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PubMed2005

Alterations in the localization of calbindin D28K-, calretinin-, and parvalbumin-immunoreactive neurons of rabbit retinal ganglion cell layer from ischemia and reperfusion.

Calcium-binding proteins are thought to play important roles in calcium buffering. The present study investigated the effects of ischemia and reperfusion on calbindin D28K, calretinin, and parvalbumin immunoreactivity in the ganglion cell layer of the rabbit. Rabbits were administered ischemic damage by increasing the intraocular pressure. After 60 and 90 min of ischemia, reperfusion (7 d) was allowed to occur. The b-wave of the electroretinogram (ERG) was reduced by more than 50% and almost 80% in retina given ischemia for 60 and 90 min, respectively. The oscillatory potential (OPs) wave was reduced approximately 50% at 60 min ischemia and 70% at 90 min ischemia. In both normal and ischemic-treated retina, calcium-binding protein immunoreactivity was seen in many cells in the ganglion cell layer. In eyes subjected to 60 min ischemia, there was a decrease of the density of calbindin D28K- (8.29%), calretinin- (14.44%), and parvalbumin- (26.83%) immunoreactive (IR) cells compared to the control retina. In eyes subjected to 90 min ischemia, there was a higher decrease of the density of calbindin D28K- (18.48%), calretinin- (33.59%), and parvalbumin- (54.26%) IR cells than at 60 min. Some calcium-binding protein-IR neurons, especially calretinin-IR neurons, showed aggregations that were abnormally packed together in retina subjected to ischemia for 90 min. The results show that calbindin D28K-, calretinin-, and parvalbumin-IR cells in the ganglion cell layer are susceptible to ischemic damage and reperfusion. The degree of reduction varied among different calcium-binding proteins and ischemic damage times. These results suggest that calbindin D28K-containing neurons are less susceptible to ischemic damage than calretinin- and parvalbumin-containing neurons in the ganglion cell layer of rabbit retina.

Animals↗
PubMed2005

Immunocytochemical localization of nitric oxide synthase-containing neurons in mouse and rabbit visual cortex and co-localization with calcium-binding proteins.

Nitric oxide (NO) occurs in various types of cells in the central nervous system. We studied the distribution and morphology of neuronal nitric oxide synthase (NOS)-containing neurons in the visual cortex of mouse and rabbit with antibody immunocytochemistry. We also compared this labeling to that of calbindin D28K, calretinin, and parvalbumin. Staining for NOS was seen both in the specific layers and in selective cell types. The densest concentration of intense anti-NOS immunoreactive (IR) neurons was found in layer VI, while the weak anti-NOS-IR neurons were found in layer II/III in both animals. The NOS-IR neurons varied in morphology. The large majority of NOS-IR neurons were round or oval cells with many dendrites coursing in all directions. Two-color immunofluorescence revealed that only 16.7% of the NOS-IR cells were double-labeled with calbindin D28K in the mouse visual cortex, while more than half (51.7%) of the NOS-IR cells were double-labeled with calretinin and 25.0% of the NOS-IR cells were double-labeled with parvalbumin in mouse. By contrast, 92.4% of the NOS-IR neurons expressed calbindin D28K while only 2.5% of the NOS-IR neurons expressed calretinin in the rabbit visual cortex. In contrast with the mouse, none of the NOS-IR cells in the rabbit visual cortex were double-labeled with parvalbumin. The results indicate that neurons in the visual cortex of both animals express NOS in specific layers and cell types, which do not correlate with the expression of calbindin D28K, calretinin or parvalbumin between the two animals.

Animals↗
PubMed2006

Distribution of AMPA glutamate receptor GluR1 subunit-immunoreactive neurons and their co-localization with calcium-binding proteins and GABA in the mouse visual cortex.

The neuronal localization of alpha-amino-3-hydroxyl-5-methyl-4-isoxazole propionic acid (AMPA) glutamate receptor (GluR) subunits is vital as they play key roles in the regulation of calcium permeability. We have examined the distribution of the calcium permeable AMPA glutamate receptor subunit GluR1 in the mouse visual cortex immunocytochemically. We compared this distribution to that of the calcium-binding proteins calbindin D28K, calretinin, and parvalbumin, and of GABA. The highest density of GluR1-immunoreactive (IR) neurons was found in layers II/III. Enucleation appeared to have no effect on the distribution of GluR1-IR neurons. The labeled neurons varied in morphology; the majority were round or oval and no pyramidal cells were labeled by the antibody. Two-color immunofluorescence revealed that 26.27%, 10.65%, and 40.31% of the GluR1-IR cells also contained, respectively, calbindin D28K, calretinin, and parvalbumin. 20.74% of the GluR1-IR neurons also expressed GABA. These results indicate that many neurons that express calcium-permeable GluR1 also express calcium binding proteins. They also demonstrate that one fifth of the GluR1-IR neurons in the mouse visual cortex are GABAergic interneurons.

Animals↗
PubMed2005

[Extrinsic cells, immunoreactive to Ca-binding protein, as sources of thalamic visual centres in tortoises].

Extrinsic sources of calcium-binding proteins involved in immunoreactive innervation of the visual thalamic nuclei Rot and GLd in turtles (Testudo horsfieldi and Emys orbicularis) were studied using HRP tracing method and immunohistochemistry. In 1.5-4.5 months after monocular enucleation calbindin (Calb)-, parvalbumin (Parv)- and calretinin (Calr)-labeling was found in fragments of degenerated retinal fibers in the contralateral optic tract and in some retinorecipient structures (optic tectum, GLd and GLv). Changes in GLd were detected in its neuropil part. in 2.0-3.5 months after unilateral ablation of tectum and pretectum, the densities of Parv-, Calb- and Aclr-immunoreactivity terminals and fibers were diminisched in the ipsilateral n. Rot, with the maximum effect seen in Parv. Following HRP injection into the visual thalamus (Rot and GLd), retrogradely labeled cells with Parv label only, were revealed in the ventrothalamic nucleus Enta, pretectal nucleus Ptv, and in all types of Ca-binding proteins (CaBPr) in separately labeled cells of the optic tectum. Thus, it has been shown that thalamic visual centers in turtles have multiple extrinsic cells, which serve as sources of CaBPr projections. The present data suggest that organization of CaBPr inputs to visual thalamus in reptiles (turtle) and higher amniotes are fundamentally similar.

Animals↗
PubMed1995

On the structure of the pretectal nuclei of the rat: an immunocytochemical and tracer study.

We have studied the distribution of the calcium-binding proteins parvalbumin, calbindin and calretinin, the NADPH diaphorase activity and the morphology of the commissural neurons, revealed by the stereotactic applications of fluorogold in the pretectal complex of the rat. The histochemical differentiation of the pretectal complex shows a complementary pattern of parvalbumin and calbindin containing cells. Only a few of the neurons in the pretectal complex contain calbindin. Calretinin immunoreactivity is scant and diffuse. The NADPH-diaphorase activity is restricted to neurons and terminals in the nucleus of the optic tract and the dorsal terminal nucleus. Due to numerous active fibers which traverse these nuclei they display a reticular appearance. Commissural neurons constitute 20% of the cell number of the pretectal complex and are restricted to the dorsal and lateral terminal nuclei.

Animals↗
PubMed1993

Light- and electron microscopic localization of parvalbumin, calbindin D-28k and calretinin in the dorsal lateral geniculate nucleus of the rat.

The localization of parvalbumin, calbindin D-28k and calretinin have been investigated in the dorsal lateral geniculate nucleus (d lgn) of the rat at the light and electron microscopical level. Parvalbumin and calretinin positive sites are restricted to nerve fibres, whereas calbindin is present in fibres as well as in nerve cells showing morphological characteristics of interneurons. Ultrastructurally parvalbumin immunoreactivity is found in large terminals surrounded by glial lamellae containing round vesicles and making asymmetric contacts on dendrites. These morphological characteristics are typical for retinal endings of type 2a. Another kind of parvalbumin positive presynaptic terminals are seen on the surface of unstained nerve cell bodies and features symmetrical contacts. We conclude that this type represents axonal terminals of GABAergic neurons of the thalamic reticular nucleus. Calbindin positive nerve cells in the d lgn occur in the latero-dorsal part and according to morphological characteristics, belong to interneurons. Calbindin positive nerve cells receive synaptic terminals deriving from different kind of unstained presynaptic profiles. Calretinin immunoreactivity is localized in small to medium sized presynaptic endings with round vesicles, pale mitochondria and Gray-type 1 contacts on dendrites of relay- and interneurons. Some calretinin positive terminals are located in triads or in complex encapsulated regions. Therefore we identify calretinin positive terminals as the retinal inputs of type 2b. Our results demonstrate the expression of the three calcium binding proteins in morphologically, physiologically and biochemically different structures within the d lgn of the rat. The distribution differs from that found in the d lgn of the cat or monkey.

Animals↗
PubMed1993

The calcium-binding protein calretinin is localized in a subset of interneurons in the rat cerebral cortex: a light and electron immunohistochemical study.

The distribution of the calcium binding protein, calretinin (CR) has been investigated immunohistochemically in the cerebral cortex of albino rats by light- and electron microscopy. At the light microscopical level the pattern of CR-immunoreactivity (ir) appeared very similar in all regions of the rat cerebral cortex. CR-immunoreactive cells were found sparsely in layer I to layer VI, and frequently also in the white matter of the corpus callosum. All CR-ir neurons revealed morphological characteristics of local interneurons. The calretinin positive interneurons could be grouped according to their laminar occurrence, dendritic arborization and the soma size into 5 cell type classes. Quantitative measurements were performed only in the visual cortex. CR-ir neurons were more frequent in the superficial layers II and III. In all other layers, CR-ir cells are sparsely distributed with no preferential laminar localization. At the electron microscopical level, CR-ir axonal boutons formed frequently symmetrical axo-dendritic contacts. In all animals we observed CR-ir axons forming also synaptses of asymmetrical type. In summary calretinin labelled an interneuronal subpopulation of the rat cerebral cortex, which seemed not to overlap in its distribution and labelled structures to those, containing the related calcium binding proteins parvalbumin and calbindin D-28k.

Animals↗
PubMed1996

Neurocalcin immunoreactivity in the rat accessory olfactory bulb.

The distribution and morphology of neurocalcin-immunopositive neurons have been studied in the rat accessory olfactory bulb. Different subsets of neurons displaying neurocalcin immunoreactivity were found in the glomerular layer, the external plexiform layer and the internal plexiform layer. The most abundant staining was detected in the glomerular layer where neurocalcin-immunoreactive periglomerular cells and external tufted cells were observed in the lateral glomeruli, whereas the central region of this layer was practically devoid of immunopositive neurons. In the external plexiform layer, medial tufted cells and Van Gehuchten cells displayed neurocalcin immunoreactivity. In the internal plexiform layer, interneurons classified as horizontal cells and vertical cells of Cajal were neurocalcin-immunoreactivity. In the internal plexiform layer, interneurons classified as horizontal cells and vertical cells of Cajal were neurocalcin-immunostained. The staining pattern for neurocalcin in the accessory olfactory bulb showed similarities with the immunostaining described in this brain region for another EF-hand calcium binding protein, calbindin D-28k. However, after double immunohistochemical labeling, colocalization of both proteins in the same neuron was not observed, reflecting a biochemical heterogeneity within morphologically homogeneous neuronal groups.

Animals↗
PubMed1997

Morphological diversity of nitric oxide synthesising neurons in mammalian cerebral cortex.

Neocortical neurons that utilise nitric oxide (NO) differ in morphology in different mammalian species. In the present study we examine these differences in the neocortex of mouse, rat, guinea-pig, rabbit, cat and monkey using histochemistry for nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) and immunocytochemistry for nitric oxide synthase (NOS), gamma amino-butyric acid (GABA), calbindin (CB), parvalbumin (PV) and calretinin (CR). NO neurons are non-pyramidal and can be divided into two distinct types, both of which react for NOS and NADPH-d. Type I neurons have a relatively large soma with heavy reaction product filling even the fine processes. They occur in all species, mainly near the border between the cortex and white matter, with fewer in the cortex, mostly in the superficial layers (II-IV). Type II cells are more numerous, smaller, and lighter in reactivity. They are in all species examined here except rodents, and in all cortical layers, but mainly layers II-IV. Most intracortical and some subcortical Type I neurons express GABA. A few intracortical Type I cells contain CB. All Type II cells express GABA and most also CB. Neither Type I nor Type II cells stain for PV or CR. We conclude that there is a tendency for a reduction of Type I cells, and increase of Type II, in mammalian neocortex with phylogeny.

Animals↗
PubMed1997

Synaptic connections of calretinin-immunoreactive neurons in the human neocortex.

Previous immunocytochemical studies in the cerebral cortex of various species have shown that the calcium-binding protein calretinin (CR) labels specific subpopulations of nonspiny nonpyramidal cells (interneurons). The present study attempts to characterize morphologically and chemically the microcircuitry of CR-immunoreactive (CR-ir) neurons in the human temporal neocortex. Postembedding immunocytochemistry for CR and GABA and combination immunocytochemistry for CR and nonphosphorylated neurofilament protein (NPNFP) or for CR and the calcium-binding proteins parvalbumin (PV) and calbindin (CB) showed CR multiterminal endings frequently innervating the distal apical dendrite or the cell body and proximal dendrites of NPNFP-ir or CB-ir pyramidal cells, respectively. Cell bodies of interneurons immunoreactive for CB or PV were innervated only occasionally by CR multiterminal endings, whereas certain GABA neurons were surrounded by them. Furthermore, CR-ir axon terminals formed either symmetrical (the majority) or asymmetrical synapses with a variety of postsynaptic elements. These results indicate that different subpopulations of CR interneurons exist that are specialized for selective innervation of somatic or dendritic regions of certain pyramidal and nonpyramidal neurons.

Adult↗
PubMed1997

Use of calcium-binding proteins to map inputs in vestibular nuclei of the gerbil.

We wished to determine whether calbindin and/or calretinin are appropriate markers for vestibular afferents, a population of neurons in the vestibular nuclear complex, or cerebellar Purkinje inputs. To accomplish this goal, immunocytochemical staining was observed in gerbils after lesions of the vestibular nerve central to the ganglion, the cerebellum, or both. Eleven to fourteen days after recovery, the brain was processed for immunocytochemical identification of calretinin and calbindin. After lesion of the vestibular nerve, no calretinin staining was seen in any of the vestibular nuclei except for a population of intrinsic neurons, which showed no obvious change in number or staining pattern. Calbindin staining was reduced in all nuclei except the dorsal part of the lateral vestibular nuclei. The density of staining of each marker, measured in the magnocellular medial vestibular nucleus, was significantly reduced. After the cerebellar lesion, no differences in calretinin staining were noted. However, calbindin staining was greatly reduced in all nuclei. The density of staining, measured in the caudal medial vestibular nucleus, was significantly lower. After a combined lesion of the cerebellum and vestibular nerve, the distribution and density of calretinin staining resembled that after vestibular nerve section alone, whereas calbindin staining was no longer seen. This study demonstrates that calretinin and calbindin are effective markers for the identification of vestibular afferents.

Animals↗
PubMed1997

Activity-dependent regulation of calcium-binding proteins in the developing rat olfactory bulb.

Intracellular calcium, important in a variety of second messenger cascades, is regulated in part by calcium-binding proteins such as calretinin, parvalbumin, and calbindin. These proteins are highly concentrated in the rat main olfactory bulb and are localized in distinct neuronal populations. In the present study, postnatal expression was characterized immunohistochemically in normal rats and in rats with functional olfactory deprivation caused by unilateral naris closure, a manipulation that attenuates electrical activity in the bulb. Bulbs were examined from rats that had undergone naris closure or sham surgery on either postnatal day 1 (P1) or P30 and were allowed varying subsequent survival times. Each of the calcium-binding proteins showed both distinct patterns of early expression and differential susceptibility to olfactory restriction. For example, at P10, the densest immunoreactivity was observed for calretinin, a protein whose expression was the least affected by naris closure. After occlusion from P1-P30, there was a 30% reduction in the density of calbindin-immunoreactive profiles in the glomerular layer, and parvalbumin-immunoreactive profiles were reduced by 64% in the external plexiform layer. Unlike many other changes induced by deprivation, the effects of olfactory restriction on calbindin and parvalbumin expression were not age dependent: naris closure from P30-P60 caused similar substantial decreases in calbindin and parvalbumin immunoreactivities. These data demonstrate that the expression of calbindin and parvalbumin in rat bulb is regulated, in part, by afferent activity that is associated with full sensory experiences. The reductions of these calcium-binding proteins following olfactory deprivation are likely to be commensurate with altered control of intracellular calcium.

Animals↗
PubMed1997

Distribution of parvalbumin-, calretinin-, and calbindin-D28k-immunoreactive neurons and fibers in the human entorhinal cortex.

Parvalbumin, calretinin, and calbindin-D28k are calcium-binding proteins that are located in largely nonoverlapping neuronal populations in the brain. The authors studied the distribution of parvalbumin-, calretinin-, and calbindin-D28k-immunoreactive (ir) cells, fibers, terminals, and neuropil in the eight subfields of the human entorhinal cortex. The distribution of each of the three calcium-binding proteins largely followed the cytoarchitectonic borders of the eight entorhinal subfields, although the regional and laminar distributions of the three proteins were segregated rather than overlapping. The highest density of parvalbumin-ir neurons and terminals was found in the caudal and lateral subfields of the entorhinal cortex. Calretinin and calbindin-D28k immunoreactivities were high rostromedially, although a large number of calretinin and calbindin-D28k neurons were also found in the caudal subfields. All parvalbumin-ir cells had a morphological appearance of nonpyramidal neurons. Parvalbumin-ir terminals formed basket-like formations around unstained somata and cartridges, suggesting that parvalbumin neurons compose a subpopulation of gamma-aminobutyric acid (GABA)ergic basket cells and chandelier cells, respectively. Although calretinin and calbindin-D28k were also found in numerous nonpyramidal neurons, both were also located in pyramidal-shaped neurons in layers V and VI (calretinin) and in layers II and III (calbindin) of the entorhinal cortex, suggesting that they play roles in projection neurons as well. Moreover, the high density of nonpyramidal neurons containing calcium-binding proteins in layers II and III of the entorhinal cortex suggests that they form an integral component of a network that controls the entorhinal outputs to the hippocampus. Furthermore, the largely nonoverlapping distributions of the parvalbumin-, calretinin-, and calbindin-ir neuronal populations in the entorhinal cortex indicate that each of them may modulate a different subset of topographically organized entorhinal outputs.

Adult↗
PubMed1998

Hippocampal interneurons expressing glutamic acid decarboxylase and calcium-binding proteins decrease with aging in Fischer 344 rats.

Aging leads to alterations in the function and plasticity of hippocampal circuitry in addition to behavioral changes. To identify critical alterations in the substrate for inhibitory circuitry as a function of aging, we evaluated the numbers of hippocampal interneurons that were positive for glutamic acid decarboxylase and those that expressed calcium-binding proteins (parvalbumin, calbindin, and calretinin) in young adult (4-5 months old) and aged (23-25 months old) male Fischer 344 rats. Both the overall interneuron population and specific subpopulations of interneurons demonstrated a commensurate decline in numbers throughout the hippocampus with aging. Interneurons positive for glutamic acid decarboxylase were significantly depleted in the stratum radiatum of CA1, the strata oriens, radiatum and pyramidale of CA3, the dentate molecular layer, and the dentate hilus. Parvalbumin interneurons showed significant reductions in the strata oriens and pyramidale of CA1, the stratum pyramidale of CA3, and the dentate hilus. The reductions in calbindin interneurons were more pronounced than other calcium-binding protein-positive interneurons and were highly significant in the strata oriens and radiatum of both CA1 and CA3 subfields and in the dentate hilus. Calretinin interneurons were decreased significantly in the strata oriens and radiatum of CA3, in the dentate granule cell and molecular layers, and in the dentate hilus. However, the relative ratio of parvalbumin-, calbindin-, and calretinin-positive interneurons compared with glutamic acid decarboxylase-positive interneurons remained constant with aging, suggesting actual loss of interneurons expressing calcium-binding proteins with age. This loss contrasts with the reported preservation of pyramidal neurons with aging in the hippocampus. Functional decreases in inhibitory drive throughout the hippocampus may occur due to this loss, particularly alterations in the processing of feed-forward information through the hippocampus. In addition, such a profound alteration in interneuron number will likely alter inhibitory control of excitability and neuronal synchrony with behavioral states.

Aging↗
PubMed1998

Complementary distributions of calbindin, parvalbumin and calretinin in the cerebellar vermis of the adult cat.

Immunocytochemistry was used to compare regional and cellular distribution of the calcium-binding proteins calbindin (CB), parvalbumin (PV) and calretinin (CR) in the cerebellar vermis of adult cats. CB and PV displayed similar patterns of distribution, mainly in Purkinje cells and their processes. Immunoreactive Purkinje cell axons were organised in bundles alternating with reaction-free strips, or raphes, of afferent fibres. In contrast, CR immunoreactivity was most apparent in unipolar brush neurons, and in mossy and climbing fibres. CR positive unipolar brush neurons were clustered and positive climbing fibres formed bands. Thus, CR was associated with afferent fibres and interneurons, and occurred in complementary structures to those demonstrated for CB and PV, mainly in efferent neurons and pathways.

Animals↗
PubMed1998

Vagal and spinal afferent innervation of the rat esophagus: a combined retrograde tracing and immunocytochemical study with special emphasis on calcium-binding proteins.

Vagal afferent neurons contain a variety of neurochemical markers and neuroactive substances, most of which are present also in dorsal root ganglion cells. To test for the suitability of the calcium-binding protein calretinin as a specific marker for vagal afferent fibers in the periphery, immunocytochemistry for this protein was combined with retrograde tracing. Nerve fibers in the rat esophagus, as well as vagal and spinal sensory neurons innervating the esophagus, were investigated for co-localization of calretinin with calbindin, calcitonin gene-related peptide, and NADPH diaphorase. The results indicated that calretinin immunocytochemistry demonstrates neuronal structures known as vagal afferent from other studies, in particular intraganglionic laminar endings. A few enteric neurons whose distribution was unrelated to intraganglionic laminar endings also stained for calretinin. Strikingly, calretinin immunoreactivity was absent from spinal afferent neurons innervating the rat esophagus. In intraganglionic laminar endings and nodose ganglion cells calretinin was highly co-localized with calbindin but not with calcitonin gene-related peptide. On the other hand, calbindin was also found in spinal afferents to the esophagus where it was co-localized with calcitonin gene-related peptide. Vagal afferent neurons innervating the esophagus were never positive for NADPH diaphorase. Thus, calretinin appears to be a more specific marker for vagal afferent structures in the esophagus than calbindin, which is expressed by both vagal and spinal sensory neurons. Calretinin immunocytochemistry may be utilized as a valuable tool for investigations of subpopulations of vagal afferents in certain viscera.

Animals↗
PubMed1998

Regional and cellular patterns of reelin mRNA expression in the forebrain of the developing and adult mouse.

The reelin gene encodes an extracellular protein that is crucial for neuronal migration in laminated brain regions. To gain insights into the functions of Reelin, we performed high-resolution in situ hybridization analyses to determine the pattern of reelin expression in the developing forebrain of the mouse. We also performed double-labeling studies with several markers, including calcium-binding proteins, GAD65/67, and neuropeptides, to characterize the neuronal subsets that express reelin transcripts. reelin expression was detected at embryonic day 10 and later in the forebrain, with a distribution that is consistent with the prosomeric model of forebrain regionalization. In the diencephalon, expression was restricted to transverse and longitudinal domains that delineated boundaries between neuromeres. During embryogenesis, reelin was detected in the cerebral cortex in Cajal-Retzius cells but not in the GABAergic neurons of layer I. At prenatal stages, reelin was also expressed in the olfactory bulb, and striatum and in restricted nuclei in the ventral telencephalon, hypothalamus, thalamus, and pretectum. At postnatal stages, reelin transcripts gradually disappeared from Cajal-Retzius cells, at the same time as they appeared in subsets of GABAergic neurons distributed throughout neocortical and hippocampal layers. In other telencephalic and diencephalic regions, reelin expression decreased steadily during the postnatal period. In the adult, there was prominent expression in the olfactory bulb and cerebral cortex, where it was restricted to subsets of GABAergic interneurons that co-expressed calbindin, calretinin, neuropeptide Y, and somatostatin. This complex pattern of cellular and regional expression is consistent with Reelin having multiple roles in brain development and adult brain function.

Age Factors↗
PubMed1998

Duodenal sensory neurons project to sphincter of Oddi ganglia in guinea pig.

Retrograde labeling of duodenum-sphincter of Oddi (SO) preparations in vitro with the carbocyanine dye DiI revealed that duodenal neurons project to the SO. The duodenum-SO-projecting neurons were immunoreactive (IR) for choline acetyltransferase but not nitric oxide synthase or calretinin, indicating that this is a cholinergic projection and that this pathway is distinct from the circuitry involved in the ascending limb of the peristaltic reflex. Approximately 20% of the duodenum-SO projection neurons were IR for calbindin. Calbindin-IR nerves within SO ganglia degenerated when the SO was maintained in organ culture alone, but persisted when the SO was cultured with the duodenum intact. Therefore, SO ganglia are a target of the calbindin-positive duodenum-SO projection. Because calbindin is a marker of intrinsic sensory neurons that have processes that pass to the mucosa, these neurons are in position to detect the release of a compound from the mucosa and signal its release to SO ganglia. When applied to retrogradely labeled neurons, cholecystokinin (CCK) elicited a prolonged depolarization, indicating that duodenum-SO-projecting neurons could be capable of detecting CCK released from the mucosa. It is proposed that the role of the intrinsic sensory neurons that project to the SO may be to signal the postprandial release of CCK, thus providing an instruction to decrease SO resistance and facilitate the flow of bile into the duodenum.

Animals↗