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Calsyntenins Are Secretory Granule Proteins in Anterior Pituitary Gland and Pancreatic Islet Cells

Michael J. Rindler, Chong-feng Xu, Iwona Gumper, Chuan Cen, Peter Sonderegger and Thomas A. Neubert

Departments of Cell Biology (MJR,IG) and Pharmacology and Kimmel Center for Biology and Medicine, Skirball Institute (CX,TAN), New York University School of Medicine, New York, New York, and Department of Biochemistry, University of Zurich, Zurich, Switzerland (CC,PS)

Correspondence to: Michael Rindler, PhD, Associate Professor, Department of Cell Biology, New York University School of Medicine, 550 First Avenue, New York, NY 10016. E-mail: rindlm01{at}med.nyu.edu

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 cells in the pancreatic islets of Langerhans. Results indicate that calsyntenins function outside the nervous system and potentially are modulators of endocrine function. (J Histochem Cytochem 56:381–388, 2008)

Key Words: pituitary gland • pancreas • calsyntenin • secretory granules • follicle-stimulating hormone • glucagon • insulin • growth hormone • prolactin

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