Somatostatin (SRIF) and SRIF receptors in the mouse retina.
In the retina, somatostatin (SRIF) acts as a neuromodulator by interacting with specific SRIF subtype (sst) receptors. The aim of this study was to detect mRNAs for sst(1-5) receptors by semiquantitative RT-PCR and to determine the cellular localization of either SRIF or individual SRIF receptor immunoreactivities. Size, density and absolute number of immunolabeled somata were measured using computer-assisted image analysis. With RT-PCR we found that all five sst receptor mRNAs were expressed, with highest levels of sst(2) and sst(4) receptors. SRIF immunolabeling was localized to sparse-occurring amacrine cells in the inner nuclear layer (INL) and to displaced amacrine cells in the ganglion cell layer (GCL). sst(2A) receptors were localized to protein kinase- (PKC) immunoreactive (IR) rod bipolar cells, calbindin- (CaBP-) IR horizontal cells, tyrosine hydroxylase- (TH-) IR amacrine cells and glycinergic amacrine cells. None of the sst(2A)-IR amacrine cells were found to express parvalbumin (PV) immunoreactivity. sst(4) receptor immunolabeling was localized to CaBP-IR and CaBP-non-IR cells in the GCL that originated long process bundles in the GC axon layer. These cells were not observed after optic nerve transection and they were therefore interpreted as ganglion cells. Quantitative analysis showed that all of the PKC-IR rod bipolar cells, CaBP-IR horizontal cells, and TH-IR amacrine cells and 5% of the glycinergic amacrine cells expressed sst(2A) receptors. In addition, 4-6% of the putative ganglion cells expressed sst(4) receptors. The localization of SRIF to sparse-occurring retinal neurons, together with the widespread expression of sst(2A) and sst(4) receptors suggests that SRIF acts at multiple levels of retinal circuitry. These results provide a database for investigations of the functional retinal networks in mice with genetic alterations of somatostatinergic transmission.
Cristiani
Rosella
R
Dipartimento di Fisiologia e Biochimica 'G.Moruzzi', Università degli Studi di Pisa, Via S. Zeno, 31, 56127, Pisa, Italy.
Petrucci
Cristina
C
Dal Monte
Massimo
M
Bagnoli
Paola
P
D025042:Amacrine Cells / Q000166:cytology / Q000378:metabolism; D000818:Animals; D064026:Calbindins; D005998:Glycine / Q000378:metabolism; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D007527:Isoenzymes / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D009433:Neural Inhibition / Q000502:physiology; D009434:Neural Pathways / Q000166:cytology / Q000378:metabolism*; D009474:Neurons / Q000166:cytology / Q000378:metabolism*; D010320:Parvalbumins / Q000378:metabolism; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism; D051571:Protein Kinase C-alpha; D012333:RNA, Messenger / Q000378:metabolism; D017481:Receptors, Somatostatin / Q000235:genetics* / Q000378:metabolism*; D012160:Retina / Q000166:cytology / Q000378:metabolism*; D012165:Retinal Ganglion Cells / Q000166:cytology / Q000378:metabolism; D017948:Retinal Rod Photoreceptor Cells / Q000166:cytology / Q000378:metabolism; D064030:S100 Calcium Binding Protein G / Q000378:metabolism; D013004:Somatostatin / Q000378:metabolism*; D009435:Synaptic Transmission / Q000502:physiology*; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism; D005680:gamma-Aminobutyric Acid / Q000378:metabolism
D064026:Calbindins; D007527:Isoenzymes; D010320:Parvalbumins; D020033:Protein Isoforms; D012333:RNA, Messenger; D017481:Receptors, Somatostatin; D064030:S100 Calcium Binding Protein G; D013004:Somatostatin; D005680:gamma-Aminobutyric Acid; D014446:Tyrosine 3-Monooxygenase; C496630:Prkca protein, mouse; D011493:Protein Kinase C; D051571:Protein Kinase C-alpha; D005998:Glycine