, Volume 154, Issue 1, pp 241–260 | Cite as

Biochemical definition of human tracheobronchial mucus

  • P. Roussel
  • P. Degand
  • G. Lamblin
  • A. Laine
  • J. J. Lafitte


Tracheobronchial mucus is a heterogeneous milieu produced by several cell types. It has viscoelastic properties related to the organization of macromolecular components such as glycoproteins, proteins, lipids and nucleic acids. Proteins comprise components antigenically related to plasma proteins and secretory proteins such as kallicrein, lysozyme, amylase, bronchotransferrin, immunoglobulins A and proline-rich polypeptides. Tracheobronchial mucus also contains protease inhibitors and, in pathological conditions, important amounts of protease. Mucins, which are glycoproteins with a very rich carbohydrate content, represent another complex and major group of tracheobronchial molecules.

Key words

Sputum biochemistry Bronchial secretion Bronchial mucins Bronchial proteins Bronchopulmonary lavages 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Afzelius, B.A.: A human syndrome caused by immotile cilia. Science193, 317–319 (1976)PubMedCrossRefGoogle Scholar
  2. 2.
    Bailleul, V., Richet, C., Hayem, A., Degand, P.: Propriétés rhéologiques des sécrétions bronchiques: mise en évidence et rôle des polypeptides riches en proline (PRP). Clin. Chim. Acta74, 115–123 (1977)PubMedCrossRefGoogle Scholar
  3. 3.
    Baker, A.P., Munro, J.R.: Multiglycosyltransferase system of canine respiratory tissue. J. Biol. Chem.246, 4358–4362 (1971)PubMedGoogle Scholar
  4. 4.
    Baker, A.P., Sawyer, J.L., Munro, J.R., Weiner, G.P., Hillegass, L.M.: Glycosyltransferases of canine respiratory tissue. J. Biol. Chem.247, 5173–5179 (1972)PubMedGoogle Scholar
  5. 5.
    Baker, A.P., Griggs, L.J., Munro, J.R., Finkelstein, J.A.: Blood group A active glycoproteins of respiratory mucus and their synthesis by an N-acetylgalactosaminyltransferase. J. Biol. Chem.248, 880–883 (1973)PubMedGoogle Scholar
  6. 6.
    Baker, A.P., Chakrin, L.W., Wardell, J.R.: Chronic cholinergic stimulation of canine respiratory tissue. Its effects on the activities of glycosyltransferases and release of macromolecules. Am. Rev. Resp. Dis.111, 423–431 (1975)PubMedGoogle Scholar
  7. 7.
    Baker, A.P., Sawyer, J.L.: Glycosyltransferases in human respiratory tissue. Biochem. Med.14, 42–50 (1975)PubMedCrossRefGoogle Scholar
  8. 8.
    Baker, A.P., Hillegass, L.M., Holden, D.A., Smith, W.J.: Effect of kallidin, substance P and other basic polypeptides on the production of respiratory macromolecules. Am. Rev. Resp. Dis.115, 811–817 (1977)PubMedGoogle Scholar
  9. 9.
    Baskerville, A.: The development and persistence of bronchial-gland hypertrophy and goblet-cell hyperplasia in the pig after injection of isoprenaline. J. Pathol.119, 35–47 (1976)PubMedCrossRefGoogle Scholar
  10. 10.
    Bhattacharyya, S.N., Sahu, S., Lynn, W.S.: Structural studies on a glycoprotein isolated from alveoli of patients with alveolar proteinosis. Biochim. Biophys. Acta427, 91–106 (1976)PubMedGoogle Scholar
  11. 11.
    Bhattacharyya, S.N., Lynn, W.S.: Structural studies on the oligosaccharides of a glycoprotein isolated from alveoli of patients with alveolar proteinosis. J. Biol. Chem.252, 1172–1180 (1977)PubMedGoogle Scholar
  12. 12.
    Biserte, G., Havez, R., Cuvelier, R.: Les glycoprotéides des sécrétions bronchiques. Exp. Ann. Biochim. Med.24, 85–120 (1963)Google Scholar
  13. 13.
    Boat, T.F., Matthews, L.W.: Chemical composition of human tracheo bronchial secretions. In: Sputum, pp. 243–274 (ed. M.J. Dulfano). Springfield (Ill.): C.C. Thomas 1973Google Scholar
  14. 14.
    Boat, T.F., Kleinerman, J.L.: Human respiratory tract secretions. Effect of cholinergic and adrenergic agents on in vitro release of protein and mucous glycoprotein. Chest67 (Suppl.), 325–345 (1975)CrossRefGoogle Scholar
  15. 15.
    Boat, T.F., Cheng, P.W., Iyer, R.N., Carlson, D.M., Polony, I.: Human respiratory tract secretions. Arch. Biochem. Biophys.177, 95–104 (1976)PubMedCrossRefGoogle Scholar
  16. 16.
    Bowes, D., Corrin, B.: Ultrastructural immunocytochemical localisation of lysozyme in human bronchial glands. Thorax32, 163–170 (1977)PubMedCrossRefGoogle Scholar
  17. 17.
    Brandtzaeg, P.: Immunohistochemical studies on various aspects of glandular immunoglobulin transport in man. Histochem. J.9, 553–572 (1977)PubMedCrossRefGoogle Scholar
  18. 18.
    Brogan, T.D.: The high molecular weight components of sputum. Brit. J. Exp. Pathol.41, 288–297 (1960)Google Scholar
  19. 19.
    Brogan, T.D., Ryley, H.C., Neale, L., Yassa, J.: Soluble proteins of bronchopulmonary secretions from patients with cystic fibrosis, asthma and bronchitis. Thorax30, 72–79 (1975)PubMedCrossRefGoogle Scholar
  20. 20.
    Bukantz, S.C., Berns, A.W.: Studies with sputum. I - Initial observation on the chemical nature and blood group substance content of asthmatic sputum. J. Allergy29, 29–43 (1958)CrossRefGoogle Scholar
  21. 21.
    Bürgi, H., Wiesman, U., Richterich, R., Regli, J., Medici, T.: New objective criteria for inflammation in bronchial secretions. Brit. Med. J. 1968/II, 654-656Google Scholar
  22. 22.
    Christensen, T.G., Korthy, A.L., Snider, G.L., Hayes, J.A.: Irreversible bronchial goblet-cell metaplasia in hamsters with elastase induced panacinar emphysema. J. Clin. Invest.59, 397–404 (1977)PubMedCrossRefGoogle Scholar
  23. 23.
    Degand, P.: Examen biochimique des sécrétions bronchiques. Intérêt dans le traitement de l’hypersécrétion bronchique. In: Sécrétions et excrétions bronchiques. Monographies du Collège de Médecine des Hôpitaux de Paris (Expansion Scientifique), p. 32–36. Paris, 1976Google Scholar
  24. 24.
    Degand, P., Roussel, P., Lamblin, G., Havez, R.: Purification et étude des mucines de kystes bronchogéniques. Biochim. Biophys. Acta320, 318–330 (1973)PubMedGoogle Scholar
  25. 25.
    Degand, P., Ruffin, P., Lamblin, G., Havez, R.: Etude en ultracentrifugation de deux mucines bronchiques humaines. C. R. Acad. Sci. (Paris)276, 113–116 (1973)Google Scholar
  26. 26.
    Degand, P., Roussel, P., Lamblin, G.: Définition des mucines synthétisées au niveau de kystes bronchogéniques. Clin. Chim. Acta50, 223–236 (1974)CrossRefGoogle Scholar
  27. 27.
    Elliasson, R., Mossberg, B., Camner, P., Afzelius, B.A.: Immotile cilia, chronic airway infections and male sterility. N. Engl. J. Med.297, 1–6 (1977)CrossRefGoogle Scholar
  28. 28.
    Havez, R., Degand, P., Roussel, P., Biserte, G.: Isolement et caractérisation immunologique de la kallicréine bronchique humaine. C. R. Acad. Sci. (Paris)262, 309–311 (1966)Google Scholar
  29. 29.
    Havez, R., Roussel, P., Degand, P., Biserte, G.: Etude des structures fibrillaires de la sécrétion bronchique humaine. Clin. Chim. Acta17, 281–295 (1967)PubMedCrossRefGoogle Scholar
  30. 30.
    Havez, R., Roussel, P., Degand, P., Delmas-Marsalet, Y., Biserte, G.: Etude des substances de groupe sanguin A isolées de mucus bronchique. Bull. Soc. Chim. Biol.51, 245–259 (1969)PubMedGoogle Scholar
  31. 31.
    Havez, R., Roussel, P.: Bronchial mucus: physical and biochemical features. In: Bronchial Asthma, pp. 409–422 (eds. E.B. Weiss and M.S. Segal). Boston: Little, Brown and Co. 1976Google Scholar
  32. 32.
    Hochstrasser, K., Reichert, R., Schwarz, S., Werle, E.: Isolierung und Charakterisierung eines Protease Inhibitors aus menschlichem Bronchialsekret. Hoppe-Seyler’s Z. Physiol. Chem.353, 221–226 (1972)PubMedGoogle Scholar
  33. 33.
    Hochstrasser, K., Reichert, R., Heimburger, N.: Antigenic relationship between the human bronchial mucus inhibitor and plasma inter α-trypsin inhibitor. Hoppe-Seyler’s Z. Physiol. Chem.354, 587–588 (1973)PubMedGoogle Scholar
  34. 34.
    Hochstrasser, K., Reichert, R., Schwarz, S., Werle, E.: Detection and isolation of a second acid-stable proteinase inhibitor from human bronchial mucus. Hoppe Seyler’s Z. Physiol. Chem.354, 923–926 (1973)PubMedGoogle Scholar
  35. 35.
    Hochstrasser, K., Schorn, K., Rasche, B., Lemparth, K., Raffelt, C.: Characterization of masked specific proteinase inhibitor from bronchial secretions in purulent sputum as complex with leucocytic proteinase. Pneumonologie152, 15–24 (1975)PubMedCrossRefGoogle Scholar
  36. 36.
    Ishizaka, K., Newcomb, R.W.: Presence of γE in nasal washings and sputum from asthmatic patients. J. Allerg.46, 197–204 (1970)PubMedCrossRefGoogle Scholar
  37. 37.
    Janoff, A., Sloan, B., Weinbaum, G., Damiano, V., Sandhaus, R.A., Elias, J., Kimbel, P.: Experimental emphysema induced with purified human neutrophil elastase: tissue localization of the instilled protease. Am. Rev. Respir. Dis.115, 461–478 (1977)PubMedGoogle Scholar
  38. 38.
    Kaplan, P.D., Kuhn, C., Pierce, J.A.: The induction of emphysema with elastase. I - The evolution of the lesion and the influence of serum. J. Lab. Clin. Med.82, 349–356 (1973)PubMedGoogle Scholar
  39. 39.
    Klockars, M., Reitamo, S.: Tissue distribution of lysozyme in man. J. Histochem. Cytochem.23, 932–940 (1975)PubMedGoogle Scholar
  40. 40.
    Kollerstrom, N., Lord, P.W., Whimster, W.F.: A difference in the composition of bronchial mucus. Thorax32, 155–159 (1977)PubMedCrossRefGoogle Scholar
  41. 41.
    Lafitte, J.J., Lamblin, G., Lhermitte, M., Humbert, P., Degand, P., Roussel, P.: Etude des mucines humaines obtenues par lavage de bronches macroscopiquement saines. Carbohyd. Res.56, 383–389 (1977)Google Scholar
  42. 42.
    Laine, A., Hayem, A.: Identification et caractérisation des constituants protéiques de la sécrétion bronchique humaine. Clin. Chim. Acta67, 159–167 (1976)PubMedCrossRefGoogle Scholar
  43. 43.
    Laine, A., Hayem, A.: Constituants protéiques de liquides de lavages bronchiques humains. Bull. Europ. Physiopath. Resp.13, 47–56 (1977)Google Scholar
  44. 44.
    Lamb, D.: Acidic glycoproteins of the mucous glands of the bronchus in cystic fibrosis (mucoviscidosis). In: Colloq. Int. Pathol. Thorac. Lille (Hypersécrétion bronchique), pp. 143–153. Clichy, France: Poinsot, 1968Google Scholar
  45. 45.
    Lamb, D., Reid, L.: Histochemistry, autoradiography, tissue culture and biochemical analysis in the study of bronchial epithelial glycoproteins. In: Colloq. Int. Pathol. Thorax. Lille (Hypersécrétion bronchique), pp. 11–22. Clichy, France: Poinsot, 1968Google Scholar
  46. 46.
    Lamblin, G., Roussel, P., Mazzuca, M., Degand, P.: Action de la bradykinine et de différentes molécules basiques sur les battements ciliaires de la trachée de lapin. C. R. Soc. Biol. (Paris)166, 618–621 (1972)Google Scholar
  47. 47.
    Lamblin, G., Lhermitte, M., Degand, P., Sergeant, Y.H., Roussel, P.: Isolation and immunological properties of neutral bronchial mucins from a patient with chronic bronchitis. Biochim. Biophys. Acta322, 372–382 (1973)PubMedGoogle Scholar
  48. 48.
    Lamblin, G., Lhermitte, M., Lafitte, J.J., Filliat, M., Degand, P., Roussel, P.: Etude comparative des mucines bronchiques purifiées à partir de l’expectoration de sujets atteints de mucoviscidose ou d’autres affections bronchiques chroniques. Bull. Europ. Physiopath. Resp.13, 175–190 (1977)Google Scholar
  49. 49.
    Lamblin, G., Humbert, P., Degand, P., Roussel, P.: Hétérogénéité des chaînes glycanniques des mucines bronchiques isolées à partir de l’expectoration de deux sujets atteints de bronchite chronique. Clin. Chim. Acta79, 425–436 (1977)PubMedCrossRefGoogle Scholar
  50. 50.
    Lev, R., Spicer, S.S.: A histochemical comparison of human epithelia mucins in normal and in hypersecretory states including pancreatic cystic fibrosis. Am. J. Pathol.46, 23–47 (1965)PubMedGoogle Scholar
  51. 51.
    Lewis, R.W.: Lipid composition of human bronchial mucus. Lipids6 859–861 (1971)PubMedCrossRefGoogle Scholar
  52. 52.
    Lhermitte, M., Lamblin, G., Humbert, P., Roussel, P., Biserte, G.: Rôle d’adjuvant immunitaire des mucines bronchiques humaines à l’égard de protéines du sérum humain. C. R. Acad. Sci. (Paris)282, 1057–1058 (1976)Google Scholar
  53. 53.
    Lhermitte, M., Lamblin, G., Lafitte, J.J., Rousseau, J., Degand, P., Roussel, P.: Properties of human neutral bronchial mucins after modification of the peptide or the carbohydrate moieties. Biochimie58, 367–372 (1976)PubMedCrossRefGoogle Scholar
  54. 54.
    Lhermitte, M., Lamblin, G., Degand, P., Roussel, P.: Affinity of bronchial secretion glycoproteins and cells of human bronchial mucosa for Ricinus communis lectins. Biochimie59, 611–620 (1977)PubMedCrossRefGoogle Scholar
  55. 55.
    Lhermitte, M., Roche, A.C., Roussel, P., Mazzuca, M.: Affinity for human bronchial mucosa and secretions. In: Proc. of 4th International Symposium of Glycoconjugates (in press)Google Scholar
  56. 56.
    Lieberman, J., Trimmer, B.M., Kurnick, N.B.: Substrate specificity of protease activities in purulent sputum. Lab. Invest.14, 249–257 (1965)PubMedGoogle Scholar
  57. 57.
    Lieberman, J., Gaward, M.A.: Inhibitors and activators of leukocytic proteases in purulent sputum. Digestion of human lung inhibition by α1-antitrypsin. J. Lab. Clin. Med.77, 713–727 (1971)PubMedGoogle Scholar
  58. 58.
    Lieberman, J., Kaneshiro, W.: Inhibition of leukocytic elastase from purulent sputum by α1-antitrypsin. J. Lab. Clin. Med.80, 88–101 (1972)PubMedGoogle Scholar
  59. 59.
    Lorenz, T.H., Korst, D., Simpson, J.F., Musser, M.J.: A quantitative method of bronchial lysozyme I. An investigation of bronchial lysozyme. J. Lab. Clin. Med.49, 145–150 (1957)PubMedGoogle Scholar
  60. 60.
    Louisot, P., Levrat, C., Gilly, R.: A new pathogenic hypothesis for cystic fibrosis: Hyperactivity of glycosyl transferases at microsomic level. Clin. Chim. Acta48, 373–376 (1973)PubMedCrossRefGoogle Scholar
  61. 61.
    Martinez-Tello, F.J., Braun, D.G., Blanc, W.A.: Immunoglobulin production in bronchial mucosa and bronchial lymph nodes, particularly in cystic fibrosis of the pancreas. J. Immunol.101, 989–1003 (1968)PubMedGoogle Scholar
  62. 62.
    Masson, P.L., Heremans, J.F.: Molecular size of γA-immunoglobulin from bronchial secretions. Biochim. Biophys. Acta120, 172–173 (1966)PubMedCrossRefGoogle Scholar
  63. 63.
    Masson, P.L., Heremans, J.F., Prignot, J.J., Wauters, G.: Immunohistochemical localisation and bacteriostatic properties of an ironbinding protein from bronchial mucus. Thorax21, 538–541 (1966)PubMedCrossRefGoogle Scholar
  64. 64.
    Masson, P.L., Heremans, J.F.: Sputum proteins. In: Sputum, pp. 412–475 (ed. M.J. Dulfano). Springfield (Ill.): C.C. Thomas 1973Google Scholar
  65. 65.
    Mazzuca, M., Roche, A.C., Lhermitte, M., Roussel, P.: Limulus polyphemus lectin sites in human bronchial mucosa. J. Histochem. Cytochem.25, 470–473 (1977)PubMedGoogle Scholar
  66. 66.
    Meyer, F.A.: Comparison of structural glycoproteins from mucus of different sources. Biochim. Biophys. Acta493, 272–282 (1977)PubMedGoogle Scholar
  67. 67.
    Ohlsson, K., Olsson, I.: The neutral proteases of human granulocytes. Isolation and partial characterization of two granulocytes collagenases. Europ. J. Biochem.36, 473–481 (1975)CrossRefGoogle Scholar
  68. 68.
    Ohlsson, K., Tegner, H.: Granulocytes collagenase, elastase and plasma protease inhibitors in purulent sputum. Europ. J. Clin. Invest.5, 221–227 (1975)PubMedCrossRefGoogle Scholar
  69. 69.
    Ohlsson, K., Tegner, H.: Inhibition of elastase from granulocytes by the low molecular weight bronchial protease inhibitor. Scand. J. Clin. Lab. Invest.36, 437–445 (1976)PubMedCrossRefGoogle Scholar
  70. 70.
    Passero, M.A., Ross, W.T., Kilburn, K.H., Lynn, W.S.: Isolation and characterization of two glycoproteins from patients with alveolar proteinosis. Proc. Natl. Acad. Sci. USA70, 973–976 (1973)PubMedCrossRefGoogle Scholar
  71. 71.
    Potter, J.L., Matthews, L.W., Lemm, J., Spector, S.: Human pulmonary secretions in health and disease. Ann. N.Y. Acad. Sci.106, 692–697 (1963)PubMedCrossRefGoogle Scholar
  72. 72.
    Puchelle, E., Zahm, J.M., Havez, R.: Biochemical and rheological data in sputum. III. Relationship between the biochemical constituents and the rheological properties of sputum. Bull. Physiopath. Resp.9, 237–256 (1973)Google Scholar
  73. 73.
    Puchelle, E., Girard, F., Beck, G., Hayem, A., Bailleul, V., Laine, A.: Propriétés rhéologiques et biochimiques de l’expectoration. Path. Biol.24, 93–96 (1976)Google Scholar
  74. 74.
    Ramirez, R.J., Harlan, W.R.: Pulmonary alveolar proteinosis. Am. J. Med.45, 502–512 (1968)PubMedCrossRefGoogle Scholar
  75. 75.
    Reid, L.: Measurement of the bronchial mucous gland layer: a diagnostic yardstick in chronic bronchitis. Thorax15, 132–141 (1960)PubMedCrossRefGoogle Scholar
  76. 76.
    Reid, L.: Natural history of mucus in the bronchial tree. Arch. Environ. Health10, 265–273 (1965)PubMedGoogle Scholar
  77. 77.
    Reid, L., De Haller, R.: The bronchial mucous glands. Their hypertrophy and change in intracellular mucus. Bibl. Paediatr.86, 195–199 (1967)PubMedGoogle Scholar
  78. 78.
    Reid, L.: Disturbances in the pattern of secretion of bronchial mucous glands. In: Cystic Fibrosis, Ciba Foundation no. 32, pp. 45–67, (eds. Porter R., O’Connor, M.). Boston: Little Brown and Co. 1968Google Scholar
  79. 79.
    Reid, L.: Histopathological aspects of bronchial secretion. Scand. J. Resp. Dis. (Supplem. no 90), 9–15 (1974)Google Scholar
  80. 80.
    Reynolds, H.Y., Newball, H.H.: Analysis of proteins and respiratory cells obtained from human lungs by bronchial lavage. J. Lab. Clin. Med. 84, 559–573 (1974)PubMedGoogle Scholar
  81. 81.
    Reynolds, H.Y., Fulmer, J.D., Kazmierowski, J.A., Roberts, W.C., Frank, M., Crystal, R.G.: Analysis of cellular and protein content of bronchoalveolar lavage fluid from patients with idiopathic pulmonary fibrosis and chronic hypersensivity pneumonitis. J. Clin. Invest.59, 165–175 (1977)PubMedCrossRefGoogle Scholar
  82. 82.
    Roberts, G.P.: Isolation and characterization of glycoproteins from sputum. Europ. J. Biochem.50, 265–280 (1974)PubMedCrossRefGoogle Scholar
  83. 83.
    Roberts, G.P.: The role of disulfide bonds in maintaining the gel structure of bronchial mucus. Arch. Biochem. Biophys.173, 528–537 (1976)PubMedCrossRefGoogle Scholar
  84. 84.
    Roussel, P., Lamblin, G., Degand, P., Havez, R.: Isolement des mucines bronchiques sécrétées au cours de la mucoviscidose. Clin. Chim. Acta.36, 315–328 (1972)PubMedCrossRefGoogle Scholar
  85. 85.
    Roussel, P., Lamblin, G., Degand, P., Walker-Nasir, E., Jeanloz, R.W.: Heterogeneity of the carbohydrate chains of sulfated bronchial glycoproteins isolated from a patient suffering from cystic fibrosis. J. Biol. Chem.250, 2114–2122 (1975)PubMedGoogle Scholar
  86. 86.
    Ryley, H.C.: An immunoelectrophoretic study of the soluble secretory proteins of sputum. Biochim. Biophys. Acta271, 300–309 (1972)Google Scholar
  87. 87.
    Sahu, S., Di Augustine, R.P., Lynn, W.S.: Lipids found in pulmonary lavage of patients with alveolar proteinosis and in rabbit lung lamellar organelles. Am. Rev. Resp. Dis.114, 177–184 (1976)PubMedGoogle Scholar
  88. 88.
    Sahu, S., Lynn, W.S.: Lipid composition of airway secretions from patients with asthma and patients with cystic fibrosis. Am. Rev. Resp. Dis.115, 233–239 (1977)PubMedGoogle Scholar
  89. 89.
    Sheffner, A.L.: The reduction in vitro in viscosity of mucoprotein solution by a new mucolytic agent, N-acetylcysteine. Ann. N.Y. Acad. Sci.106, 298–310 (1963)PubMedCrossRefGoogle Scholar
  90. 90.
    Smith, J.M.: Interference with tryptic digestion by sputum from asthmatic patients. Am. Rev. Resp. Dis.88, 858–860 (1963)PubMedGoogle Scholar
  91. 91.
    Spicer, S.S., Chakrin, L.W., Wardell, J.: Respiratory mucous secretion. In: Sputum, pp. 22–68 (ed. M.J. Dulfano). Springfield (Ill.): C.C. Thomas 1973Google Scholar
  92. 92.
    Stahl, G.H., Ellis, D.B.: Biosynthesis of respiratory-tract mucins. A comparison of canine epithelial goblet-cell and submucosal-gland secretions. Biochem. J.136, 845–850 (1973)PubMedGoogle Scholar
  93. 93.
    Sturgess, J., Reid, L.: Secretory activity of the human bronchial mucous glands in vitro. Exp. Mol. Path.16, 362–381 (1972)CrossRefGoogle Scholar
  94. 94.
    Sturgess, J., Reid, L.: An organ culture study of the effect of drugs on the secretory activity of the bronchial submucosal gland. Clin. Sci.43, 533–543 (1972)PubMedGoogle Scholar
  95. 95.
    Sturgess, J., Reid, L.: The effect of isoprenaline and pilocarpine on bronchial mucus secreting tissue and pancreas, salivary glands, heart, thymus, liver and spleen. Brit. J. Exp. Path.54, 388–403 (1973)PubMedGoogle Scholar
  96. 96.
    Tegner, H., Ohlsson, K.: Localization of a low molecular weight protease inhibitor to tracheal and maxillary sinus mucosa. Hoppe-Seyler’s Z. Physiol. Chem.358, 425–429 (1977)PubMedGoogle Scholar
  97. 97.
    Tegner, H., Ohlsson, K., Olsson, I.: The interactions between a low molecular weight protease inhibitor of bronchial mucus and chymotrypsin-like cationic proteins of granulocytes. Hoppe-Seyler’s Z. Physiol. Chem.358, 431–433 (1977)PubMedGoogle Scholar
  98. 98.
    Toremtram, N.C.: The daily amount of tracheo-bronchial secretions in man. Acta Otolaryngol. (Stockh.)158 (Suppl.), 43–53 (1960)Google Scholar
  99. 99.
    Tourville, D.R., Adler, R.H., Bienenstock, J., Tomasi, T.B.: The human secretory immunoglobulin system. Immunohistological localization of γA "secretory piece" and lactoferrin in normal tissues. J. Exp. Med.129, 411–423 (1969)PubMedCrossRefGoogle Scholar
  100. 100.
    Twumasi, D.Y., Liener, I.E.: Protease from purulent sputum purification and properties of the elastase and chymotrypsin-like enzymes. J. Biol. Chem.252, 1917–1926 (1977)PubMedGoogle Scholar
  101. 101.
    Warembourg, H., Havez, R., Sezille, G., Sherpereel, P., Roussel, P. Degand, P.: Les lipides de l’expectoration. Isolement et caractérisation du surfactant pulmonaire dans l’expectoration. In: Hypersecrétion Bronchique, Colloq. Int. Pathol. Thorac., Lille, pp. 181–192. Clichy, France: Poinsot, 1968Google Scholar
  102. 102.
    Warr, G.A., Martin, R.R., Sharp, P.M., Rossen, R.D.: Normal human immunoglobulins and proteins. Am. Rev. Resp. Dis.116, 25–30 (1977)PubMedGoogle Scholar
  103. 103.
    Whimster, W.F., Reid, L.: The influence of dibutyryl cyclic adenosine monophosphate and other substances on human bronchial mucous gland discharge. Exp. Mol. Pathol.18, 234–240 (1973)PubMedCrossRefGoogle Scholar
  104. 104.
    Yeager, H.: Tracheobronchial secretions. Am. J. Med.50, 493–509 (1971)PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag 1976

Authors and Affiliations

  • P. Roussel
    • 1
  • P. Degand
    • 1
  • G. Lamblin
    • 1
  • A. Laine
    • 1
  • J. J. Lafitte
    • 1
  1. 1.Unité de Recherches No. 16 I.N.S.E.R.M. Place de VerdunLille CédexFrance

Personalised recommendations