Skip to main content
SpringerLink
Log in

Untersuchungen über Muster und Verteilung von Enzymen in der Schleimhaut des menschlichen Gastrointestinaltraktes

II. Mitteilung Histochemische und ergänzende Isoenzymuntersuchungen

  • Originalien
  • Published:
Klinische Wochenschrift Aims and scope Submit manuscript

Zusammenfassung

An Gefrierschnitten von bioptisch und chirurgisch gewonnener Schleimhaut des Magens, Duodenum, Jejunum und Rectum wurde histochemisch die Verteilung von unspezifischer Esterase, alkalischer Phosphatase, Adenosintriphosphatase, Leucinaminopeptidase, Disaccharidasen, saurer Phosphatase, Lactatdehydrogenase, Succinodehydrogenase und Thiaminpyrophosphatase untersucht. Der Dünndarm als resorptiv aktivster Abschnitt des Magen-Darmkanals war gegenüber Magen und Rectum durch das zusätzliche und spezifische Vorkommen von Leucinaminopeptidase, alkalischer Phosphatase und Disaccharidasen ausgezeichnet. Die intraepitheliale Fermentverteilung ergab durch die Assoziation einiger der dargestellten Enzyme mit Cytoplasmaorganellen charakteristische Besonderheiten. Die dündarmspezifischen Fermente fanden sich z.B. nur im Bereich der Zotten (nicht der Krypten) und hier wiederum im iepthelialen Bürstensaumbesatz, der unmittelbaren Kontaktstelle des Zottenepithels mit dem Chymus. Im Gegensatz zu den Disaccharidasen und der Leucinaminopeptidase ist die funktionelle Bedeutung der intestinalen alkalischen Phosphatase bei der Resorption der drei Hauptnahrungsbestandteile nicht ohne weiteres ersichtlich. Ihre vonFishman beschriebene Eigenschaft durch l-phenylalanin gehemmt zu werden, gestattet die Abgrenzung der Darmphosphatase von alkalischen Phosphatasen anderer Gewebe. Durch elektrophoretische Trennung von Jejunumhomogenaten in Acrylamidgel ließ sich die Dünndarmphosphatase in drei Komponenten fraktionieren, die alle mit l-phenylalanin gehemmt werden konnten. Die intensivste dieser drei Phosphatasefraktionen war im Chylus des Ductus thoracicus elektrophoretisch identifizierbar und trat auch im Serum unter oraler Fettbelastung vorübergehend auf. Daraus wird auf die Mitwirkung der alkalischen Dünndarmphosphatase bei der enteralen Fettresorption geschlossen.

Summary

Cryostat sections of bioptically and surgically obtained mucosa of stomach, duodenum, jejunum and rectum were stained histochemically to determine the distribution of non specific esterase, alkaline phosphatase, adenosine triphosphatase, leucine aminopeptidase, disaccharidases, acid phosphatase, lactic dehydrogenase, succinodehydrogenase and thiamine pyrophosphatase. Compared with stomach and rectum the small intestine as functionally most active part of the entire gut was characterized by additionally and specifically demonstrable leucine aminopeptidase, alkaline phosphatase and disaccharidases. The intraepithelial enzyme distribution showed particular features by association with cytoplasmic organells. The enzymes specific for the small intestine were found for example in the area of the villi and here only in the epithelial brush border, the immediate site of contact to the chymus. Contrary to the disaccharidases and the leucine amino-peptidase the functional meaning of the alkaline phosphatase during the absorption of the three main components of the diet ist not evident a priori. The inhibitory action of l-phenylalanine on intestinal alkaline phosphatase described byFischman permits its distinction from alkaline phosphatases of other tissues. In the present investigation the intestinal phosphatase from homogenates of the jejunum was separated electrophoretically in acrylamide gel in three fractions, which could all be inhibited by l-phenylalanine. The most intense of these fractions was identified electrophoretically also in the chylus of the thoracic duct. This fraction was also transitory demonstrable in serum after an oral fat load. Therefore the participation of the intestinal alkaline phosphatase in fat absorption is concluded.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Literatur

  1. Barka, T., andP. J. Anderson: Histochemical methods for acid phosphatase using hexazonium pararosanilin as coupler. J. Histochem. Cytochem10, 741–753 (1962).

    Google Scholar 

  2. Bolt, R. J., H. M. Pollard, andS. McCool: Staining of enzymes in mucosa of the small bowel, using a peroral biopsy tube. Amer. J. clin. Path.34, 43–49 (1960).

    Google Scholar 

  3. Boyer, S. H.: Human organ alkaline phosphatase, discrimination by serveral means including starch gel electrophoresis, of antienzyme-enzyme supernatant fluids. Ann. N. Y. Acad. Sci.103, 938–950 (1963).

    Google Scholar 

  4. Celle, G., M. Dodero eR. Cheli: Le esterasi specifiche della mucosa digiunale nella norma e nella sprue non tropicale. Minerva gastroent.9, 116–119 (1963);

    Google Scholar 

  5. Le fosfomonoesterasi della mucosa digiunale nella norma e nella sprue non tropicale. Minerva gastroent.9, 119–123 (1963).

    Google Scholar 

  6. Correira, J. P., M. I. Filipe, andJ. C. Santos: Histochemistry of the gastric mucosa. Gut4, 68–76 (1963).

    Google Scholar 

  7. Crane, R. K.: Enzymes and malabsorption: A concept of brush border membrane disease. Gastroenterology50, 254–262 (1966).

    Google Scholar 

  8. Dahlqvist, H., andA. Brun: A method for the histochemical demonstration of disacchardiase activities: application to invertase and trehalase in some animal tissues. J. Histochem. Cytochem.10, 294–302 (1962).

    Google Scholar 

  9. Dawson, J., andJ. Pryse-Davies: The distribution of certain enzyme systems in the normal human gastrointestinal tract. Gastroenterology44, 745–760 (1963).

    Google Scholar 

  10. Fishman, W. H., S. Green, andN. I. Inglis: l-phenylalanine: an organ specific, stereospecific inhibitor of human intestinal alkaline phosphatase. Nature (Lond.)198, 685–686 (1963).

    Google Scholar 

  11. Frić, Pr., andZd. Lojda: Enzymes of the human jejunal mucosa. Acta gastro-ent. belg.27, 526–530 (1964).

    Google Scholar 

  12. Foldfischer, S., E. Essner, andA. B. Novikoff: The localization of phosphatase activities at the level of ultrastructure. J. Histochem. Cytochem.12, 72–95 (1964).

    Google Scholar 

  13. Gomori, G.: Microscopic histochemistry, principles and practice. Chicago: Chicago University Press 1952.

    Google Scholar 

  14. Heinkel, K., u.N. Henning: Die Probe-excision aus dem Rectum und der Mundhöhle durch Saugbiopsie. Münch. med. Wschr.1955, 1182.

  15. Isselbacher, K. J.: Metabolism and transport of lipid by intestinal mucosa. Fed. Proc.24, 16–22 (1965).

    Google Scholar 

  16. Keiding, N. P.: The alkaline phosphatase fractions of human lymph. Clin. Sci.26, 291–297 (1964).

    Google Scholar 

  17. Klein, U. E.: Zur Organspezifität multipler alkalischer Serumphosphatasen. Gastroenterologia (Basel) (1966) (im Druck).

  18. Klein, U. E., H. Löffler u.E. Leuckfeld: Elektrophoretische Trennung von Milchsäuredehydrogenaseisoenzymen, unspezifischen Esterasen u. alkalischen Phosphatasen aus menschlichen Blutzellen. Klin. Wschr.44, 637–640 (1966).

    Google Scholar 

  19. Klein, U. E., H. CH. Drube, H. Th. Hansen u.F. Mielke: Untersuchungen über Muster und Verteilung von Enzymen in der Schleimhaut des menschlichen Gastrointestinaltraktes. III. Mitt. Elektrophoretische Isoenzymuntersuchung. In Vorbereitung.

  20. Kotzaurek, R., u.B. Schobel: Das Verhalten der alkalischen Phosphataseaktivitäten im menschlichen Serum bei Skelettund Leber-Gallenwegserkrankungen. Klin. Wschr.41, 956–961 (1963).

    Google Scholar 

  21. Krisher, J. H., V. A. Close, andW. H. Fishman: Identification by means of l-phenylalanine inhibition of intestinal alkaline phosphatase components separated by starch gel electrophoresis of serum. Clin. chim. Acta11, 122–127 (1965).

    Google Scholar 

  22. Langr, F., J. Pařízek, M. Hradskýn u.V. Vortel: Die Aktivität der Esterase, der alkalischen Phosphatase und Aminopeptidase in der Magenschleimhaut bei einigen praecanzerösen Zuständen. Gastroenterologia (Basel)104, 213–224 (1965).

    Google Scholar 

  23. Lazarus, S., andB. J. Wallace: Nucleoside phosphatase and thiamine pyrophosphatase activity of rabbit golgiapparatus. J. Histochem. Cytochem.12, 729–736 (1964).

    Google Scholar 

  24. Leblond, C. P., andB. Messier: Reneval of chief cells and goblet cells in the small intestine as shown by radioautography after injection of thymidine-H3 into mice. Anat. Rec.132, 247–260 (1958).

    Google Scholar 

  25. Lojda, Z.: Some remarks concerning the histochemical detection of disaccharidases and glucosidases. Histochemie5, 339–360 (1965).

    Google Scholar 

  26. Lojda, Z., andP. Frić: Enzymes of the jejunal enterochromaffine cells in man. Histochemie3, 455–461 (1964).

    Google Scholar 

  27. Markert, C. L., andF. Möller: Multiple forms of enzymes: tissue, ontogenetic and species specific patterns Proc. nat. Acad. Sci. (Wash.)45, 753–763 (1959).

    Google Scholar 

  28. Markert, C. L., andH. Ursprung: The ontogeny of isozyme patterns of lactate dehydrogenase in the mouse. Develop. Biol.5, 363–381 (1962).

    Google Scholar 

  29. McMinn, R. M., andL. Fry: Diarrhoea of small bowel origin, cytology and cytochemistry of intestinal biopsies. Proc. roy. Soc. Med.56, 1078–1079 (1963).

    Google Scholar 

  30. Melnik, P. J., andS. H. Lawrence: Histochemical enzyme technics applied to starch gel electrophoresis. Ann. Histochem.6, 511–518 (1961).

    Google Scholar 

  31. Mendeloff, A. J., andB. Monis: Histochemical study of 3 dehydrogenase systems in ulcerative colitis biopsy specimens. Gastroenterology43, 669–674 (1962).

    Google Scholar 

  32. Monis, B., andA. J. Mendeloff: Studies in ulcerative colitis, TPN-linked dehydrogenases and nonspecific esterase in rectal biopsy specimens. Gastroenterology48, 173–184 (1965).

    Google Scholar 

  33. Moss, D. W.: Properties of alkaline phosphatase fractions in extracts of human small intestine. Biochem. J.94, 458–562 (1965).

    Google Scholar 

  34. Novikoff, A. B.: Biochemical and staining reactions of cytoplasmic constituents. In: Developing cell systems and their control (D. Rudnick, ed.), p. 167–203. New York: Ronald Press 1960.

    Google Scholar 

  35. Novikoff, A. B., andE. Essner: Pathological changes in cytoplasmic organells. Fed. Proc.21, 1130–1142 (1962).

    Google Scholar 

  36. Novikoff, A. B., andS. Goldfischer: Nucleoside-diphosphatase activity in the golgi apparatus and it's usefullnes for cytological studies. Proc. nat. Acad. Sci. (Wash.)47, 802–810 (1961).

    Google Scholar 

  37. Padykula, H. A.: Recent functional interpretations of intestinal morphology. Fed. Proc.21, 873–879 (1962).

    Google Scholar 

  38. Pearse, A. G. E.: Histochemistry, theoretical and applied, p. 910. London: J. A. Churchil LTD 1961.

    Google Scholar 

  39. Planteydt, H. T., andR. G. J. Willighagen: Enzyme histochemistry of the human stomach with special reference to intestinal metaplasia. J. Path. Bact.80, 317–324 (1960).

    Google Scholar 

  40. Planteydt, H. T., andR. G. J. Willighagen: Enzyme histochemistry of gastric carcinoma. J. Path. Bact.90, 393–398 (1965).

    Google Scholar 

  41. Plosscowe, R. P., G. G. Berg, andH. L. Segal: Enzyme histochemical studies of human gastric and jejunal biopsy specimens in normal and disease states. Amer. J. dig. Dis.8, 311–318 (1963).

    Google Scholar 

  42. Pryse-Davies, J., andI. M. P. Dawson: Some observations on the enzyme histochemistry of the small intestine in human malabsorption states, with some experimental studies on the effect of neomycin in rats. Acta gastro-ent. belg.27, 537–542 (1964).

    Google Scholar 

  43. Ragins, H., andM. Dittbrenner: Intracellular enzymatic histochemistry of the human stomach with special reference to atrophic gastritis. Gut6, 357–363 (1965).

    Google Scholar 

  44. Ragins, H., M. Dittbrenner, andJ. Diaz: Comparative histochemistry of the gastric mucosa: A survey of the common laboratory animals and man. Anat. Rec.150, 179–194 (1964).

    Google Scholar 

  45. Raymond, S., andY.-J. Wang: Preparation and properties of acrylamide gel for use in electrophoresis. Analyt. Biochem.1, 391–396 (1960).

    Google Scholar 

  46. Riecken, E. O., R. H. Dowling, C. C. Both, andA. G. E. Pearse: Histochemical changes in the rat small intestine associated with enhanced absorption after high bulk feeding: Enzymol. biol. clin.5, 231–244 (1965).

    Google Scholar 

  47. Samloff, I. M., J. S. Davis, andE. A. Schenk: A clinical and histochemical study of celiac disease before and during a gluten free diet. Gastroenterology48, 155–172 (1965).

    Google Scholar 

  48. Schobel, B., u.F. Wewelka: Die Heterogenität der Leucinaminopeptidase. Klin. Wschr.40, 1048–1056 (1962).

    Google Scholar 

  49. Shnitka, Th.: Enzymatic histochemistry of gastrointestinal mucous membrane. Fed. Proc.19, 897–906 (1960).

    Google Scholar 

  50. Sielaff, H. J.: Die Bedeutung der bioptischen Untersuchung des Intestinal-traktes für die Diagnose und Therapie intestinaler Störungen. Internist (Berl.)2, 479–489 (1961).

    Google Scholar 

  51. Spiro, H. M., M. I. Filipe, J. S. Stewart, C. C. Booth, andA. G. E. Pearse: Functional histochemistry of the small bowel mucosa in malabsorptive syndromes. Gut5, 145–154 (1964).

    Google Scholar 

  52. Taswell, H. F., andD. M. Jeffers: Isoenzymes of serum alkaline phosphatase in hepatobiliary and skeletal disease. Amer. J. clin. Path.40, 349–356 (1963).

    Google Scholar 

  53. Teodori, U., etP. Gentilini: Histochimie enzymatique de la muqueuse gastrique dans certaines conditions pathologiques. Gastroenterologia (Basel)103, 351–358 (1965).

    Google Scholar 

  54. Wachstein, M., andF. Meisel: Histochemistry of hepatic phosphatases at a physiologic pH with special reference to the demonstration of bile canaliculi. Amer. J. clin. Path.27, 13–23 (1957).

    Google Scholar 

  55. Watanabe, K., andW. H. Fishman: Application of the stereospecific inhibitor l-phenylalanine to the enzyme morphology of intestinal alkaline phosphatase. J. Histochem. Cytochem.12, 252–260 (1964).

    Google Scholar 

  56. Wattenberg, L. W.: Histochemical study of aminopeptidase in metaplasia and carcinoma of the stomach. Arch. Path.67, 281–286 (1959).

    Google Scholar 

  57. Wieland, Th., u.G. Pfleiderer: Differente und multiple Formen von Enzymen. Angew. Chem.74, 261–270 (1962).

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Medizinische Universitätsklinik Kiel, Germany

    U. E. Klein, H. Chr Drube & H. Th. Hansen

Authors
  1. U. E. Klein
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. H. Chr Drube
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. H. Th. Hansen
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Mit Unterstützung der Deutschen Forschungsgemeinschaft.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Klein, U.E., Drube, H.C. & Hansen, H.T. Untersuchungen über Muster und Verteilung von Enzymen in der Schleimhaut des menschlichen Gastrointestinaltraktes. Klin Wochenschr 45, 95–101 (1967). https://doi.org/10.1007/BF01747971

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01747971

Search

Navigation