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A non-receptor-type protein phosphotyrosine phosphatase is enriched in secretory vesicles of glucagon – and pancreatic polypeptide – secreting cells of the endocrine pancreas.

Authors :
Wimmer, M.
Tag, Claudia
Hofer, H. Werner
Source :
Histochemistry & Cell Biology; Jan1999, Vol. 111 Issue 2, p135-142, 8p
Publication Year :
1999

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
09486143
Volume :
111
Issue :
2
Database :
Complementary Index
Journal :
Histochemistry & Cell Biology
Publication Type :
Academic Journal
Accession number :
50144956
Full Text :
https://doi.org/10.1007/s004180050343