

    Google Scholar 

  • Goldstein, I. J., Holterman, C. E. &Smith, E. E. (1965) Protein-carbohydrate interaction. II. Inhibition studies on the interaction of Con A with polysaccharides.Biochemistry 4, 876–85.

    Google Scholar 

  • Coldstein, I. J., Hammarstrom, S. &Sundblad, G. (1975) Precipitation and carbohydrate binding specificity studies on wheat germ agglutinin.Biochim. biophys. Acta. 405, 53–61.

    Google Scholar 

  • Grant, M. E., Steven, F. S., Jackson, D. S. &Sandberg, J. B. (1971) Carbohydrate content of insoluble elastins prepared from adult bovine and calf ligamentum nuchae and tropoelastin isolated from copper-deficient porcine aorta.Biochem. J. 121, 197–202.

    Google Scholar 

  • Hynes, R. O. (1981) Fibronectin and its relation to cellular structure and behaviour. InCell Biology of Extracellular Matrix (edited byHay, E. D.) pp. 295–334. New York: Plenum Press.

    Google Scholar 

  • Jensen, B. A., Holund, B. &Clemmensen, I. (1983) Demonstration of fibronectin in normal and injured aorta by an indirect immunoperoxidase technique.Histochemistry 77, 395–403.

    Google Scholar 

  • Kadar, A., Gardner, D. L. &Bush, V. (1972) Glycosaminoglycans in developing chick embryo aorta revealed by ruthenium red: an electron microscope study.J. Path. 108, 275–80.

    Google Scholar 

  • Katsuyama, T. &Spicer, S. S. (1978) Histochemical differentiation of complex carbohydrates with variants of the Concanavalin A-horseradish peroxidase method.J. Histochem. Cytochem. 26, 233–50.

    Google Scholar 

  • Kewley, M. A., Stevens, F. S. &Williams, G. (1977) Preparation of a specific antiserum towards the microfibrillar protein of elastic tissues.Immunology 32, 483–9.

    Google Scholar 

  • Khan, A. M. &Walker, F. (1984) Age related detection of tissue amyloid P in the skin.J. Path. 143, 183–6.

    Google Scholar 

  • Kuhlmann, W. D., Peschke, P. &Wurster, K. (1983) Lectin-peroxidase conjugates in histopathology of gastointestinal mucosa.Virchows Archiv. A. 398, 319–28.

    Google Scholar 

  • Kumar, V., Berenson, G. S., Ruiz, H., Dalferes, E. R. &Strong, J. P. (1967) Acid mucopolysaccarides of human aorta.J. Atherosclerosis Res. 7, 573–90.

    Google Scholar 

  • Labat-Robert, J., Szendroi, M., Godeau, G. &Robert, L. (1985) Comparative distribution patterns of type I and III collagens and fibronectin in human arteriosclerotic aorta.Path. Biol. 33, 261–5.

    Google Scholar 

  • Leathem, J. C. &Atkins, N. J. (1983) Lectin binding to paraffin sections. InTechniques in Immunocytochemistry Vol. 2 (edited byBullock, G. R. andPetrusz, P.) pp. 39–70. London: Academic Press.

    Google Scholar 

  • Mangkornkanok-Mark, M., Eisenstein, R. &Bahu, R. H. (1981) Immunologic studies of bovine aortic and cartilage proteoglycans.J. Histochem. Cytochem. 29, 547–52.

    Google Scholar 

  • Mera, S. L., Lovett, F. &Davies, J. D. (1985) The effects of preliminary proteolysis on the immunohistochemical and dye staining properties of elastic fibres.Histochem. J. 17, 243–57.

    Google Scholar 

  • Moczar, M., Moczar, E. &Robert, L. (1967) Composition of the glycopeptides isolated from the structural glycoproteins of aortas of different species.Biochem. Biophys. Res. Commun. 28, 380–4.

    Google Scholar 

  • Muir, L. W., Bornstein, P. &Ross, R. (1976) A presumptive subunit of elastic fiber microfibrils secreted by arterial smooth muscle cells in culture.Eur. J. Biochem. 64, 105–14.

    Google Scholar 

  • Murata, K., Nakazawa, K. &Hamai, A. (1975) Distribution of acidic glycosaminoglycans in the intima, media, and adventitia of bovine aorta and their anticoagulant properties.Arteriosclerosis 21, 93–103.

    Google Scholar 

  • Pearse, A. C. E. (1985)Histochemistry: Theoretical and Applied, Vol. 2,Analytical Technology, 4th edn, pp. 688–9. Edinburgh: Churchill Livingstone.

    Google Scholar 

  • Prosser, I. W., Gibson, M. A. &Cleary, E. G. (1984) Microfibrillar protein from elastic tissue: a critical evaluation.Aust. J. exp. Biol. Med. Sci. 62, 485–505.

    Google Scholar 

  • Robert, L., Junqua, S. &Moczar, M. (1976) Structural glycoproteins of the intercelluar matrix. InFrontiers of Matrix Biology, Vol. 3 (edited byRobert, L.) pp. 113–42, Basel, Karger.

    Google Scholar 

  • Ross, R. &Bornstein, P. (1969) The elastic fibre. I. Separation and partial characterization of its macromolecular components.J. Cell Biol. 40, 366–81.

    Google Scholar 

  • Schwartz, E., Goldfischer, S., Coltoff-Schiller, B. &Blumenfeld, O. O. (1985) Extracellular matrix microfibrils are composed of core proteins coated with fibronectin.J. Histochem. Cytochem. 33, 268–74.

    Google Scholar 

  • Sear, C. H. J., Grant, M. E. &Jackson, D. S. (1981) The nature of the microfibrillar glycoproteins of elastic fibres.Biochem. J. 194, 487–98.

    Google Scholar 

  • Silbert, J. E. (1982) Structure and metabolism of proteoglycans and glycosaminoglycans.J. Invest. Dermat. 79, 31–7s.

    Google Scholar 

  • Stoward, P. J., Spicer, S. S. &Miller, R. L. (1980) Histochemical reactivity of peanut lectin horseradish peroxidase conjugate.J. Histochem. Cytochem. 28, 979–90.

    Google Scholar 

  • Tanimura, T., Nelson, T., Hollingsworth, R. R. &Shepard, T. H. (1971) Weight standards for organs from early human foetuses.Anat. Rec. 171, 227–36.

    Google Scholar 

  • Vaccaro, C. A. &Brody, J. S. (1979) Ultrastructural localization and characterization of proteoglycans in the pulmonary alveolus.Am. Rev. Resp. Dis. 120, 901–10.

    Google Scholar 

  • Wight, T. N. &Ross, R. (1975) Proteoglycans in primate arteries. II. Synthesis and secretion of glycosaminoglycans by arterial smooth muscle cells in culture.J. Cell Biol. 67, 675–86.

    Google Scholar 

  • Yamada, K. M. (1981) Fibronectin and otherstructural proteins. InCell Biology of the Extracelluar Matrix (edited byHay, E. D.), pp. 95–114. New York: Plenum Press.

    Google Scholar 

  • Yamada, K. &Shimizu, S. (1977) The histochemistry of galactose residues of complex carbohydrates as studied by peroxidase labelledRicinus communis agglutinin.Histochemistry 53, 143–56.

    Google Scholar 

  • Yamagata, T., Saito, H., Habuchi, O. &Suzuki, S. (1968) Purification and properties of bacterial chondroitinases and chondrosulphatases.J. biol. Chem. 243, 1523–35.

    Google Scholar 

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  1. University Department of Pathology, Bristol Royal Infirmary, BS2 8HW, Bristol, UK

    S. L. Mera & J. D. Davies

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  1. S. L. Mera
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  2. J. D. Davies
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Mera, S.L., Davies, J.D. Lectin binding to elastic fibres and associated components during development of the human aorta. Histochem J 17, 1359–1376 (1985). https://doi.org/10.1007/BF01002532

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  • DOI: https://doi.org/10.1007/BF01002532

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