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PubMed2001

Contribution of the neural cell adhesion molecule to neuronal and synaptic plasticity.

The neural cell adhesion molecule (NCAM) and its polysialylated form PSA-NCAM contribute to many aspects of the development and plasticity of the central nervous system. This includes mechanisms of cell differentiation and migration, neurite outgrowth, establishment of specific patterns of synaptic connections, synaptic plasticity and long-term potentiation. How NCAM and PSA-NCAM contribute to regulate all these different mechanisms remains essentially unknown. Adhesive properties appear to be important, but recent studies also point to possible interactions between NCAM and PSA-NCAM with intracellular signalling cascades that are essential to biological functions. Some of these mechanisms are discussed and a hypothesis is proposed based on the existence of cross-talk between these molecules and signalling pathways mediated by growth factors.

Animals↗

PubMed1992

Induction of the neural cell adhesion molecule and neuronal aggregation by osteogenic protein 1.

The neural cell adhesion molecule (N-CAM) plays a fundamental role in nervous system development and regeneration, yet the regulation of the expression of N-CAM in different brain regions has remained poorly understood. Osteogenic protein 1 (OP-1) is a member of the transforming growth factor beta superfamily that is expressed in the nervous system. Treatment of the neuroblastoma-glioma hybrid cell line NG108-15 for 1-4 days with recombinant human OP-1 (hOP-1) induced alterations in cell shape, formation of epithelioid sheets, and aggregation of cells into multilayered clusters. Immunofluorescence studies and Western blots demonstrated a striking differential induction of the three N-CAM isoforms in hOP-1-treated cells. hOP-1 caused a 6-fold up-regulation of the 140-kDa N-CAM, the isoform showing the highest constitutive expression, and a 29-fold up-regulation of the 180-kDa isoform. The 120-kDa isoform was not detected in control NG108-15 cells but was readily identified in hOP-1-treated cells. Incubation of NG108-15 cells with an antisense N-CAM oligonucleotide reduced the induction of N-CAM by hOP-1 and decreased the formation of multilayered cell aggregates. Anti-N-CAM monoclonal antibodies also diminished the formation of multilayered cell aggregates by hOP-1 and decreased cell-cell adhesion when hOP-1-treated NG108-15 cells were dispersed and replated. Thus, hOP-1 produces morphologic changes in NG108-15 cells, at least in part, by inducing N-CAM. These observations suggest that OP-1 or a homologue may participate in the regulation of N-CAM during nervous system development and regeneration.

Animals↗

PubMed1994

Expression of M-cadherin protein in myogenic cells during prenatal mouse development and differentiation of embryonic stem cells in culture.

Molecules regulating morphogenesis by cell-cell interactions are the cadherins, a class of calcium-dependent adhesion molecules. One of its members, M-cadherin, has been isolated from a myoblast cell line (Donalies et al. [1991] Proc. Natl. Acad. Sci. U.S.A. 88:8024-8028). In mouse development, expression of M-cadherin mRNA first appears at day 8.5 of gestation (E8.5) in somites and has been postulated to be down-regulated in developing muscle masses (Moore and Walsh [1993] Development 117:1409-1420). Affinity-purified polyclonal M-cadherin antibodies, detecting a protein of approximately 120 kDa, were used to study the cell expression pattern of M-cadherin protein. It was first visualized in somites at E10 1/3 and could be confined to desmin positive, myotomal cells. At all subsequent prenatal stages, M-cadherin was only found in myogenic cells of somitic origin. The detection of the protein at E10 1/3 suggests a translational delay of M-cadherin mRNA of 1 to 2 days (E8.5 vs. E10 1/3). This was further supported by the finding that during differentiation of ES cell line BLC6 into skeletal muscle cells in culture, expression of M-cadherin mRNA can be detected 2 days prior to M-cadherin protein. During prenatal development, the pattern of M-cadherin expression changes: In E10 1/3 embryos and also in myotomal cells of later stages, M-cadherin is evenly distributed on the cell surface. In developing muscle masses (tested at E16 to E18), however, M-cadherin protein becomes clustered most likely at sites of cell-cell contact as indicated by double-labelling experiments: M-cadherin-staining is the positive image of laminin negative areas excluding the presence of a basal lamina at M-cadherin positive sites. Furthermore, M-cadherin is coexpressed with the neuronal cell adhesion molecule N-CAM which has been shown to mediate cell-cell contact in myogenic cells. In summary, our results are in line with the idea that M-cadherin might play a central role in myogenic morphogenesis.

Amino Acid Sequence↗

PubMed1991

Reinnervation of murine muscle following fetal sciatic nerve transection.

A technique is reported that permits transection of the sciatic nerve of mouse fetuses without interfering with fetal viability. Sciaticotomy was performed on Swiss Webster mice at day 17 of gestation; the contralateral side served as control. Six weeks later the extensor digitorum longus (EDL) muscles on both sides were injected with horseradish peroxidase (HRP). Examination of the lumbar spinal cord revealed that while a substantial number of motor neurons in the region of the spinal cord giving rise to the sciatic nerve died, the EDL muscle did become reinnervated. The size of the EDL motor neuron pool on the denervated-reinnervated side was approximately 43% of that seen on the control side. While the control EDL motor neuron pool was located in lumbar segments L3-L5, the location of the pool to the denervated-reinnervated EDL was shifted cranially to L2-L4. Denervated-reinnervated EDL muscles were analyzed immunohistochemically to study the effect of fetal denervation on the neuronal cell adhesion molecule (N-CAM) expression. At 2 weeks postnatal, N-CAM immunoreactivity in control muscle was segregated to the motor end-plate region, while fetally denervated muscle continued to express N-CAM along the length of the sarcolemma. Thus fetally denervated muscle does not develop the same pattern of N-CAM expression as normal, innervated muscle. By 6 weeks of age, the denervated-reinnervated muscle showed the same level and distribution of N-CAM immunoreactivity as did age-matched control muscle, indicating that most, if not all, of its myofibers had been reinnervated.

Animals↗

PubMed2004

Characterization of a fasciclin I-like protein with cell attachment activity from sea urchin (Strongylocentrotus intermedius) ovaries.

Fasciclin I, a neuronal cell adhesion molecule, was first identified in the grasshopper. To date, various fasciclin I-like proteins have been identified but their biological functions have not been well characterized. Here, we have purified a fasciclin I-like protein with a molecular weight of 33kDa from sea urchin (Strongylocentrotus intermedius) ovaries using hydrophobic chromatography and gel filtration. The protein was not N-glycosylated. Partial amino acid sequences of cyanogen bromide (CNBr)-cleaved fragments were highly conserved to other sea urchin fasciclin I-like proteins identified previously. The circular dichroism (CD) spectrum analysis demonstrated that the 33kDa protein contained high content of alpha-helical structure. These results suggest that the 33kDa protein is a fasciclin I-like family. Additionally, the fasciclin I-like protein promoted HT1080 human fibrosarcoma cell attachment. Further, a synthetic peptide (P1: GLREAANIAEQVDLRQVLRDVDL) of the protein corresponding to a highly conserved region of the fasciclin I-like family promoted heparin-dependent HT1080 cell attachment. Moreover, the peptide inhibited HT1080 cell attachment to the fasciclin I-like protein. These results suggest that the 33kDa protein from sea urchin ovaries isolated here is a member of the fasciclin I family and that the N-terminal region of the protein is important for cell attachment activity. The protein has a potential to be involved in biological functions in sea urchin as a cell adhesive molecule.

Amino Acid Sequence↗

PubMed1984

A neuronal surface glycoprotein associated with the cytoskeleton.

A cytoskeleton-associated glycoprotein of 130-kilodalton molecular mass (GP 130) was purified from a nonionic detergent-insoluble fraction of 10-16-d-old chicken embryo brains. GP 130 is tightly associated with other proteins in actin-containing complexes (Moss, D.J., 1983, Eur. J. Biochem., 135:291-297); thus, pure protein preparations were obtained only after the partial dissociation of the complexes with the zwitterionic detergent, dimethyl dodecyl glycine (EMPIGEN BB), followed by ion-exchange chromatography and electrophoresis on preparative SDS polyacrylamide gels. Specific monoclonal and polyclonal antibodies were raised to GP 130 and used to examine its distribution in the developing nervous system. Experiments with these antibodies revealed that GP 130 is confined to nervous tissue and is restricted to the surface of neurons in cultures derived from both the central and peripheral nervous systems. This novel glycoprotein is immunologically unrelated to the neuronal cell adhesion molecule (N-CAM), or to vinculin, a protein of similar molecular mass which has been suggested to link actin filaments to the plasma membrane. In the developing chicken embryo brain, GP 130 is first detectable around day 8 after fertilization and increases to approximately 50% of its adult level by embryonal day 13. In contrast, no increase is observed over a similar developmental period in sciatic nerve. In the adult chicken, GP 130 is most abundant in brain and has a particularly high content in areas rich in dendrites and synapses.

Aging↗

PubMed1990

Segregation of the myogenic cell lineage in mouse muscle development.

With increasing interest in the idea of therapeutic implantation of normal muscle precursor cells into muscle lacking the protein product of the dystrophin gene, it has become important to obtain enriched populations of myogenic cells from biopsied muscle sources. Myogenic cells for implantation are highly favoured as they are the only cells that will fuse readily with host muscle fibres into which they are implanted, thus carrying the introduced gene into the target fibre with the maximum of efficiency. Second, myogenic cells appear less immunogenic than those of a non-myogenic nature; and third, the use of mononuclear myogenic cells may permit the introduction of multiple copies of a deficient gene into the patient's own cells. From a mixed population of cells obtained by the enzymic disaggregation of neonatal murine muscle we have selected, utilising a modification of the panning technique, for a cell population rich in myogenic cells. Segregation was accomplished using Mab H28, an antibody to the mouse neuronal cell adhesion molecule (N-CAM), derived from mouse/rat hybridoma cells. Following incubation with Mab H28, disaggregated muscle was applied to the surface of a bacteriological grade dish previously coated with anti-rat immunoglobulin. Cells segregated into two populations; those bearing N-CAM, and hence labelled with Mab H28, were adherent to the dish, whereas those not expressing N-CAM remained in suspension. Use of this technique, which involves minimal cell loss, resulted in the segregation of prefusion myogenic cells together with fibroblasts in the 'non-adherent' fraction, whereas cells in the adherent fraction consisted of a highly enriched population of actively dividing myogenic cells.

Animals↗

PubMed1992

Solubility and posttranslational regulation of GP130/F11--a neuronal GPI-linked cell adhesion molecule enriched in the neuronal membrane skeleton.

GP130 (renamed contactin) has previously been identified by its detergent insolubility and retention with the actin-containing "membrane skeleton" isolated from chicken neurons and brain. The contactin sequence predicted a transmembrane and cytoplasmic domain for the molecule. Recently, F11 was shown to have an identical sequence except for the C terminus, and it was predicted to be linked to the plasma membrane by a glycosylphosphatidylinositol (GPI) group. Here we describe that GP130 can be released both from brain membranes and the detergent-insoluble membrane skeleton by a phosphoinositol-specific phospholipase C (PI-PLC) indicating that F11 and GP130/contactin are probably identical and that surprisingly the lipid anchor is partly or totally responsible for its non-ionic detergent insolubility. The "membrane skeleton" is a rich source of GPI-linked glycoproteins as judged by 1) most glycoproteins can be released by a PI-PLC and 2) most [3H]ethanolamine-labeled glycoproteins are present in, or enriched in the membrane skeleton. Thus, detergent insolubility appears to be a characteristic of GPI-anchored glycoproteins. No evidence has been obtained that GP130/F11 is released or secreted in vivo or in culture. In addition, GP130/F11 has an unusually long half-life in culture of greater than 3 days. The structure of the neuronal membrane skeleton and the potential function of GPI-anchored glycoproteins is discussed.

Animals↗

PubMed1995

The neural cell adhesion molecule and synaptic plasticity.

Highly stereotyped patterns of neuronal connections are laid down during the development of the nervous system via a range of activity independent and activity dependent mechanisms. Whereas the coarse hard-wiring of the nervous system appears to rely on molecular recognition events between the neuron, its pathway, and its target, the establishment of precisely patterned functional circuits is thought to be driven by neuronal activity. In this review we discuss the role that the neuronal cell adhesion molecule (NCAM) plays in morphological plasticity. Recent studies on NCAM and its probable species homologue in Aplysia (apCAM) suggests that an individual CAM can function to both promote synaptic plasticity and maintain the structure of the synapse. In the adult brain, changes between stability and plasticity are likely to underlie dynamic morphological changes in synaptic structures associated with learning and memory. In this review we use NCAM as an example to illustrate mechanisms that can change the function of an individual CAM from a molecule that promotes plasticity to one that does not. We also discuss evidence that NCAM promotes plasticity by activating a conventional signal transduction cascade, rather than by modulating adhesion per se. Finally, we consider the evidence that supports a role for NCAM in learning and memory.

Animals↗

PubMed2004

Regulators of neurite outgrowth: role of cell adhesion molecules.

Neuronal differentiation is a fundamental event in the development of the nervous system as well as in the regeneration of damaged nervous tissue. The initiation and guidance of a neurite are accomplished by positive (permissive or attractive), negative (inhibitory or repulsive), or guiding (affecting the advance of the growth cone) signals from the extracellular space. The signals may arise from either the extracellular matrix (ECM) or the surface of other cells, or be diffusible secreted factors. Based on this classification, we briefly describe selected positive, negative, and guiding signaling cues focusing on the role of cell adhesion molecules (CAMs). CAMs not only regulate cell-cell and cell-ECM adhesion "mechanically," they also trigger intracellular signaling cascades launching neurite outgrowth. Here, we describe the structure, function, and signaling of three key CAMs found in the nervous system: N-cadherin and two Ig-CAMs, L1 and the neural cell adhesion molecule NCAM.

Animals↗

PubMed1996

Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site.

The neuronal cell adhesion molecule axonin-1 is composed of six immunoglobulin and four fibronectin type III domains. Axonin-1 promotes neurite outgrowth, when presented as a substratum for neurons in vitro, via a neuronal receptor that has been identified as the neuron-glia cell adhesion molecule, NgCAM, based on the blocking effect of polyclonal antibodies directed to NgCAM. Here we report the identification of axonin-1 domains involved in NgCAM binding. NgCAM-conjugated microspheres were tested for binding to COS cells expressing domain deletion mutants of axonin-1. In addition, monoclonal antibodies directed to axonin-1 were assessed for their ability to block the axonin-1-NgCAM interaction, and their epitopes were mapped using the domain deletion mutants. The results suggest that the four amino-terminal immunoglobulin domains of axonin-1 form a domain conglomerate which is necessary and sufficient for NgCAM binding. Surprisingly, NgCAM binding to membrane-bound axonin-1 was increased strongly by deletion of the fifth or sixth immunoglobulin domains of axonin-1. Based on these results and on negative staining electron microscopy, we propose a horseshoe-shaped domain arrangement of axonin-1 that obscures the NgCAM binding site. Neurite outgrowth studies with truncated forms of axonin-1 show that axonin-1 is a neurite outgrowth-promoting substratum in the absence of the NgCAM binding site.

Animals↗

PubMed1985

Initial appearance and regional distribution of the neuron-glia cell adhesion molecule in the chick embryo.

This study represents a global survey of the times of the first appearance of the neuron-glia cell adhesion molecule (Ng-CAM) in various regions and on particular cells of the chick embryonic nervous system. Ng-CAM, originally characterized by means of an in vitro binding assay between glial cells and brain membrane vesicles, first appears in development at the surface of early postmitotic neurons. By 3 d in the chick embryo, the first neurons detected by antibodies to Ng-CAM are located in the ventral neural tube; these precursors of motor neurons emit well-stained fibers to the periphery. To identify locations of appearance of Ng-CAM in the peripheral nervous system (PNS), we used a monoclonal antibody called NC-1 that is specific for neural crest cells in early embryos to show the presence of numerous crest cells in the neuritic outgrowth from the neural tube; neither these crest cells nor those in ganglion rudiments bound anti-Ng-CAM antibodies. The earliest neurons in the PNS stained by anti-Ng-CAM appeared by 4 d of development in the cranial ganglia. At later stages and progressively, all the neurons and neurities of the PNS were found to contain Ng-CAM both in vitro and in vivo. Many central nervous system (CNS) neurons also showed Ng-CAM at these later stages, but in the CNS, the molecule was mostly associated with neuronal processes (mainly axons) rather than with cell bodies; this regional distribution at the neuronal cell surface is an example of polarity modulation. In contrast to the neural cell adhesion molecule and the liver cell adhesion molecule, both of which are found very early in derivatives of more than one germ layer, Ng-CAM is expressed only on neurons of the CNS and the PNS during the later epoch of development concerned with neural histogenesis. Ng-CAM is thus a specific differentiation product of neuroectoderm. Ng-CAM was found on developing neurons at approximately the same time that neurofilaments first appear, times at which glial cells are still undergoing differentiation from neuroepithelial precursors. The present findings and those of previous studies suggest that together the neural cell adhesion molecule and Ng-CAM mediate specific cellular interactions during the formation of neuronal networks by means of modulation events that govern their prevalence and polarity on neuronal cell surfaces.

Age Factors↗

PubMed1993

A homopurine:homopyrimidine sequence derived from the rat neuronal cell adhesion molecule-encoding gene alters expression in transient transfections.

A 178-bp homopurine-homopyrimidine (R:Y) sequence is located upstream from the transcription start point (tsp) of the rat neuronal cell adhesion molecule-encoding gene (NCAM). This R:Y sequence contains several mirror repeats. Such sequences have been proposed to regulate gene expression. To determine its effect on gene transcription, a DNA fragment containing the R:Y sequence was cloned into a luciferase-encoding (luc) expression vector. Transient transfection assays with the R:Y-luc constructs were performed in cell lines which constitutively express (B104 rat neuronal cells and C6 rat glial cells) or lack (H411E rat liver cells and L mouse fibroblast cells) NCAMs. In its natural orientation, the R:Y sequence caused a 2.5-fold reduction in luc expression in B104 and H411E cells, but had a statistically insignificant effect in C6 and L cells. The magnitude of the R:Y sequence reduction in luc expression was position and orientation dependent (varying from 2- to 5.5-fold). To determine if nuclear protein(s) specifically bind the sequence, gel retardation assays of a DNA fragment containing the R:Y sequence were carried out with nuclear extracts from these four cell lines. Specific DNA-protein interaction was found with B104 and H411E nuclear extracts, but not with C6 and L cell nuclear extracts. Competition experiments indicate that the (AGG):(TCC) repeat segment within the rat R:Y sequence may constitute the protein-binding domain. These results indicate that the R:Y sequence may have a negative effect on gene transcription in certain cell lines. In correlation with this negative effect, these same cell lines also contain nuclear proteins which bind the sequence.

Animals↗

PubMed1999

NrCAM, cerebellar granule cell receptor for the neuronal adhesion molecule F3, displays an actin-dependent mobility in growth cones.

The neuronal adhesion glycoprotein F3 is a multifunctional molecule of the immunoglobulin superfamily that displays heterophilic binding activities. In the present study, NrCAM was identified as the functional receptor mediating the inhibitory effect of F3 on axonal elongation from cerebellar granule cells. F3Fc-conjugated microspheres binding to neuronal growth cones resulted from heterophilic interaction with NrCAM but not with L1. Time-lapse video-microscopy indicated that F3Fc beads bind at the leading edge and move retrogradely to reach the base of the growth cone within a lapse of 30-60 seconds. Such velocity (5.7 microm/minute) is consistent with a coupling between F3 receptors and the retrograde flow of actin filaments. When actin filaments were disrupted by cytochalasin B, the F3Fc beads remained immobile at the leading edge. The retrograde mobility appeared to be dependent on NrCAM clustering since it was induced upon binding with cross-linked but not dimeric F3Fc chimera. These data indicate that F3 may control growth cone motility by modulating the linkage of its receptor, NrCAM, to the cytoskeleton. They provide further insights into the mechanisms by which GPI-anchored adhesion molecules may exert an inhibitory effect on axonal elongation.

Actins↗

PubMed1996

Heterologous retinal cultured neurons and cell adhesion molecules induce clustering of acetylcholine receptors and polynucleation in mouse muscle BC3H-1 clonal cell line.

Several features of the clonal cell line BC3H-1 resemble those of embryonic muscle cells at their early stage of development (Patrick et al.: J Biol Chem 252:2143-2153, 1977). Under normal culture conditions, fully differentiated BC3H-1 cells possess a spindle-shaped, muscle-like morphology with a single nucleus. Like embryonic muscle cell counterparts, they neither express the epsilon subunit nor exhibit the clustered organization of the nicotinic acetylcholine receptor (AChR) characteristic of mature myocytes. Instead, AChRs are evenly distributed upon the sarcolemma upon differentiation. Here we report that BC3H-1 cells can be induced to express AChR clusters by co-culturing the cell line with heterologous retinal neurons, which establish contacts with former cells. Clustering was also triggered by pretreating the culture substratum with several cell adhesion molecules. Polynucleation, a phenomenon observed in mature myotubes in vivo, was also observed in BC3H-1 cells under the two sets of experimental conditions. AChR clustering and polynucleation, both characteristic of the mature postsynaptic region, can thus be induced in BC3H-1 cells by at least two quite distinct pathways: neuronal cell contact and/or cell adhesion molecules. It is suggested that heterologous retinal neurons can elicit only an incomplete differentiation of BC3H-1 cells, failing to concentrate the clusters beneath the neuronal endings, and failing to induce expression of the epsilon subunit, characteristic of the mature AChR.

Animals↗

PubMed1996

Dorsal rhizotomy induces transient expression of the highly sialylated isoform of the neural cell adhesion molecule in neurons and astrocytes of the adult rat spinal cord.

Expression of the weakly adhesive, highly sialylated isoform of the neural cell adhesion molecule is a feature common to cell capable of migration and conformation changes. 11,18,19 Polysialylated neural cell adhesion molecule also intervenes in axonal outgrowth and synaptogenesis during development and after lesion. 11,13 High levels of polysialylated neural cell adhesion molecule immunoreactivity are normally visible in laminae I,II and X of the adult rat spinal cord. 2,15 We how here that unilateral cervical dorsal rhizotomy induced no detectable changes in immunoreactivity in these areas. However, 24 h after lesion, polysialylated neural cell adhesion molecule immunoreactivity appeared in neurons scattered in laminae III-IX, ipsi-and contralateral to lesion. This reaction increased particularly on the contralateral side, became maximal at four days and disappeared eight days later. At this time, there was immunolabelling of astrocytes with an activated morphology. The astrocytic labelling, predominant on the side ipsilateral to the lesion, was strongest 12 days after rhizotomy, then diminished progressively. Deafferentation thus causes a transient expression of polysialylated neural cell adhesion molecule within areas of the spinal cord distinct from those which permanently express this adhesion molecule. Such expression occurs both in neurons and glial cells, with a temporal pattern specific to each type of cell.

Afferent Pathways↗

PubMed2005

Neuronal characteristics of small-cell lung cancer.

Wide ranging experimental evidence suggests that human small-cell lung cancer (SCLC) has a number of molecular and subcellular characteristics normally associated with neurones. This review outlines and discusses these characteristics in the light of recent developments in the field. Emphasis is placed upon neuronal cell adhesion molecules, neurone-restrictive silencer factor, neurotransmitters/peptides and voltage-gated ion, especially Na(+) channels. The hypothesis is put forward that acquisition of such characteristics and the membrane 'excitability' that would follow can accelerate metastatic progression. The clinical potential of the neuronal characteristics of SCLC, in particular ion channel expression/activity, is discussed in relation to possible novel diagnostic and therapeutic modalities.

Carcinoma, Small Cell↗

PubMed2003

Immunohistochemistry of the canine vomeronasal organ.

The canine's olfactory acuity is legendary, but neither its main olfactory system nor its vomeronasal system has been described in much detail. We used immunohistochemistry on paraffin-embedded sections of male and female adult dog vomeronasal organ (VNO) to characterize the expression of proteins known to be expressed in the VNO of several other mammals. Basal cell bodies were more apparent in each section than in rodent VNO and expressed immunoreactivity to anticytokeratin and antiepidermal growth factor receptor antibodies. The thin layer of neurone cell bodies in the sensory epithelium and axon fascicles in the lamina propria expressed immunoreactivity to neurone cell adhesion molecule, neurone-specific beta tubulin and protein gene product 9.5. Some neurones expressed growth-associated protein 43 (GAP43): and a number of those also expressed neurone-specific beta tubulin-immunoreactivity. Some axon fascicles were double labelled for those two proteins. The G-protein alpha subunits Gi and Go, involved in the signal transduction pathway, showed immunoreactivity in the sensory cell layer. Our results demonstrate that the canine vomeronasal organ contains a population of cells that expresses several neuronal markers. Furthermore, GAP43 immunoreactivity suggests that the sensory epithelium is neurogenic in adult dogs.

Animals↗