Journalartikel
Autorenliste: Wimmer, M; Tag, C; Hofer, HW
Jahr der Veröffentlichung: 1999
Seiten: 135-142
Zeitschrift: Histochemistry and Cell Biology
Bandnummer: 111
Heftnummer: 2
ISSN: 0301-5564
DOI Link: https://doi.org/10.1007/s004180050343
Verlag: Springer
Abstract:
The secretory vesicles of some cells of the islets of Langerhans of the pancreas contain high amounts of immunoreactive tyrosine phosphatase of the PTP1B/TCPTP subfamily. The cells are located in the peripheral parts of the islets and were identified as glucagon- and pancreatic polypeptide-forming cells. The tyrosine phosphatase is also enriched in some of the somatostatin-producing cells but is not elevated either in insulin-producing B-cells or in the exocrine pancreas. Virtually the same patterns were found in pancretic tissues of rats, guinea pigs, pigs, and mice. High levels of detergent-soluble tyrosine phosphatase were measured in the particular fraction of pancreatic islets with a substrate preferred by PTP1B/TCPTP-type protein tyrosine phosphatases.
Zitierstile
Harvard-Zitierstil: Wimmer, M., Tag, C. and Hofer, H. (1999) A non-receptor-type protein phosphotyrosine phosphatase is enriched in secretory vesicles of glucagon - and pancreatic polypeptide - secreting cells of the endocrine pancreas, Histochemistry and Cell Biology, 111(2), pp. 135-142. https://doi.org/10.1007/s004180050343
APA-Zitierstil: Wimmer, M., Tag, C., & Hofer, H. (1999). A non-receptor-type protein phosphotyrosine phosphatase is enriched in secretory vesicles of glucagon - and pancreatic polypeptide - secreting cells of the endocrine pancreas. Histochemistry and Cell Biology. 111(2), 135-142. https://doi.org/10.1007/s004180050343
Schlagwörter
AMYLASE SECRETION; AUTOANTIGEN; endocrine secretion; HOMOLOG; PHOGRIN; RAT PANCREAS; tyrosine phosphatase; TYROSINE-PHOSPHATASE