Skip to main content
Log in

Synaptophysin immunoreactivity in the mammalian endocrine pancreas

  • Published:
Cell and Tissue Research Aims and scope Submit manuscript

Summary

Synaptophysin, a major membrane glycoprotein of small presynaptic vesicles in neurons, has also been found in microvesicles of endocrine cells, e.g., of the endocrine pancreas. In the present study, the endocrine pancreas in 9 mammalian species (man, dog, mink, bovine, rabbit, guinea pig, rat, mouse, gerbil) has been investigated immunohistochemically for synaptophysin immunoreactivity. Synaptophysin-positive cells have been identified and localized on semithin plastic sections. Our study demonstrates that, in all species examined, all pancreatic endocrine cell types are consistently synaptophysin-positive independent of their location within the tissue, or the conditions of tissue processing. In addition, a few cells that cannot be hormonally identified show synaptophysin immunoreactivity. Hence, synaptophysin appears to be a regular constituent of all pancreatic endocrine cells in mammals. In several species, a subpopulation of endocrine cells, consisting of glucagon-containing and/or pancreatic-polypeptide-containing cells, exhibits a significantly higher degree of synaptophysin immunoreactivity. In the gerbil, this heterogeneity can readily be detected from the day of birth onwards. Our findings indicate that closely related endocrine cell types may differ with respect to the content of synaptophysin.

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

Access this article

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

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Buffa R, Rindi G, Sessa F, Gini A, Capella C, Jahn R, Navone F, De Camilli P, Solcia E (1988) Synaptophysin immunoreactivity and small clear vesicles in neuroendocrine cells and related tumours. Mol Cell Probes 2:367–381

    Google Scholar 

  • Cowan D, Linial M, Scheller RH (1990) Torpedo synaptophysin: evolution of a synaptic vesicle protein. Brain Res 509:1–7

    Google Scholar 

  • Culter DF, Cramer LP (1990) Sorting during transport to the surface of PC12 cells: divergence of synaptic vesicle and secretory granule proteins. J Cell Biol 110:721–730

    Google Scholar 

  • De Camilli P, Navone F (1987) Regulated secretory pathways of neurons and their relation to the secretory pathway of endocrine cells. Ann NY Acad Sci 493:461–479

    Google Scholar 

  • Fischer von Mollard G, Mignery GA, Baumert M, Perin MS, Hason TJ, Burger PM, Jahn R, Südhof TC (1990) Rab 3 is a small GTP-binding protein exclusively localized to synaptic vesicles. Proc Natl Acad Sci USA 87:1988–1992

    Google Scholar 

  • Grube D (1980) Immunoreactivities of gastrin (G-) cells. II. Non-specific binding of immunoglobulins to G-cells by ionic interactions. Histochemistry 66:149–167

    Google Scholar 

  • Grube D, Bohn R (1983) The microanatomy of human islets of Langerhans with special reference to somatostatin (D-) cells. Arch Histol Jpn 46:327–353

    Google Scholar 

  • Grube D, Kusumoto Y (1986) Serial semithin sections in immunohistochemistry: techniques and applications. Arch Histol Jpn 49:391–410

    Google Scholar 

  • Grube D, Eckert I, Speck PT, Wagner H-J (1983) Immunohistochemistry and microanatomy of the islets of Langerhans. Biomed Res 4 [Suppl]:25–36

    Google Scholar 

  • Grube D, Aunis D, Bader F, Cetin Y, Jörns A, Yoshie S (1986) Chromogranin A (CGA) in the gastro-entero-pancreatic (GEP) endocrine system. I. CGA in the mammalian endocrine pancreas. Histochemistry 85:441–452

    Google Scholar 

  • Haimoto H, Takahashi Y, Koshikawa T, Nagura H, Kato K (1985) Immunohistochemical localization of γ-enolase in normal human tissues other than nervous and neuroendocrine tissues. Lab Invest 52:257–263

    Google Scholar 

  • Hoog A, Gould VE, Grimelius L, Franke WW, Falkmer S, Chejfec G (1988) Tissue fixation methods alter the immunohistochemical demonstrability of synaptophysin. Ultrastruct Pathol 12:673–678

    Google Scholar 

  • Hsu SM, Raine L, Fanger H (1981) Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques. A comparison between ABC and unlabeled antibody (PAP) procedures. J Histochem Cytochem 29:577–580

    Google Scholar 

  • Jahn R, Schiebler W, Ouimet C, Greengard P (1985) A 38000-dalton membrane protein (p38) present in synaptic vesicles. Proc Natl Acad Sci USA 82:4137–4141

    Google Scholar 

  • Johnston PA, Cameron PL, Stukenbrok H, Jahn R, DeCamilli P, Südhof TC (1989a) Synaptophysin is targeted to similar microvesicles in CHO and PC12 cells. EMBO J 8:2863–2872

    Google Scholar 

  • Johnston PA, Jahn R, Südhof TC (1989b) Transmembrane topography and evolutionary conservation of synaptophysin. J Biol Chem 264:1268–1273

    Google Scholar 

  • Klöppel G, Lenzen S (1984) Anatomy and physiology of the endocrine pancreas. In: Klöppel G, Heitz PU (eds) Pancreatic pathology. Churchill Livingstone, Edinburg, pp 133–153

    Google Scholar 

  • Lowe AW, Madeddu L, Kelly RB (1988) Endocrine secretory granules and neuronal synaptic vesicles have three integral membrane proteins in common. J Cell Biol 106:51–59

    Google Scholar 

  • Navone F, Jahn R, DiGioia G, Stukenbrok H, Greengard P, DeCamilli P (1986) Protein p 38: an integral membrane protein specific for small vesicles of neurons and neuroendocrine cells. J Cell Biol 103:2511–2527

    Google Scholar 

  • Obendorf D, Schwarzenbrunner U, Fischer-Colbrie R, Laslop A, Winkler H (1988) In adrenal medulla synaptophysin (protein p38) is present in chromaffin granules and in a special vesicle population. J Neurochem 51:1573–1580

    Google Scholar 

  • Redecker P, Grube D, Jahn R (1990) Immunohistochemical localization of synaptophysin (p38) in the pineal gland of the Mongolian gerbil (Meriones unguiculatus). Anat Embryol 181:433–440

    Google Scholar 

  • Schilling K, Gratzl M (1988) Quantification of p38/synaptophysin in highly purified adrenal medullary chromaffin vesicles. FEBS Lett 233:22–24

    Google Scholar 

  • Schilling K, Blanco Barco R, Rhinehart D, Pilgrim C (1989) Expression of synaptophysin and neuron-specific enolase during neuronal differentiation in vitro: effects of dimethyl sulfoxide. J Neurosci Res 24:347–354

    Google Scholar 

  • Sternberger LA (1986) Immunocytochemistry, 3rd edn. Wiley, New York

    Google Scholar 

  • Wiedemann B, Franke WW (1985) Identification and localization of synaptophysin, an integral membrane glycoprotein of M 38000 characteristic of presynaptic vesicles. Cell 41:1017–1028

    Google Scholar 

  • Wiedenmann B, Huttner WB (1989) Synaptophysin and chromogranins/secretogranins — widespread constituents of distinct types of neuroendocrine vesicles and new tools in tumor diagnosis. Virchows Arch [B] 58:95–121

    Google Scholar 

  • Wiedenmann B, Franke WW, Kuhn C, Moll R, Gould VE (1986) Synaptophysin: a marker protein for neuroendocrine cells and neoplasms. Proc Natl Acad Sci USA 83:3500–3504

    Google Scholar 

  • Wiedenmann B, Waldherr R, Buhr H, Hille A, Rosa P, Huttner WB (1988) Identification of gastroenteropancreatic neuroendocrine cells in normal and neoplastic human tissue with antibodies against synaptophysin, chromogranin A, secretogranin I (chromogranin B), and secretogranin II. Gastroenterology 95:1364–1374

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Redecker, P., Jörns, A., Jahn, R. et al. Synaptophysin immunoreactivity in the mammalian endocrine pancreas. Cell Tissue Res 264, 461–467 (1991). https://doi.org/10.1007/BF00319036

Download citation

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00319036

Key words

Navigation