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PubMedDate not supplied

Immunoelectron-microscopic localization of synaptophysin in the organ of Corti of the guinea pig.

Synaptophysin has been localized previously in the mammalian cochlea at the light-microscopic level and in few reports by electron microscopy using either a preincubation procedure or the avidin-biotin reaction. Here we present results of the electron-microscopic analysis for postembedding immunoreactivity of synaptophysin in the cochlea of the guinea pig of LR-White-embedded samples. Strong synaptophysin immunoreactivity is located in the cytoplasm of the efferent nerve endings at the base of inner and outer hair cells. Besides this, some antibodies to synaptophysin were also identified in the cytoplasm of outer hair cells. To get more information about the cellular content of synaptophysin, the density of the immunoreaction per square micrometer was determined for the outer hair cells of the second turn of the cochlea counting the gold particles in numerous ultrathin sections. The role of synaptophysin identified in the cytoplasm of outer hair cells is discussed.

Animals↗
PubMed1998

Synaptophysin immunoreactivity in the cat cochlear nuclei.

The presence of synaptophysin, a presynaptic Ca2+ binding glycoprotein, has been analyzed in the cochlear nucleus complex of the adult cat using an antisynaptophysin monoclonal antibody. Synaptophysin immunoreactivity was differently distributed between regions of cochlear nuclei. Terminal boutons contacting directly with neurons (cell bodies and dendrites) or in the neuropil of ventral and dorsal cochlear nuclei appeared immunostained. In the ventral cochlear nucleus, synaptophysin-labelled boutons were clearly defined in contact with spherical, globular, multipolar, octopus and cochlear-nerve root neurons. However, the dorsal cochlear nucleus showed a dense immunostained network of synaptophysin-labelled puncta, inside which some neuron cell bodies were observed. The present findings show a differential distribution of synaptophysin-immunostained boutons between the ventral and the dorsal cochlear nuclei of the cat. The present description of the different synaptophysin-labelled terminal boutons in the cochlear nuclei complex and their pattern of distribution, will be useful for further studies on development, degeneration or regeneration of the peripheral auditory pathway.

Animals↗
PubMed1991

Synaptophysin. A widespread constituent of small neuroendocrine vesicles and a new tool in tumor diagnosis.

Synaptophysin, a vesicular integral membrane protein, is specifically expressed in neuroendocrine tissues. According to cDNA cloning studies, it has a molecular weight of 33,300 Dalton, one potential N-glycosylation site at the vesicle inside, four major hydrophobic domains as well as a C-terminus containing approximately 90 amino acids. The C- and N-termini of synaptophysin are located on the cytoplasmic side of the vesicle membrane. No signal sequence is found. Transfection of non-neuroendocrine cells with synaptophysin cDNA leads to the synthesis of synaptophysin-containing vesicles, which contain this protein in highly enriched form and have biophysical properties similar to presynaptic vesicles of neurons. So far, the vesicular content has only been determined in rat neurons, where classical neurotransmitters such as biogenic amines and transmitter-active amino acids were found. Reconstitution of the purified protein in liposomes suggests a possible channel function of synaptophysin. Using mono- and polyvalent antibodies against synaptophysin, a considerable number of studies in several laboratories have shown that this protein is a reliable marker molecule for neuroendocrine tumors of various degrees of differentiation.

Adenoma, Islet Cell↗
PubMed1995

Overexpression of synaptophysin enhances neurotransmitter secretion at Xenopus neuromuscular synapses.

Previous studies have suggested the importance of synaptophysin (p38), a major integral membrane protein of the synaptic vesicle, in transmitter secretion, but few have directly addressed its functional role at intact synapses. In the present study, injection of synthetic mRNA for synaptophysin into one of the early blastomeres of a Xenopus embryo resulted in elevated synaptophysin expression in 1 and 2 d embryos and in cultured spinal neurons derived from the injected blastomere, as shown by immunocytochemistry. At neuromuscular synapses made by neurons overexpressing synaptophysin [p38(+)] in 1 d cell cultures, the spontaneous synaptic currents (SSCs) showed a markedly higher frequency, as compared to control synapses. This increase in frequency was not accompanied by a change in the mean amplitude or the amplitude distribution of the SSCs, suggesting that synaptophysin is not involved in determining the size of transmitter quanta. The impulse-evoked synaptic currents (ESCs) of synapses made by p38(+) neurons showed increased amplitude as well as reduced fluctuation and delay of onset of ESCs. Under high-frequency tetanic stimulation at 5 Hz, the rate of tetanus-induced depression was faster for p38(+) neurons. Taken together, these results suggest a role for synaptophysin in the late steps of transmitter secretion, affecting the probability of vesicular exocytosis and/or the number of synaptic vesicles initially docked at the active zone.

Animals↗
PubMed1992

Widespread Distribution of Synaptophysin, a Synaptic Vesicle Glycoprotein, in Growing Neurites and Growth Cones.

Synaptophysin, a 38-kD glycoprotein, is one of the most abundant of the integral membrane proteins of small synaptic vesicles. The protein is widely distributed at synapses throughout the nervous system, where it is believed to be involved in the exocytosis of stored neurotransmitter. We show here that synaptophysin is also widely expressed in growing neurites and growth cones both in vitro and in vivo. In dissociated rat cerebral cortical cultures anti-synaptophysin antiserum (G-95) stains growth cones punctately as soon as they emerge from the cell body. In early cultures all neurites are immunoreactive. Later, synaptophysin is redistributed to become concentrated in axonal varicosities. In developing rat embryos, synaptophysin is expressed in the growing axons of, for instance, the spinal commissural interneurons and the parallel fibres of the cerebellar granule cells long before these neurons have established synaptic connections. These observations suggest that synaptic vesicle proteins like synaptophysin are functionally important in neuronal development.

Journal Article↗
PubMed1996

Distributions of two homologous synaptic vesicle proteins, synaptoporin and synaptophysin, in the mammalian retina.

Synaptophysin and synaptoporin are homologous proteins that are among the most abundant synaptic vesicle proteins. Despite their high degree of sequence similarity, they are differentially distributed in the brain. The distribution of synaptophysin and synaptoporin was examined in the adult rat and rabbit retina by using single- and double- labeling immunocytochemistry with conventional light microscopy and confocal laser scanning microscopy. In the rat retina, synaptophysin immunoreactivity was found in the outer plexiform layer in terminals of photoreceptors and was homogeneously distributed throughout the inner plexiform layer. Synaptoporin immunoreactivity, however, was restricted to the inner plexiform layer. Labeling was most prominent in three distinct bands of the inner plexiform layer separated by two bands of very low synaptoporin immunoreactivity. In the rabbit retina, synaptophysin and synaptoporin immunoreactivity were found in the inner and outer plexiform layers. In the inner plexiform layer, labeling for both vesicle proteins was homogeneous, with no detectable stratification. In the outer plexiform layer, synaptophysin was present in photoreceptor terminals, and synaptoporin was present in horizontal cells. Staining of isolated rabbit retinal cells confirmed that both the axonless A type and the axon-bearing B type horizontal cells are immunoreactive for synaptoporin. In addition, electron microscopy of synaptoporin-immunostained rabbit retinas revealed no labeling of photoreceptor terminals but of putative synaptic sites in horizontal cells in the outer plexiform layer. No functional correlation was found in the expression of either synaptic vesicle protein with the type of neuron or synapse (ribbon or conventional).

Animals↗
PubMed1993

Synaptophysin has a selective distribution in early endosomes of PC12 cells.

We have studied the endocytic pathway in PC12 cells and localized synaptophysin to a subpopulation of early endosomes. Endocytosis was examined by electron microscopy using horseradish peroxidase as an endocytic tracer. Immediately following brief incubations with horseradish peroxidase, label was seen in small vesicles and tubules which appeared to be part of the tubular early endosomal network. A large vacuolar structure, containing a rim of horseradish peroxidase reaction product and an electron-lucent central region, was also labelled at the earliest time point examined. Within 5 min after the horseradish peroxidase pulse, reaction product was seen in multivesicular bodies. After prolonged chase periods, horseradish peroxidase label was lost from the early endosomal structures and accumulated in large dense vesicles containing lamellar stacks of membranes. The observed pattern of horseradish peroxidase distribution is consistent with delivery of the tracer into tubular and vacuolar early endosomes with subsequent movement of horseradish peroxidase out of these compartments and into lysosomes. Examination of synaptophysin distribution by EM immunocytochemistry following incubations with horseradish peroxidase revealed selective immunogold labelling of early endosomal structures. Notably, small vesicular and tubular profiles were frequently double-labelled while vacuolar early endosomes were only rarely labelled for synaptophysin. Immunocytochemical labelling was not observed in multivesicular bodies or large dense vesicles with lamellar stacks. Results of experiments in which endosomal structures were immunoprecipitated with antibody to synaptophysin were consistent with the immunocytochemical findings. Maximal recovery of endocytosed horseradish peroxidase activity was seen immediately following the horseradish peroxidase pulse, and a significant decrease was seen after brief chase periods. These results indicate the presence of synaptophysin in vesicles and tubules of the early endosomal compartment.

Animals↗
PubMed1990

Immunohistochemical localization of synaptophysin (p38) in the pineal gland of the Mongolian gerbil (Meriones unguiculatus).

Synaptophysin (protein p38), a major integral membrane glycoprotein of small presynaptic vesicles, was localized immunohistochemically in semithin sections of the superficial pineal gland of the Mongolian gerbil (Meriones unguiculatus). Synaptophysin immunoreactivity could be detected in all pinealocytes, which were visualized with antibodies directed against neuron-specific enolase (NSE) in adjacent sections. No p38 immunoreactivity was discernible in the interstitial glial cells, which showed a heterogeneous pattern of immunostaining for the intermediate filament proteins glial fibrillary acidic protein (GFAP) and vimentin. Pinealocytes exhibited considerable intercellular differences in the densities of immunostaining. The various degrees of synaptophysin immunoreactivities in pinealocytes were not correlated with the densities of NSE immunostaining. Nerve terminals and varicosities displayed stronger immunoreactivities than pinealocytes. They were particularly numerous in the perivascular spaces. It is not clear whether this distribution indicates an innervation of pineal capillaries in addition to the functionally important innervation of pinealocytes. Several highly p38-positive dots of variable size were a conspicuous feature throughout the gland. By the consecutive semithin-thin section technique, they could be identified as processes of pinealocytes, filled with accumulations of small clear vesicles. Obviously, these vesicles represent the major site of synaptophysin immunoreactivity in pinealocytes. In the gerbil, similar vesicles have been ascribed a role in the secretory activity of the gland, and/or in the transport of calcium. The intercellular differences in the degrees of p38 immunostaining may, therefore, reflect different states of a specific cellular activity. The presence of synaptophysin in pinealocytes of the normal pineal, including the deep portions of the gland, emphasizes the paraneuronal character of these cells.

Animals↗
PubMed2006

Tactile stimulation-induced rapid elevation of the synaptophysin mRNA expression level in rat somatosensory cortex.

Synaptophysin is an integral membrane protein abundant in the synaptic vesicle and is found in nerve terminals throughout the brain. It was recently suggested that synaptophysin is also involved in the modulation of activity-dependent synapse formation. In this study, we examined at the individual level whether tactile stimulation selectively influenced the synaptophysin mRNA expression level in the somatosensory cortex of rats. Anesthetized rats were caressed on the back by an experimenter's palms for 20 min and the mRNA expression levels in the somatosensory and the visual cortices 5 min afterwards were determined using quantitative PCR methodology. The synaptophysin mRNA expression level was selectively higher in the experimental group than in the control group in the somatosensory cortex but not in the visual cortex. This suggests that the mRNA expression level of synaptophysin induced by neuronal activity is related to the regulation of synapse formation or remodeling or both.

Animals↗
PubMed1989

Expression of synaptophysin in the rat pheochromocytoma cell line PC12.

Expression of the integral membrane protein of small synaptic vesicles, synaptophysin, was investigated in the pheochromocytoma cell line PC12 using a quantiative dot immunoassay. Specific synaptophysin contents of the cultures varied with cell density, high levels being observed in densely seeded dishes and/or after some days of subculturing. Northern blot analysis revealed these cell density-related changes in synaptophysin protein contents to result partly from corresponding alterations in mRNA levels. Treatment with nerve growth factor (NGF), but not with various other effectors of intracellular messenger systems, inhibited both synaptophysin and DNA accumulation in the cultures. These data indicate that synaptophysin expression is high in densely proliferating PC12 cells and uncoupled from process formation and neuronotypic differentiation induced by NGF.

Animals↗
PubMed1991

Reactive synaptogenesis assessed by synaptophysin immunoreactivity is associated with GAP-43 in the dentate gyrus of the adult rat.

Reactive synaptogenesis and terminal proliferation are known to occur in the dentate gyrus of the rat hippocampus following removal of specific afferents. In the present study we have examined the relation of synaptophysin immunoreactivity to the immunohistochemical staining pattern of GAP-43, a putative marker of neuritic growth. Within the molecular layer of the normal dentate gyrus, synaptophysin immunolabeling shows a trilaminar pattern, with the inner and outer layers having the greatest density of staining. Within the first week following denervation, there was a significant decrease in the staining density in the outer two-thirds of the molecular layer, followed by a moderate recovery at 14 days and 80% recovery by 30 days. This pattern is consistent with the time course of denervation and reinnervation in this system as determined previously by electron microscopy. By comparison, the staining pattern for GAP-43 in the intact dentate gyrus showed the middle and outer thirds of the molecular layer to be less densely stained than the inner third. Within a week following deafferentation, the outer two-thirds of the molecular layer displayed decreased levels of GAP-43 immunoreactivity, followed by recovery to normal levels by 30 days. By 84 days postlesion, patterns of both synaptophysin and GAP-43 immunostaining reflected an increased width of the inner molecular layer. Laser confocal imaging of double-immunolabeled sections at 14 days postlesion showed a 370% increase in the number of GAP-43-positive terminals in the molecular layer as compared to unoperated controls. Many of these GAP 43-positive terminals were synaptophysin negative. We conclude that GAP-43 may play a role in the synaptic remodeling that occurs in the denervated rat hippocampus and that quantitative morphometry of synaptophysin immunolabeling accurately reflects the fate of presynaptic terminals in this model of degeneration and reinnervation.

Animals↗
PubMed1996

Sensory cells of the chick cochlea express synaptophysin.

Previous evidence has shown expression of synaptophysin by sensory cells of the auditory and vestibular systems in the human, but not in other mammalian species. Using a monoclonal antibody, SBI 20.10, we investigated the expression of synaptophysin in the sensory cells of the avian cochlea. We present immunohistochemical data showing synaptophysin expression by cochlear hair cells in both late stage embryos and adult chickens. Immunoblotting of cochleae confirmed an antigen with an apparent molecular weight appropriate for synaptophysin that increases with development. Immunoreactivity in the apex of the cochlea occurred in hair cells on both neural and abneural sides, whereas immunoreactivity in the base of the cochlea was relegated to hair cells on the neural side. These observations indicate that, in the avian auditory system, like the human, synaptophysin is expressed in the sensory cells of both the embryo and adult.

Age Factors↗
PubMed1987

Synaptophysin immunoreactivity and small clear vesicles in neuroendocrine cells and related tumours.

Synaptophysin (protein p38) immunoreactivity has been detected immunohistochemically in neuroendocrine cells of the human adrenal medulla, carotid body, skin, pituitary, thyroid, lung, pancreas and gastrointestinal mucosa as well as in 87 out of 93 neuroendocrine tumours investigated, including pheochromocytomas, chromaffin and non-chromaffin paragangliomas, ganglioneuromas, pituitary adenomas, thyroid medullary carcinomas, parathyroid adenomas, lung carcinoids and neuroendocrine carcinomas, pancreatic and gut endocrine tumours and cutaneous merkelomas. Parallel ultrastructural investigation of synaptophysin-reactive cells and tumours revealed the presence, in addition to dense-cored, secretory granules, of a population of pleomorphic, small, clear vesicles resembling synaptic vesicles of nerve terminals as well as the synaptophysin immunoreactive vesicles already described in rat adrenal medullary and pituitary cells. Synaptophysin immunoreactivity showed several differences in its distribution among tumour and non-tumour endocrine cells when compared to chromogranin A immunoreactivity, a well known marker of the core of endocrine granules. Synaptophysin represents a reliable general marker of neuroendocrine cells and tumours, which may be useful in diagnostic histopathology.

Chromogranin A↗
PubMed2006

Bone marrow stromal cells upregulate expression of bone morphogenetic proteins 2 and 4, gap junction protein connexin-43 and synaptophysin after stroke in rats.

Bone morphogenetic proteins play a key role in astrocytic differentiation. Astrocytes express the gap junctional protein connexin-43, which permits exchange of small molecules in brain and enhances synaptic efficacy. Bone marrow stromal cells produce soluble factors including bone morphogenetic protein 2 and bone morphogenetic protein 4 (bone morphogenetic protein 2/4) in ischemic brain. Here, we tested whether intra-carotid infusion of bone marrow stromal cells promotes synaptophysin expression and neurological functional recovery after stroke in rats. Adult male Wistar rats were subjected to 2 h of right middle cerebral artery occlusion. Rats were treated with or without bone marrow stromal cells at 24 h after middle cerebral artery occlusion via intra-arterial injection (n=8/group). A battery of functional tests was performed. Immunostaining of 5-bromo-2-deoxyuridine, Ki67, bone morphogenetic protein 2/4, connexin-43, synaptophysin, glial fibrillary acidic protein, neuronal nuclear antigen, and double staining of 5-bromo-2-deoxyuridine/glial fibrillary acidic protein, 5-bromo-2-deoxyuridine/neuronal nuclear antigen, glial fibrillary acidic protein/bone morphogenetic protein 2/4 and glial fibrillary acidic protein/connexin-43 were employed. Rats treated with bone marrow stromal cells significantly (P<0.05) improved functional recovery compared with the controls. 5-Bromo-2-deoxyuridine and Ki67 positive cells in the ipsilateral subventricular zone were significantly (P<0.05) increased in bone marrow stromal cell treatment group compared with the controls, respectively. Administration of bone marrow stromal cells significantly (P<0.05) promoted the proliferating cell astrocytic differentiation, and increased bone morphogenetic protein 2/4, connexin-43 and synaptophysin expression in the ischemic boundary zone compared with the controls, respectively. Bone morphogenetic protein 2/4 expression correlated with the expression of connexin-43 (r=0.84, P<0.05) and connexin-43 expression correlated with the expression of synaptophysin (r=0.73, P<0.05) in the ischemic boundary zone, respectively. Administration of bone marrow stromal cells via an intra-carotid route increases endogenous brain bone morphogenetic protein 2/4 and connexin-43 expression in astrocytes and promotes synaptophysin expression, which may benefit functional recovery after stroke in rats.

Analysis of Variance↗
PubMed2004

Growth-associated protein 43 (GAP-43) and synaptophysin alterations in the dentate gyrus of patients with schizophrenia.

Growth-associated protein 43 (GAP-43) expression is critical for the proper establishment of neural circuitry, a process thought to be disrupted in schizophrenia. Previous work from our laboratory demonstrated decreased GAP-43 levels in post-mortem tissue from the entire hippocampal formation of affected individuals. In the present study, we used immunocytochemical techniques to localize alterations in GAP-43 protein to specific synapses. GAP-43 distribution was compared to that of synaptophysin, another synaptic protein known to be altered in schizophrenia. The levels and distribution of GAP-43 and synaptophysin proteins were measured in the dentate gyrus of subjects with schizophrenia and sex-, age-, and postmortem interval-matched normal controls and subjects with bipolar disorder. Tissue from subjects was provided by the Harvard Brain Tissue Resource Center. In control subjects, GAP-43 immunostaining was prominent in synaptic terminals in the inner molecular layer and hilar region. Subjects with schizophrenia had significant decreases in GAP-43 immunoreactivity in the hilus (p<0.05, paired t-test) and inner molecular layer (p<0.05, paired t-test) but not in the outer molecular layer. In the same tissues, synaptophysin immunoreactivity was significantly reduced in both the inner and outer molecular layers of the dentate gyrus (both p<0.01 by paired t-test), but not in the hilus. In contrast to patients with schizophrenia, GAP-43 and synaptophysin levels in subjects with bipolar disorder did not differ from controls. Given the relationship of GAP-43 and synaptophysin with the development and plasticity of synaptic connections, the observed alterations in the hippocampus of patients with schizophrenia may be related to cognitive deficits associated with this illness.

Adult↗
PubMed1998

Differential ultrastructural distribution of synapsin and synaptophysin proximal to a ligation in bovine splenic nerve.

Synaptophysin and synapsin, closely correlated on synaptic vesicles in terminals, may show a differential distribution at synapse formation and maturation. In order to disclose the fine structural details of these differences, synapsin and synaptophysin distribution was studied by immunocytochemistry on ligated bovine splenic axons in vitro and compared with terminals in the vas deferens. In the synaptic differentiations taking place proximally synapsin could only be detected on the accumulating elements of the axonal reticulum. Large dense granules and clusters of small synaptic vesicles were negative. Synaptophysin was restricted to these clusters. In the vas deferens, co-localization of synapsin and synaptophysin could be seen on small vesicles. From their formation small synaptic vesicles carry synaptophysin. Synapsin may be involved in the dynamic membrane changes taking place at the ligation. At a functional terminal, synapsin shifts to small synaptic vesicles.

Animals↗
PubMed1998

Determination of synapsin I and synaptophysin in body fluids by two-site enzyme-linked immunosorbent assays.

Two-site enzyme-linked immunosorbent assays (ELISA) have been established for the specific and sensitive determination of two membrane proteins of the small synaptic vesicles (SSV), namely: peripheral synapsin I and integral synaptophysin. The ELISA used highly specific capture monoclonal antibodies (mAB) and polyclonal antibodies (pAB) as detectors. For synapsin I, the mAB were newly generated, whereas for synaptophysin, the commercially available mAB SY38 was applied. In order to calibrate the ELISA and to raise pAB, both proteins were purified in the mg-range. Synapsin I was purified by conventional means from human and porcine brain and synaptophysin was purified by immunoaffinity chromatography from porcine brain. Using the ELISA, neither synapsin I nor synaptophysin could be determined in serum or cerebrospinal fluid (CSF) from healthy donors or patients suffering various neurological disorders or pheochromocytomas. For this reason, the degradation of both proteins in serum and CSF was investigated. With the exception of synaptophysin measured in serum, both proteins exhibited fast rates of degradation. Despite the negative results in human body fluids, the two ELISA are appropriate for the quantification of these membrane proteins in neuronal or neuroendocrine cell extracts or preparations of SSV.

Amino Acid Sequence↗
PubMed1999

Synaptophysin is phosphorylated in rat cortical synaptosomes treated with botulinum toxin A.

Phosphorylation and dephosphorylation of neuronal proteins have been implicated in regulation of synaptic transmission. Studies were performed to determine if synaptophysin was phosphorylated or dephosphorylated during exposure of synaptosomes to botulinum toxin A (BoTX/A). Cholinergic-enriched synaptosomes were preincubated in the presence of 3H-choline to label newly synthesized acetylcholine (3H-ACh). This was followed by incubation with low or high potassium to stimulate release of newly synthesized 3H-ACh. BoTX/A inhibited total Ach release by 15-19% and inhibited release of newly synthesized 3H-ACh by 35%. A 165% increase in synaptophysin phosphorylation occurred in a dose-dependent manner over a range of doses (0.2 nM, 2 nM, 20 nM, 100 nM) of BoTX/A. When 4-Aminopyridine was added to synaptosomes that were BoTX/A treated, synaptophysin was dephosphorylated to control levels. Synaptosomes incubated with BoTX/A exhibited an inhibition of potassium stimulated ACh release and an increase in synaptophysin phosphorylation. Synaptophysin phosphorylation may be involved in inhibition of acetylcholine release.

4-Aminopyridine↗