Expression of synaptic vesicle trafficking proteins in the developing rat pineal gland.
Adult mammalian pinealocytes contain several synaptic membrane proteins that are probably involved in the regulation of targeting and exocytosis of synaptic-like microvesicles (SLMVs). Immunohistochemical techniques have now demonstrated the spatiotemporal expression pattern of some of these proteins during rat pineal ontogenesis. Various synaptic vesicle trafficking proteins are detectable in proliferating epithelial cells of the pineal anlage even at embryonic day 17.5 (E 17.5), with the exception of syntaxin I (weakly expressed from E 19.5) and dynamin I (whose levels increase markedly during the first postnatal week). Numerous cells exhibiting strong immunoreactivity for synaptobrevin II, SNAP-25, synaptophysin, and munc-18-1 are distributed throughout the increasingly compact gland at E 19.5 and E 20.5; however, their number declines toward the proximal deep part of the organ. Groups of postmitotic cells situated at the surface of the developing gland exhibit marked immunoreactivity for the aforementioned proteins and lie close to the laminin-immunoreactive outer limiting basement membrane or to its remnants in regions of basement membrane dissolution. We also show that synthesis of vimentin and S-antigen seems to begin earlier during pineal development than previously recognized. Thus, synaptic vesicle trafficking proteins are the earliest molecular markers of pinealocyte differentiation known to date, being expressed well before the onset of rhythmic hormone secretion in the pineal gland, where they may play a role in morphogenetic events. Components of the extracellular matrix such as laminin may be critically involved in the upregulation of synaptic membrane protein expression. The dynamin immunostaining pattern indicates that SLMVs of pinealocytes begin to undergo regulated cycles of exo/endocytosis during postnatal week 1.
Redecker
P
P
Medizinische Hochschule Hannover, Abt. Anatomie 1, Germany. redecker.peter@mh-hannover.de
D000818:Animals; D000954:Antigens, Surface / Q000276:immunology / Q000378:metabolism; D034284:Dynamin I; D034281:Dynamins; D020558:GTP Phosphohydrolases / Q000276:immunology / Q000378:metabolism; D007150:Immunohistochemistry; D008565:Membrane Proteins / Q000276:immunology / Q000378:metabolism; D051938:Munc18 Proteins; D009419:Nerve Tissue Proteins / Q000276:immunology / Q000378:metabolism*; D010870:Pineal Gland / Q000166:cytology / Q000196:embryology* / Q000254:growth & development / Q000378:metabolism*; D050683:R-SNARE Proteins; D051381:Rats; D017208:Rats, Wistar; D013572:Synaptic Vesicles / Q000378:metabolism*; D016708:Synaptophysin / Q000276:immunology / Q000378:metabolism; D050825:Synaptosomal-Associated Protein 25; D050827:Syntaxin 1; D033921:Vesicular Transport Proteins; D014746:Vimentin / Q000276:immunology / Q000378:metabolism
D000954:Antigens, Surface; D008565:Membrane Proteins; D051938:Munc18 Proteins; D009419:Nerve Tissue Proteins; D050683:R-SNARE Proteins; C494210:Snap25 protein, rat; C497939:Stxbp1 protein, rat; D016708:Synaptophysin; D050825:Synaptosomal-Associated Protein 25; D050827:Syntaxin 1; D033921:Vesicular Transport Proteins; D014746:Vimentin; D034284:Dynamin I; D020558:GTP Phosphohydrolases; D034281:Dynamins