Calsyntenins Are Secretory Granule Proteins in Anterior Pituitary Gland and Pancreatic Islet Alpha Cells
Michael J. Rindler 1*, Chong-feng Xu 1, Iwona Gumper 1, Chuan Cen 1, Peter Sonderegger 1 and Thomas A. Neubert 1
1 Departments of Cell Biology (MJR,IG) and Pharmacology and Kimmel Center for Biology and Medicine of the Skirball Institute (C-FX,TAN), New York University School of Medicine, New York, New York, and Department of Biochemistry, University of Zurich, Zurich, Switzerland (CC,PS)
* To whom correspondence should be addressed. E-mail: rindlm01{at}med.nyu.edu.
Submitted on September 5, 2007
Accepted on 30 November 2007
 |
Abstract |
|---|
Calsyntenins are members of the cadherin superfamily of cell adhesion molecules. They are present in post-synaptic membranes of excitatory neurons and in vesicles in transit to neuronal growth cones. In the current study, calsyntenin-1 (CST-1) and calsyntenin-3 (CST-3) were identified by mass spectrometric analysis (LC-MS/MS) of integral membrane proteins from highly enriched secretory granule preparations from bovine anterior pituitary gland. Immunofluorescence microscopy on thin frozen sections of rat pituitary revealed that CST-1 was present only in gonadotropes where it co-localized with follicle stimulating hormone (FSH) in secretory granules. By contrast, CST-3 was present not only in gonadotrope secretory granules but also in those of somatotropes and thyrotropes. Neither protein was detected in mammatropes. In addition, CST-1 was also localized to the glucagon-containing secretory granules of alpha cells in the pancreatic islets of Langerhans. The results indicate that calsyntenins function outside the nervous system and potentially are modulators of endocrine function.
Key Words:
pituitary gland, pancreas, calsyntenin, secretory granules, FSH, LH, glucagon, insulin, growth hormone, prolactin