Connexin36 localization to pinealocytes in the pineal gland of mouse and rat
| Autor: | Kimberly G. Vanderpool, S. G. Wang, Thomas Yasumura, Deborah D. Tsao, James I. Nagy, John E. Rash |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Male Pathology medicine.medical_specialty genetic structures Connexin Biology Immunofluorescence Cell junction Pineal Gland Connexins Article Pinealocyte Rats Sprague-Dawley 03 medical and health sciences Pineal gland Mice 0302 clinical medicine medicine Animals medicine.diagnostic_test General Neuroscience Gap junction Gap Junctions Immunogold labelling Cell biology Rats Mice Inbred C57BL 030104 developmental biology medicine.anatomical_structure Reticular connective tissue sense organs 030217 neurology & neurosurgery |
| Zdroj: | The European journal of neuroscience. 45(12) |
| ISSN: | 1460-9568 |
| Popis: | Several cell types in the pineal gland are known to establish intercellular gap junctions, but the connexin constituents of those junctions have not been fully characterized. Specifically, the expression of connexin36 (Cx36) protein and mRNA has been examined in the pineal, but the identity of cells that produce Cx36 and that form Cx36-containing gap junctions has not been determined. We used immunofluorescence and freeze fracture replica immunogold labelling (FRIL) of Cx36 to investigate the cellular and subcellular localization of Cx36 in the pineal gland of adult mouse and rat. Immunofluorescence labelling of Cx36 was visualized exclusively as puncta or short immunopositive strands that were distributed throughout the pineal, and which were absent in pineal sections from Cx36 null mice. By double immunofluorescence labelling, Cx36 was localized to tryptophan hydroxylase-positive and 5-hydroxytryptamine-positive pinealocyte cell bodies and their large initial processes, including at intersections of those processes and at sites displaying a confluence of processes. Labelling for the cell junction marker zonula occludens-1 (ZO-1) either overlapped or was closely associated with labelling for Cx36. Pinealocytes thus form Cx36-containing gap junctions that also incorporate the scaffolding protein ZO-1. FRIL revealed labelling of Cx36 at ultrastructurally defined gap junctions between pinealocytes, most of which was at gap junctions having reticular, ribbon or string configurations. The results suggest that the endocrine functions of pinealocytes and their secretion of melatonin is supported by their intercellular communication via Cx36-containing gap junctions, which may now be tested by the use of Cx36 null mice. |
| Databáze: | OpenAIRE |
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