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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.
- 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