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At least 19 recordsLinked to original sources

PubMed1995

Solution structure of (Cd2+)1-calbindin D9k reveals details of the stepwise structural changes along the Apo-->(Ca2+)II1-->(Ca2+)I,II2 binding pathway.

The three-dimensional solution structure of (Cd2+)1-calbindin D9k has been determined by distance geometry, restrained molecular dynamics and relaxation matrix calculations using experimental constraints obtained from two-dimensional 1H and 15N-1H NMR spectroscopy. The final input data consisted of 1055 NOE distance constraints and 71 dihedral angle constraints, corresponding to 15 constraints per residue on average. The resulting ensemble of 24 structures has no distance or dihedral angle constraints consistently violated by more than 0.07 A and 1.8 degrees, respectively. The structure is characteristic of an EF-hand protein, with two helix-loop-helix calcium binding motifs joined by a flexible linker, and a short anti-parallel beta-type interaction between the two ion-binding sites. The four helices are well defined with a root mean square deviation from the mean coordinates of 0.35 A for the backbone atoms. The structure of the half-saturated cadmium state was compared with the previously determined solution structures of the apo and fully calcium saturated calbindin D9k. The comparisons were aided by introducing the ensemble averaged distance difference matrix as a tool for analyzing differences between two ensembles of structures. Detailed analyses of differences between the three states in backbone and side-chain dihedral angles, hydrogen bonds, interatomic distances, and packing of the hydrophobic core reveal the reorganization of the protein that occurs upon ion binding. Overall, it was found that (Cd2+)1-calbindin D9k, representing the half-saturated calcium state with an ion in site II, is structurally more similar to the fully calcium-saturated state than the apo state. Thus, for the binding sequence apo-->(Ca2+)II1-->(Ca2+)I,II2, the structural changes occurring upon ion binding are most pronounced for the first binding step, an observation that bears significantly on the molecular basis for cooperative calcium binding in calbindin D9k.

Animals↗

PubMed2005

Expression of S100 proteins in normal human tissues and common cancers using tissue microarrays: S100A6, S100A8, S100A9 and S100A11 are all overexpressed in common cancers.

AIMS: To survey the expression of members of the S100 family of calcium-binding proteins in normal human tissues and common cancers using tissue microarrays. S100A6, S100A8, S100A9 and S100A11 have all been suggested to have potential roles in carcinogenesis and tumour progression but their expression has not been described in a wide range of human tissues and tumours. METHODS AND RESULTS: A custom-made tissue array, containing 291 tissue cores representing 28 tissue types and 21 tumour types, was used to produce sections that were immunostained for S100A2, S100A6, S100A8, S100A9, S100A11, calbindin 1, calbindin 2, S100B and parvalbumin. S100A6, S100A8 and S100A9 were expressed in 32%, 12% and 28% of breast cancers, respectively. There was a translocation of S100A11 expression from exclusively nuclear in normal tissues to cytoplasmic and nuclear in all common cancers. CONCLUSIONS: S100A6, S100A8, S100A9 and S100A11 are all expressed in common cancers, especially breast cancer. In addition, S100A11 undergoes a nucleocytoplasmic translocation which may have a direct influence on the proliferation of the cancer cells.

Calbindin 1↗

PubMed1999

NMR investigation and secondary structure of domains I and II of rat brain calbindin D28k (1-93).

Calbindin D28k, a member of the troponin C superfamily of calcium-binding proteins, contains six putative EF hand domains but binds only four calcium-atoms: one at a binding site of very high affinity and three calcium-atoms at binding sites of lower affinity. The high-affinity site could be located within domain I while domains III, IV, and V bind calcium less tightly. The recombinant protein construct calb I-II (residues 1-93) comprising the first two EF hands affords a unique opportunity to study a pair of EF hands with one site binding calcium tightly and the second site empty. A series of heteronuclear 2D, 3D and 4D high-resolution NMR experiments were applied to calb I-II, and led to the complete assignment of the 1H, 13C and 15N resonances. The secondary structure of the protein was deduced from the size of the 3JHN-Halpha coupling constants, the chemical shift indices of 1Etaalpha, 13Calpha, 13C' and 13Cbeta nuclei and from an analysis of backbone NOEs observed in 3D and 4D NOESY spectra. Four major alpha-helices are identified: Ala13-Phe23, Gly33-Ala50, Leu54-Asp63, Val76-Leu90, while residues Ala2-Leu6 form a fifth, flexible helical segment. Two short beta-strands (Tyr30-Glu32, Lys72-Gly74) are found preceding helices B and D and are arranged in an anti-parallel interaction. Based on these data a structural model of calb I-II was constructed that shows that the construct adopts a tertiary structure related to other well-described calcium-binding proteins of the EF-hand family. Surprisingly, the protein forms a homodimer in solution, as was shown by its NMR characterization, size-exclusion chromatography and analytical ultra-centrifugation studies.

Amino Acid Sequence↗

PubMed1987

Distribution of Calbindin-D28K 1 (CaBP) in the cerebral cortex and hippocampus of the epileptic (El) mouse.

The distribution of Calbindin-D28K (CaBP), a calcium-binding protein that binds Ca2+ with high affinity, was measured by radioimmunoassay in various cortical regions of the epileptic strain of mice El. The El strain, in which seizures are induced by repeated vestibular stimulation, had significantly lower levels of CaBP in the hippocampus and dorsal occipital cortical areas than the control CF-1 strain. Following induction of seizures in the El strain, a further decrease in CaBP levels was observed in the hippocampal formation and ventral temporal cortical regions, areas where paroxysmal activity is generated in this strain. Considering the role of CaBP as an intraneuronal calcium buffer, the present findings indicate that neuronal calcium regulation is genetically altered in the El strain and is further disturbed during the events that lead to induction of seizures.

Animals↗

PubMed2000

The role of calbindin and 1,25dihydroxyvitamin D3 in the kidney.

The identification of a putative apical Ca++ channel in 1,25dihydroxyvitamin D3 responsive epithelia (proximal intestine and the distal nephron) as well as recent studies using calbindin-D28k knock-out mice indicating the first direct in-vivo evidence for a role for this calcium-binding protein in renal calcium absorption suggest mechanisms, which had remained incomplete, related to the control of renal calcium absorption.

Animals↗

PubMed1991

Molecular basis for co-operativity in Ca2+ binding to calbindin D9k. 1H nuclear magnetic resonance studies of (Cd2+)1-bovine calbindin D9k.

The molecular basis for the co-operativity in binding of calcium ions by bovine calbindin D9k has been addressed by carrying out a comparative analysis of the solution conformation and dynamics of the apo, half saturated and fully saturated species using two-dimensional 1H nuclear magnetic resonance spectroscopy. Since the half saturated calcium form of the protein is not significantly populated under equilibrium conditions due to the co-operativity in binding of calcium ions, the half saturated cadmium form of the protein has been substituted for the calcium form. To verify that cadmium forms of calbindin D9k represent viable models for the calcium-bound species, the fully saturated cadmium form has been prepared and compared to the calcium-saturated protein. Virtually complete 1H resonance assignments have been obtained for both the (Cd2+)1 and the (Cd2+)2 states. Secondary structure elements and the global folding pattern were determined from nuclear Overhauser effects, backbone spin-spin coupling constants and slowly exchanging amide protons. Comparisons of the half saturated protein with the apo and calcium-saturated forms of calbindin D9k show that all three structures are highly similar. However, a change in the structural and dynamic properties of the protein does occur upon binding of the first ion; the half saturated form is found to be more similar to the calcium-saturated form than to the apo form. These results have important implications concerning the molecular basis for the co-operativity, and suggest that entropic effects associated with the protein dynamics play an important role.

Amino Acid Sequence↗

PubMed1995

Assignment of five loci from human chromosome 8q onto sheep chromosome 9.

Using a chromosomally characterized minipanel of sheep x hamster cell hybrids, five new loci, including carbonic anhydrase II (CA2), calbindin 1 (28 kDa) (CALB1), corticotropin releasing hormone (CRH), cytochrome P450 11B subfamily XIB (steroid-11-beta-hydroxylase), polypeptide 1 (CYP11B1), and interleukin 7 (IL7), have been assigned to sheep chromosome 9. A homolog of CA2 was detected on sheep chromosome 1. CRH was regionally localized to sheep 9q23-->q28 by in situ hybridization. This study assigns chromosome 9 as the sheep equivalent of cattle chromosome 14 and indicates that CALB1, CYP11B1, and IL7, which have not been mapped on the cattle genome, are likely to be present on cattle chromosome 14. It also shows by comparative genome analysis that a large segment of human chromosome 8q is highly conserved in sheep chromosome 9 and cattle chromosome 14. Based on these data, we propose that sheep chromosome 9 be recognised as the equivalent of cattle chromosome 14.

Animals↗

PubMed1999

Expression of calcium-binding protein regucalcin and microsomal Ca2+-ATPase regulation in rat brain: attenuation with increasing age.

The expression of calcium-binding protein regucalcin and its effect on the microsomal Ca2+-ATPase activity in rat brain tissues was investigated. The expression of regucalcin mRNA was demonstrated by reverse transcription-polymerase chain reaction (RT-PCR) analysis in brain tissues using rat regucalcin-specific primers. Regucalcin concentration in the brain tissues was about 5 x 10(-9)) M as measured using enzyme-linked immunoadsorbent assay (ELISA), and this level was lowered with increasing age (50 weeks old). The presence of regucalcin (10(-9) to 10(-7) M) in the enzyme reaction mixture caused a significant decrease in Ca2+-ATPase activity in the brain microsomes of young rats (5 weeks old). Meanwhile, the enzyme activity was not significantly altered by the addition of calmodulin (1 or 50 microg/ml), calbindin (1 or 10 microg/ml), and S-100 A protein (5 or 25 microg/ml), which are other Ca2+-binding proteins in rat brain. The effect of regucalcin to inhibit microsomal Ca2+-ATPase activity was weakened in the brain of rats with increasing age (50 weeks old). The present study demonstrates that regucalcin is expressed in the brain, and that it can uniquely inhibit Ca2+-ATPase activity in the brain microsomes of rats. The findings suggest that regucalcin plays a role in the regulation of microsomal Ca2+-ATPase activity in rat brain tissues.

Aging↗

PubMed1993

Effects of ion binding on the backbone dynamics of calbindin D9k determined by 15N NMR relaxation.

The backbone dynamics of apo- and (Cd2+)1-calbindin D9k have been characterized by 15N nuclear magnetic resonance spectroscopy. Spin-lattice and spin-spin relaxation rate constants and steady-state [1H]-15N nuclear Overhauser effects were measured at a magnetic field strength of 11.74 T by two-dimensional, proton-detected heteronuclear NMR experiments using 15N-enriched samples. The relaxation parameters were analyzed using a model-free formalism that characterizes the dynamics of the N-H bond vectors in terms of generalized order parameters and effective correlation times. The data for the apo and (Cd2+)1 states were compared to those for the (Ca2+)2 state [Kördel, J., Skelton, N. J., Akke, M., Palmer, A. G., & Chazin, W. J. (1992) Biochemistry 31, 4856-4866] to ascertain the effects on ion ligation on the backbone dynamics of calbindin D9k. The two binding loops respond differently to ligation by metal ions: high-frequency (10(9)-10(12) s-1) fluctuations of the N-terminal ion-binding loop are not affected by ion binding, whereas residues G57, D58, G59, and E60 in the C-terminal ion-binding loop have significantly lower order parameters in the apo state than in the metal-bound states. The dynamical responses of the four helices to binding of ions are much smaller than that for the C-terminal binding loop, with the strongest effect on helix III, which is located between the linker loop and binding site II. Significant fluctuations on slower time scales also were detected in the unoccupied N-terminal ion-binding loop of the apo and (Cd2+)1 states; the apparent rates were greater for the (Cd2+)1 state. These results on the dynamical response to ion binding in calbindin D9k provide insights into the molecular details of the binding process and qualitative evidence for entropic contributions to the cooperative phenomenon of calcium binding for the pathway in which the ion binds first in the C-terminal site.

Amino Acid Sequence↗

PubMed2001

Structural and biochemical characterization of neuronal calretinin domain I-II (residues 1-100). Comparison to homologous calbindin D28k domain I-II (residues 1-93).

This study characterizes the calcium-bound CR I-II domain (residues 1-100) of rat calretinin (CR). CR, with six EF-hand motifs, is believed to function as a neuronal intracellular calcium-buffer and/or calcium-sensor. The secondary structure of CR I-II, defined by standard NMR methods on 13C,15N-labeled protein, contains four helices and two short interacting segments of extended structure between the calcium-binding loops. The linker between the two helix-loop-helix, EF-hand motifs is 12 residues long. Limited trypsinolysis at K60 (there are 10 other K/R residues in CR I-II) confirms that the linker of CR I-II is solvent-exposed and that other potential sites are protected by regular secondary structure. 45Ca-overlay of glutathione S-transferase (GST)-CR(1-60) and GST-CR(61-100) fusion proteins confirm that both EF-hands of CR I-II have intrinsic calcium-binding properties. The primary sequence and NMR chemical shifts, including calcium-sensitive glycine residues, also suggest that both EF-hand loops of CR I-II bind calcium. NMR relaxation, analytical ultracentrifugation, chemical cross-linking and NMR translation diffusion measurements indicate that CR I-II exists as a monomer. Calb I-II (the homologous domain of calbindin D28k) has the same EF-hand secondary structures as CR I-II, except that helix B is three residues longer and the linker has only four residues [Klaus, W., Grzesiek, S., Labhardt, A. M., Buckwald, P., Hunziker, W., Gross, M. D. & Kallick, D. A. (1999) Eur. J. Biochem. 262, 933-938]. In contrast, Calb I-II binds one calcium cation per monomeric unit and exists as a dimer. Despite close homology and similar secondary structures, CR I-II and Calb I-II probably have distinct tertiary structure features that suggest different cellular functions for the full-length proteins.

Amino Acid Sequence↗

PubMed2005

Transmitter content, origins and connections of axons in the spinal cord that possess the serotonin (5-hydroxytryptamine) 3 receptor.

Recent evidence suggests that serotonin has pronociceptive actions in the spinal cord when it acts through 5-hydroxytryptamine (5-HT)(3) receptors. Cells and axon terminals which are concentrated in the superficial dorsal horn possess this receptor. We performed a series of immunocytochemical studies with an antibody raised against the 5-HT(3A) subunit in order to address the following questions: 1) Are axons that possess 5-HT(3) receptors excitatory? 2) Are 5-HT(3) receptors present on terminals of myelinated primary afferents? 3) What is the chemical nature of dorsal horn cells that possess 5-HT(3) receptors? 4) Do axons that possess 5-HT(3) receptors target lamina I projection cells? Approximately 45% of 5-HT(3A) immunoreactive boutons were immunoreactive for the vesicular glutamate transporter 2 and almost 80% formed synapse-like associations with GluR2 subunits of the AMPA receptor therefore it is principally glutamatergic axons that possess the receptor. Immunoreactivity was not present on myelinated primary afferent axons labeled with the B-subunit of cholera toxin or those containing the vesicular glutamate transporter 1. Calbindin (which is associated with excitatory interneurons) was found in 44% of 5-HT(3A) immunoreactive cells but other markers for inhibitory and excitatory cells were not present. Lamina I projection cells that possessed the neurokinin-1 receptor were associated with 5-HT(3A) axons but the density of contacts on individual neurons varied considerably. The results suggest that 5-HT(3) receptors are present principally on terminals of excitatory axons, and at least some of these originate from dorsal horn interneurons. The relationship between lamina I projection cells and axons possessing the 5-HT(3) receptor indicates that this receptor has an important role in regulation of ascending nociceptive information.

Animals↗

PubMed2002

Effect of 192 IgG-saporin on circadian activity rhythms, expression of P75 neurotrophin receptors, calbindin-D28K, and light-induced Fos in the suprachiasmatic nucleus in rats.

Photic entrainment of circadian rhythms in mammals is mediated through a direct retinal projection to the core region of the suprachiasmatic nucleus (SCN), the circadian clock. A proportion of this projection contains the low-affinity p75 neurotrophic receptor (p75NTR). Neonatal monosodium glutamate (MSG) treatment, which dramatically reduces p75NTR immunoreactivity in the SCN has no impact on photic entrainment. In order to clarify the contribution of p75NTR fibers in photic entrainment, targeted lesions of the p75NTR-immunoreactive SCN plexus were performed using intracerebroventricular (ICV) or intrahypothalamic injections of the immunotoxin 192 IgG-saporin (SAP) in rats. SAP treatment effectively abolished p75NTR immunoreactivity within the SCN core. ICV SAP treatment produced three different behavioral activity patterns: Animals became arrhythmic, displayed a shorter free-running period, or remained rhythmic following the lesion. Arrhythmic animals had large hypothalamic lesion which encompassed the entire SCN. In rhythmic rats, ICV-SAP significantly reduced immunostaining for calbindin-D28k (CaBP) in the SCN, and rats with shortened free-running periods had the lowest number of CaBP immunoreactive cells. ICV SAP also attenuated light-induced Fos expression in the SCN core. Despite lack of p75NTR and reduced CaBP and Fos expression in the SCN, SAP-treated rhythmic rats displayed normal photic entrainment. Intrahypothalamic SAP treatment reduced CaBP expression in the SCN but had no effect on light-induced Fos expression, free-running rhythms, or photic entrainment. The data show that p75NTR-immunoreactive elements in the SCN are not required for photic entrainment.

Activity Cycles↗

PubMed2004

Modulation of photic resetting in rats by lesions of projections to the suprachiasmatic nuclei expressing p75 neurotrophin receptor.

The suprachiasmatic nuclei of the hypothalamus (SCN) are the site of the master circadian clock in mammals. The SCN clock is mainly entrained by the light-dark cycle. Light information is conveyed from the retina to the SCN through direct, retinohypothalamic fibres. The SCN also receive other projections, like cholinergic fibres from basal forebrain. To test whether cholinergic afferents are involved in photic resetting, lesions of cholinergic projections were performed in rats with intracerebroventricular (i.c.v.) injections or intra-SCN microinjections of 192 IgG-saporin. When injected in the SCN, this immunotoxin destroys the cholinergic projections and retinohypothalamic afferents that express p75 low-affinity nerve growth factor (p75(NGF)) receptors. The extent of lesions in the basal forebrain and SCN was assessed by acetylcholinesterase histochemistry, p75(NGF) receptor, choline acetyl-transferase, calbindin-D28K and VIP immunocytochemistry. The intra-SCN treatment reduced light-induced phase advances by 30%, and induced a complete loss of forebrain and retinal afferents expressing p75(NGF) receptors within the SCN and a decrease of forebrain cholinergic neurons, most likely those projecting to the SCN. The i.c.v. treatment reduced light-induced phase advances by 40%, increased phase delays and led to extensive damage of forebrain p75(NGF)-expressing neurons, while sparing half of the fibres expressing p75(NGF) receptors (retinal afferents?) in the SCN. Because the integrity of forebrain p75(NGF)-expressing neurons appears to be critical in mediating the effects on light-induced phase advances, we therefore suggest that anterior cholinergic projections expressing p75(NGF) receptors modulate the sensitivity of the SCN clock to the phase advancing effects of light.

Acetylcholine↗

PubMed1996

Cytoarchitectural distribution of calcium binding proteins in midbrain dopaminergic regions of rats and humans.

The present study compares the distribution of three calcium binding proteins, calbindin-D28k, calretinin, and parvalbumin, in the midbrain tegmentum of rats and humans. In order to compare the distributions of these proteins directly, the cytoarchitecture of this region was evaluated by using immunohistochemistry for tyrosine hydroxylase and substance P in serial sections in both transverse and horizontal planes. There was a high degree of homology in the cytoarchitecture of the three main dopaminergic regions identified. The A8 group was localised in the retrorubral fields, which extended rostrally into the midbrain reticular fields in the human. The A9 group corresponded to the substantia nigra, which was delimited by its dense substance P innervation. The heterogeneous A10 group, situated along the dorsal border as well as medial to the A9 group, comprised multiple nuclei. The distribution of calcium binding proteins was similar in both species, although a larger proportion of neurons contained these proteins in the rat. Calbindin-D28k was localised in neurons within A8 and A10 nuclei and within the caudomedial A9 region (and rostrolateral A9 in the rat only). Calretinin was localised in similar regions. In contrast, neurons containing parvalbumin were concentrated in the substantia nigra pars reticulata. The results suggest that few dopaminergic neurons receiving striatal input in the substantia nigra contain calcium binding proteins; rather, the nondopaminergic nigral neurons contain parvalbumin. Interestingly, dopaminergic neurons are more numerous in humans, whereas nondopaminergic neurons predominate in rats, which suggests that functional differences may exist between rats and humans.

Adult↗

PubMed1996

Shell and core in monkey and human nucleus accumbens identified with antibodies to calbindin-D28k.

The neurochemical division of the rodent nucleus accumbens into shell and core is now a widely accepted concept. However, such divisions in the primate nucleus accumbens have yet to be fully clarified and described. In the present study, the forebrains of three primates--marmoset, rhesus monkey, and human--and a Wistar rat, were immunoreacted with antibodies directed against calbindin-D28k. The patterns of immunoreactivity in the primates' ventral striatum were mapped and compared to that of rat. Calbindin staining was uneven in all species and there was no evidence of a bicompartmental organization, i.e., striosome/patch and matrix, in central parts of the nucleus. Nucleus accumbens in primates, as in rat, could be divided immunohistochemically into a crescent-shaped outer shell--medially, ventrally and laterally--and an inner core. In general, medial parts of the shell stained less intensely for calbindin than did lateral parts. However, interspecific variation in the intensity of the immunoreactive staining and the mediolateral extent of the shell was obvious. The core, which immunostained unevenly, was consistently more intensely immunoreactive than either medial or lateral shell in all species except the marmoset. These results suggest that the neurochemical subdivisions of shell and core established for nucleus accumbens of rodents are also present in primates. However, further work is needed to establish whether these territories are homologous and, if so, the full extent of that homology.

Animals↗

PubMed1997

Neurochemical architecture of the human striatum.

The striatum of the human brain has a highly differentiated neurochemical architecture visible in stains for many of the neurotransmitter-related molecules present in the striatum. The distributions for these chemical markers have never been analyzed comprehensively. We compared the distributions of multiple neurochemical markers in a serial-section analysis of the caudate nucleus, the putamen, and the ventral striatum in normal human brains. The cholinergic system was identified with choline acetyltransferase (ChAT). The organization of the cholinergic fiber system was compared with that of striatal systems expressing immunoreactivity for calbindin D28k, met-enkephalin, substance P, tyrosine hydroxylase, and parvalbumin. Each striatal region analyzed displayed a unique neurochemical organization. In the dorsal caudate nucleus, the distribution of all markers followed the classical striosome/matrix organization as previously reported. In the dorsal putamen, ChAT-staining was less intense, and striosomes were delineated primarily by unstained fiber bundles. In the ventral caudate nucleus/nucleus accumbens region, the boundaries of ChAT-stained regions were not always visible with stains for calbindin, enkephalin, and substance P. The ventral putamen displayed a similar organization, except in its lateral part, where ChAT-poor regions were often found adjacent to, rather than in register with, regions expressing low levels of the other markers (calbindin, enkephalin, substance P, and tyrosine hydroxylase). Our findings suggest that, in addition to the classical striosome-matrix organization visible in the dorsal caudate nucleus and putamen, there is further neurochemical differentiation in a large ventral part of the caudate nucleus and putamen and in the ventral striatum-nucleus accumbens proper. The more complex relationships among the different neurochemical systems in the ventral striatum may reflect the increase in size in the primate of striatal regions associated with association and limbic cortex.

Adult↗

PubMed1997

Connections of the hippocampal formation in humans: I. The mossy fiber pathway.

The hippocampal formation has been one of the most extensively studied cortical regions in rats, yet little is known about the anatomical connections of the hippocampus in primates, especially humans. With the use of an antibody against the calcium-binding protein, calbindin-D28K, in normal autopsy tissue and the neuronal tracers biocytin or biotinylated dextrans in in vitro slice preparations from tissue removed during surgery for intractable epilepsy, we examined the human hippocampal mossy fiber pathway. The injections of biocytin into the dentate granule cell layer labeled neurons in a Golgi-like manner, revealing the presence of basal dendrites on about 30% of the granule cells. The granule cell axons, the mossy fibers, initially formed a diffuse plexus of fibers in the polymorphic layer before organizing into fiber fascicles in the hilar pyramidal region. These fiber fascicles were much more prominent rostrally than caudally. Within the hilus and proximal portions of the extrahilar CA3 field, the mossy fibers ran through the pyramidal cell layer, and while near the transition to field CA2, the fibers turned superficially and crossed the pyramidal layer to run in the stratum lucidum. All of these features, seen following injections of tracer into hippocampal slices from the brains of epileptics, were confirmed by calbindin-staining of mossy fibers in normal brains. Biocytin-labeled mossy fiber axons revealed two characteristic types of enlargements: small varicosities and larger expansions. The expansions were found throughout the neuropil and were highly irregular, diaminobenzidine-dense profiles that had pleiomorphic modes of attachment to the parent axon. Electron microscopic images of these biocytin labeled expansions revealed that they were large synaptic boutons bearing asymmetric synapses. This study indicates that the human mossy fiber pathway shows some minor deviations from the rodent brain but little difference from monkeys. We argue that these changes mirror a phylogenetic growth of the CA3 pyramidal neurons (subfield CA3c) into the hilus rather than an evolutionary change of the mossy fiber pathway. This growth of subfield CA3c and the increase in mossy fibers running through the pyramidal layer (and a presumed accompanying increase in proximal basal dendritic contacts) may reflect a growing role of the projection from the dentate granule cells to subfield CA3c and from there to field CA1 in the primate hippocampus.

Adult↗

PubMed1998

Chemically defined neuron groups and their subpopulations in the glomerular layer of the rat main olfactory bulb: III. Structural features of calbindin D28K-immunoreactive neurons.

The present study analyzed three-dimensional structural features and synaptic contacts of morphologically and chemically identified calbindin D28K-immunoreactive neurons in the glomerular layer of the rat main olfactory bulb by means of combined confocal laser scanning light microscopy, high-voltage electron microscopy and electron microscopic serial section/three-dimensional reconstruction. Most of calbindin D28K-immunoreactive neurons were identified as the periglomerular cell type by combined high-voltage electron microscopic and confocal laser scanning light microscopic observations, and the minority were the short-axon cell type and others. The combined confocal laser scanning light microscopic and electron microscopic study revealed that the calbindin D28K-immunoreactive neurons exhibited unique synaptic contact patterns; they received asymmetrical synapses from presumed mitral/tufted dendrites and made conversely symmetrical synapses with them. About 30% of asymmetrical postsynaptic sites and about 40% of symmetrical presynaptic sites formed reciprocal pairs of synapses. Calbindin D28K-immunoreactive dendrites and somata also received synapses from GABA-like-immunoreactive profiles containing numerous pleomorphic, and a few dense-cored, vesicles. On the other hand, surprisingly, calbindin D28K-immunoreactive neurons had almost no synaptic contacts from olfactory nerve terminals. The present study clearly revealed that calbindin D28K-immunoreactive neurons are a type of periglomerular cell involving unique synaptic contacts that have not been reported so far, and thus indicated that so-called periglomerular cells should be heterogeneous in their synaptic connections as well as in their chemical and structural features.

Animals↗