The locations of cell bodies of sympathetic neurons projecting to the stomach, the duodenum, the ileum, the colon, the spleen and the pancreas have been studied using retrograde tracing. Projections arose from both pre- and paravertebral ganglia. In the rat, the prevertebral ganglia are the paired coeliac ganglia lying caudo-lateral to the root of the coeliac artery, paired splanchnic ganglia in the abdominal segments of the greater splanchnic nerves, unpaired superior mesenteric and inter-renal ganglia and the inferior mesenteric ganglia. The projections from the prevertebral sympathetic ganglia to the different parts of the gut were organised somatotopically. The most rostral ganglia (splanchnic, coeliac, and superior mesenteric ganglia) contained neurons innervating all regions of the gastrointestinal tract, the pancreas and the spleen. The inter-renal and inferior mesenteric ganglia, located more caudally, contained neurons innervating the distal part of the gut (distal ileum and colon). The innervation of the spleen and the pancreas came from the closest ganglia (sympathetic chains, splanchnic and coeliac ganglia). This organotopic organisation was not found in the sympathetic chain ganglia; the innervation of all organs came predominantly from the lower part of the thoracic chains. A large proportion of the retrogradely labelled nerve cells in the splanchnic ganglia received nitric oxide synthase immunoreactive innervation probably from the spinal cord. In the other prevertebral ganglia, most of the neurons received nitric oxide synthase immunoreactive innervation and/or bombesin immunoreactive innervation. This leads to the conclusion that, in these ganglia, many neurons receive projections from the gastrointestinal tract in addition to the spinal cord.

The MRC OX‐2 antigen is a rat cell surface glycoprotein of mol. wt. 41 000‐47 000 found on neurones, thymocytes, B cells, follicular dendritic cells and endothelium. We now report the amino sequence for this antigen as deduced from the nucleotide sequence of cDNA clones detected by use of an oligonucleotide probe. The sequence contains 248 amino acid residues of which 202 residues are likely to be outside the cell with two domains that show homology with immunoglobulins. The N‐terminal domain fits best with Ig V domains and Thy‐1 antigen while the C‐terminal part is like an Ig C domain. Thus the structure overall is similar to an Ig light chain or the T cell receptor beta chain. Three glycosylation sites are identified on each of the MRC OX‐2 antigen domains.

The neurotransmitter gamma-aminobutyric acid (GABA) is removed from the extracellular space by sodium and chloride dependent high affinity plasma membrane transporters. In the rat central nervous system, three GABA transporters, GAT1, GAT2 and GAT3, have been cloned and localized by immunohistochemistry. The purpose of this study was to examine the distribution of these transporters within the myenteric plexus of the rat gastrointestinal tract. We investigated their cellular locations using GAT1-3 specific antisera in lightly fixed segments of rat duodenum, ileum and colon. Immunohistochemistry revealed a large number of GAT2-immunoreactive structures that surrounded neurons within each ganglion of the myenteric plexus. GAT2 was colocalized in these structures with the glial cell marker p75(NTR), suggesting that the predominant high affinity GABA transporter within enteric glia is GAT2. GAT3 immunoreactivity was localized within many nerve cell bodies, and no labeling for GAT1 was detected, although it was present in retina, which was used as a control. Double labeling for calretinin and nitric oxide synthase (NOS) revealed colocalization of GAT3 with approximately 75% of calretinin-immunoreactive neurons and 15% of NOS-immunoreactive neurons. This suggests that a small proportion of inhibitory motor neurons and at least some putative intrinsic primary afferent neurons within the rat gastrointestinal tract express GAT3. Thus NOS neurons, which appear to utilize GABA as a transmitter, and calretinin-immunoreactive neurons, which do not appear to be GABAergic, both express immunoreactivity for GABA transporters.

Four types of neurons have previously been identified by neurochemical markers in the submucosal ganglia of the guinea-pig small intestine, and functional roles have been ascribed to each type. However, morphological differences among the classes have not been determined, and there is only partial information about their projections within the submucosa. In the present work, we used intracellular microelectrodes to fill neurons of each type with biocytin, which was then converted to a permanent dye, so that the shapes of the neurons could be determined and their projections within the submucosa could be followed. Cell bodies of noncholinergic secretomotor/ vasodilator neurons had Dogiel type I morphology. These neurons, which are vasoactive intestinal peptide immunoreactive, had single axons that ran through many ganglia without providing terminals around other neurons. Cholinergic secretomotor neurons with neuropeptide Y immunoreactivity had Stach type IV morphology, and cholinergic secretomotor/vasodilator neurons had stellate cell bodies. The axons of these two types ran short distances in the plexus and did not innervate other submucosal neurons. Neurons of the fourth type, intrinsic primary afferent neurons, had cell bodies with Dogiel type II morphology and their processes supplied networks of varicose processes around other nerve cells. It is concluded that each functionally defined type of submucosal neuron has a characteristic morphology and that intrinsic primary afferent neurons synapse with secretomotor neurons to form monosynaptic secretomotor reflex circuits. Anat Rec Part A 272A: 475-483, 2003.

The MRC OX-2 antigen is a membrane glycoprotein present on rat thymocytes, neurons, follicular dendritic cells, endothelium, and some smooth muscle. The sequence of 248 amino acids has similarities to Ig domains organized with one V-like domain, one C-like domain, and transmembrane and cytoplasmic regions. Thus it resembles a T-cell receptor chain but shows no sequence divergence. We report the characterization of the human gene for this molecule. Its exon organization is similar to that found for immunoglobulins although the region with similarities to Ig J regions is found within the same exon as the V-like domain. Human MRC OX-2 is expressed at the mRNA level in brain and B-cell lines but not detected in liver or T-cell lines. It does not obviously correspond to any previously defined leukocyte antigen. The sequence homology for the human and rat MRC OX-2 molecules is higher for the Ig-related region (75%) than for many other Ig-related molecules and very high in the transmembrane region (96%), implying a functional role other than simply its anchoring into the membrane.