Summary
In addition to bovine pancreatic trypsin inhibitor (BPTI), three BPTI-related molecular forms (isoinhibitors I, II and III) were isolated from bovine lung by affinity chromatography on immobilized trypsin and subsequently purified by Fast Protein Liquid Chromatography. These inhibitors are identical to the isoinhibitors previously isolated from bovine spleen. Their localization in bovine lung was studied by immunohistochemical techniques, using two different immunoglobulin preparations, selectively recognizing BPTI or the other molecular forms.
BPTI-related immunoreactivity was found to be restricted to isolated cells, often identified as mast cells by Toluidine Blue staining. In contrast, isoinhibitor-related immunoreactivity, which also occurs in the mast cells, is present in a number of other cell types. These types include: (i) the smooth muscle cells of different calibre vessels, (ii) the ciliated cells of the bronchial epithelium and the related mucus, and (iii) many cells at alveolar level.
Comparison of these data with previous results obtained for bovine spleen suggest multiple physiological roles for these inhibitors.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
ANDERSON, S., & KINGSTON, I. B. (1983) Isolation of a genomic clone for bovine pancreatic trypsin inhibitor by a unique-sequence synthetic DNA probe.Proc. Natl. Acad. Sci. USA 80, 6838–42.
BARRA, D., SIMMACO, M., BOSSA, F., FIORETTI, E., ANGELETTI, M., & ASCOLI, F. (1987) Primary structure of a protease isoinhibitor from bovine spleen: a possible intermediate in the processing of the primary gene product.J. Biol. Chem. 262, 13916–9.
BUSINARO, R., FIORETTI, E., FUMAGALLI, L., CITRO, G., DE RENZIS, G. & ASCOLI, F. (1987) Vascular localization of bovine pancreatic trypsin-inhibitor related molecular forms in bovine spleen.Eur. J. Biochem. 165, 79–82.
CREIGHTON, T. E., & CHARLES, I. G. (1987) Sequences of the genes and polypeptide precursors for two bovine protease inhibitors.J. Mol. Biol. 194, 11–22.
FIORETTI, E., BINOTTI, I., BARRA, D., CITRO, G., ASCOLI, F., & ANTONINI, E. (1983) Heterogeneity of the basic pancreatic inhibitor (Kunitz) in various bovine organs.Eur J. Biochem. 130, 13–18.
FIORETTI, E., CITRO, G., & ASCOLI, F. (1984) Immunochemical studies on the Kunitz type inhibitors from bovine spleen.Prep. Biochem. 14, 389–401.
FIORETTI, E., ANGELETTI, M., CITRO, G., & ASCOLI, F. (1985a) Characterization of three new Kunitz-type inhibitors from bovine spleen: preparation of specific antibodies.Prep. Biochem. 15, 211–19
FIORETTI, E., IACOPINO, G., ANGELETTI, M., BARRA, D., BOSSA, F., & ASCOLI, F. (1985b) Primary structure and antiproteolytic activity of a Kunitz type inhibitor from bovine spleen.J. Biol. Chem. 260, 11451–5.
FIORETTI, E., ANGELETTI, M., FIORUCCI, L., BARRA, D., BOSSA, F., & ASCOLI, F. (1987) Aprotinin-like isoinhibitors in bovine organs.Biol. Chem. Hoppe Seyler (in press).
FIORETTI, E., ANGELETTI, M., PASSERI, D. & ASCOLI, F. (1988) Interaction between leukocytic elastase and Kunitz-type inhibitors from bovine spleen.J. Protein Chem. (in press).
FRITZ, H. & KRUCK, J. (1979) Immunofluorescence studies indicate that the basic trypsin-kallikrein-inhibitor of bovine organs (Trasylol) originates from mast cells.Hoppe-Seyler's Z. Physiol. Chem. 360, 437–44.
FRITZ, H. & WUNDERER, G. (1983) Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs.Drug Res. 33, 479–94.
KINGSTON, I. B., ANDERSON, S. (1986) Sequences encoding two trypsin inhibitors occur in strikingly similar genomic environments.Biochem. J. 233, 443–50.
ONDETTI, M. A. & CUSHMAN, D. W. (1982) Enzymes of the renin—angiotensin system and their inhibitors.Ann. Rev. Biochem. 51, 283–308
STEVENS, R. L., KATZ, H. R., SELDIN, D. C. & AUSTEN, K. F. (1985) Biochemical characteristics distinguish subclasses of mammalian mast cells. InMast Cell Heterogeneity, (edited by BEFUS, A. D., BIENENSTOCK, J. and DENBURG, J.)., New York: Raven Press.
VIRCA, G. D. & SCHNEBLI, H. P. (1984) The Elastaseα-1-proteinase inhibitor balance in the lung: a review.Schweiz. Med. Wochenschr. 114, 895–8.
WENZEL, H. R., BECKMANN, J., MEHLICH, A., SIEKMANN, J., TSCHESCHE, H., & SCHUTT, H. (1985) Potentials of high-performance ion-exchange chromatography in protein separations. InModern Methods in Protein Chemistry. Vol 2. (edited by TSCHESCHE, H.) pp. 173–84.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Businaro, R., Fioretti, E., Fumagalli, L. et al. Cellular localization of bovine pancreatic trypsin inhibitor and related molecular forms in bovine lung. Histochem J 20, 187–193 (1988). https://doi.org/10.1007/BF01747462
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF01747462