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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-4278

Rindler, M J; Xu, C-F; Gumper, I; Cen, C; Sonderegger, P; Neubert, T A (2008). Calsyntenins are secretory granule proteins in anterior pituitary gland and pancreatic islet alpha cells. Journal of Histochemistry and Cytochemistry, 56(4):381-388.

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Abstract

Calsyntenins are members of the cadherin superfamily of cell adhesion molecules. They are present in postsynaptic 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 colocalized with follicle-stimulating hormone in secretory granules. In 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. Results indicate that calsyntenins function outside the nervous system and potentially are modulators of endocrine function.

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Biochemistry
07 Faculty of Science > Institute of Biochemistry
DDC:570 Life sciences; biology
Uncontrolled Keywords:pituitary gland • pancreas • calsyntenin • secretory granules • follicle-stimulating hormone • glucagon • insulin • growth hormone • prolactin
Language:English
Date:April 2008
Deposited On:27 Oct 2008 09:39
Last Modified:28 Nov 2013 01:04
Publisher:Sage Publications
ISSN:0022-1554
Publisher DOI:10.1369/jhc.7A7351.2007
Official URL:http://www.jhc.org/cgi/content/abstract/56/4/381
PubMed ID:18158283
Citations:Web of Science®. Times Cited: 2
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