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PubMed2006

Synapsin I Cre transgene expression in male mice produces germline recombination in progeny.

The cre/LoxP system can produce conditional loss of gene function in specific cell types such as neurons. A transgenic mouse line, utilized by multiple studies, used the Synapsin I promoter to drive expression of cre (SynCre) to achieve neuronal-specific cre expression. Herein we describe that cre expression can also be observed in SynCre mice within the testes after being bred into a floxed transgenic mouse line. Cre transcript was expressed in testes resulting in recombination of the floxed substrate in testes. In the majority of cases, progeny of male SynCre mice inherited a germline recombined floxed allele, while this was never observed in progeny from female mice carrying the SynCre allele. This observation should alert investigators to a potential confound using these mice and enables male germ cell "deletor" strategies.

Animals↗
PubMed1994

Matrix-assisted laser desorption mass spectrometric peptide mapping of proteins separated by two-dimensional gel electrophoresis: determination of phosphorylation in synapsin I.

A technique is described for the rapid, sensitive analysis of posttranslational modifications of proteins that have been separated by 2-dimensional electrophoresis and blotted onto a membrane with a cationic surface. The isolated protein spots visualized by reverse staining of the blotting membrane are excised, washed, and subjected to chemical (cyanogen bromide) and/or enzymatic (endoproteinase Lys-C) degradation directly on the membrane. The resulting mixture of peptide fragments is extracted from the membrane into a solution that is compatible with matrix-assisted laser desorption mass spectrometric analysis and analyzed without fractionation. Relatively accurate (+/- 1 Da) mass determination of these peptide fragments provides a facile and sensitive means for detecting the presence of modifications and for correlating such modifications with the differential mobility of different isoforms of a given protein during 2-dimensional electrophoresis. The technique is applied to the determination of sites of phosphorylation in synapsins Ia and Ib, neuronal phosphoproteins that are believed to function in the regulation of neurotransmitter release and are substrates for cAMP and Ca2+/calmodulin-dependent protein kinases, which appear to control their biological activity.

Amino Acid Sequence↗
PubMed1995

Expression of synapsin I gene in primary cultures of differentiating rat cortical neurons.

Synapsin I is a neuron-specific protein which is present in two isoforms, Ia and Ib. In the last few years this protein has been demonstrated to play a central role in the regulation of neurotransmitter release and synaptic plasticity. In this paper the developmental expression of this protein has been investigated in primary neuronal cultures from fetal rat brain cortices. The presence of thyroid hormone in the culture medium stimulates an early expression of the protein without exerting any effect at the level of mRNA transcription and accumulation. These observations implicate a T3-dependent regulation of this neuron-specific gene at the level of mRNA translation.

Animals↗
PubMed1986

Stimulation of synapsin I phosphorylation in synaptosomes by convulsants.

Pentylenetetrazole markedly enhanced synapsin I (previously referred to as protein I) phosphorylation and synaptosomal uptake of Ca2+. Picrotoxin and strychnine sulfate caused a slight increase in the phosphorylation and no significant increase in Ca2+ uptake. The data indicate that pentylenetetrazole appears to influence this process.

Animals↗
PubMed1987

Identification of a new 84/82 kDa calmodulin-binding protein, which also interacts with actin filaments, tubulin and spectrin, as synapsin I.

A new 84/82 kDa calmodulin-binding protein, which also interacts with actin filaments, tubulin and spectrin, was purified from the bovine synaptosomal membrane. The binding of calmodulin to this protein was Ca2+-dependent, and was inhibited by trifluoperazine, the association constant being calculated to be 2.2 X 10(6) M-1. Maximally, 1 mol of calmodulin bound to 1 mol of the purified protein. This protein was phosphorylated by both kinase II (Ca2+- and calmodulin-dependent kinase) and cyclic AMP-dependent kinase. In addition, antibody against this protein was demonstrated to have an immunological crossreactivity with synapsin I in the synaptosomal membrane.

Actins↗
PubMed1991

Synapsin I phosphorylated by Ca2+, calmodulin-dependent protein kinase II is able to self-degrade.

Phosphorylation of the neurospecific protein synapsin I (SI) by various cellular protein kinases was studied. The analysis of functional properties of phosphosynapsins showed that in the case of PK II-mediated modification of the protein, it becomes capable of self-degradation. The latter process was found to be specific and did not appear to be characteristic of the phosphoforms emerging after the protein modification by PK C or PK A. A possible involvement of the process in the regulation of neurotransmitter secretion is discussed.

Animals↗
PubMed1995

beta-Bungarotoxin blocks phorbol ester-stimulated phosphorylation of MARCKS, GAP-43 and synapsin I in rat brain synaptosomes.

The phospholipase A2 neurotoxin, beta-bungarotoxin, presynaptically blocks acetylcholine release. Its mechanism of action is unknown; however, our previous studies suggest that it inhibits phosphorylation of synaptosomal proteins, which might be expected to decrease neurotransmitter release. In our present study, we found that 1 nM beta-BuTX blocked phorbol ester-stimulated phosphorylation of GAP-43, MARCKS and synapsin I without affecting their basal phosphorylation. In contrast, a 1 nM concentration of the non-neurotoxic enzyme. Naja naja atra phospholipase A2 did not affect the phorbol ester-stimulated phosphorylation of these proteins but increased the basal phosphorylation of GAP-43 and MARCKS. Although it has been suggested that cytosolic calmodulin is increased by phosphorylation of the protein kinase C substrates, GAP-43 and MARCKS, we found no change in calmodulin levels by phorbol ester or beta-bungarotoxin. The stimulation of phosphorylation by Naja naja atra phospholipase A2 may be due to products liberated as a result of its phospholipase A2 activity. In contrast, the inhibition of phosphorylation by beta-bungarotoxin appears to be due to an action which may be unrelated its relatively weak phospholipase A2 activity. Inhibition of phosphorylation by beta-bungarotoxin is a possible mechanism by which it could block acetylcholine release. Furthermore, beta-bungarotoxin may be a useful tool to study the physiological role of phosphorylation of synaptosomal proteins in neurotransmitter release.

Animals↗
PubMed1996

Long-term regulation of synapsin I gene expression and neuronal morphology by cyclic AMP and low-dose staurosporine.

We examined the phenotypic changes of neuroblastoma cells chronically treated with cAMP and nanomolar concentrations of staurosporine. These agents, given together, produced cells with a neuronal morphology and a delayed increase (approximately 10 days) in synapsin I mRNA levels. Dopamine-beta hydroxylase mRNA was upregulated within 24 h. We provide evidence that low-dose staurosporine acts cooperatively with cyclic AMP in the acquisition of mature neuronal phenotypes.

Adenylyl Cyclases↗
PubMed1995

Increase in synapsin I phosphorylation implicates a presynaptic component in septal kindling.

Synaptic plasticity in the CNS is thought to be an important component of learning and memory. Kindling is an animal model of synaptic plasticity in which repetitive local electrical stimulation eventually leads to a generalized motor seizure. Once established, the sensitivity of kindled animals to this epileptic condition is long-lasting. An increase in synaptic efficacy appears to underlie the plastic changes observed in kindling but the molecular mechanisms involved remain unknown. Here we demonstrate that the phosphorylation state of synapsin I, a synaptic vesicle-associated protein which has been implicated in the regulation of neurotransmitter release, is significantly increased in hippocampus and parietal cortex of rats two weeks after the establishment of septal kindling. Furthermore, K(+)-evoked release of L-glutamate is significantly increased in synaptosomes prepared from cerebral cortex of kindled animals. Thus, changes within the presynaptic nerve terminal may contribute, at least in part, to the long-lasting modification in neuronal function induced by kindling.

Animals↗
PubMed1989

Synaptophysin and synapsin I as tools for the study of the exo-endocytotic cycle.

Synaptophysin, an integral protein of the synaptic vesicle membrane, and synapsin I, a phosphoprotein associated with the cytoplasmic side of synaptic vesicles, represent useful markers that allow to follow the movements of the vesicle membrane during recycling. The use of antibodies against these proteins to label nerve terminals during experimental treatments which stimulate secretion has provided evidence that during the exo-endocytotic cycle synaptic vesicles transiently fuse with the axolemma, from which they are specifically recovered. When recycling is blocked, exocytosis leads to the permanent incorporation of the synaptic vesicle membrane into the axolemma and to diffusion of the vesicle components in the plane of the membrane.

Animals↗
PubMed2004

Localization of synapsin-I and PSD-95 in developing postnatal rat cerebellar cortex.

The comparative localization of two prominent synaptic proteins, synapsin-I (Syn-I) and PSD-95, was investigated in slices of developing (P3-P21) rat cerebellar cortex using double- or triple-label fluorescence immunohistochemistry and confocal microscopy. During the first postnatal week, Syn-I and PSD-95 immunoreactive (IR) puncta were strongly concentrated in the Purkinje cell layer (PCL) where they circumscribed irregularly shaped PC somata, forming pericellular nests that likely correspond to early climbing fiber synapses. PSD-95 and Syn-I puncta also were found along the shafts and at the tips of growing PC dendrite branches labeled with calbindin. During the second postnatal week, synaptic puncta were lost from the PC layer, while many new puncta were added to the molecular layer (ML). At P10, about half of the PCs were circumscribed by PSD-95 or Syn-I puncta, whereas at P14 no PCs were circumscribed. By P14, PSD-95 and Syn-I became most strongly localized to many small puncta in the ML and to large clusters at mossy fiber rosettes in the glomerular layer (GL) where PSD-95 often encircled Syn-I clusters. Some large clusters in the GL contained only PSD-95 or Syn-I, but not both, suggesting differential growth or remodeling of pre- and post-synaptic structures. No PSD-95 staining of pre-synaptic terminal pinceau was observed during the first 3 weeks of postnatal development. Thus, in relation to PCs, there is a developmental shift in PSD-95 localization whereby, first, it is concentrated on PC cell bodies and short dendrites (P3-P7), then it is lost on PC cell bodies (P7-14) and becomes localized almost exclusively to PC dendrites (P14-P21).

Animals↗
PubMed2002

Characterization of the murine Timp4 gene, localization within intron 5 of the synapsin 2 gene and tissue distribution of the mRNA.

Tissue inhibitor of matrix metalloproteinases type 4 (TIMP-4), the newest member in the mammalian TIMP family of inhibitors of matrix metalloproteinases (MMPs), differs from the other three TIMPs by its restricted expression pattern. This suggests that TIMP-4 could play a role in tissue-specific regulation of extracellular matrix (ECM) turnover. To define this role, modulation of TIMP-4 production by overexpression, aberrant expression and inactivation of the Timp4 gene in transgenic mice should be performed. In preparation for such experiments we have cloned and characterized the murine Timp4 gene and determined the tissue distribution of its mRNA in mice. The gene spans 7.1 kb, consists of five exons and shares considerable homology with the other Timp genes. The gene is located on mouse chromosome 6 in an antisense orientation between exons 5 and 6 of the mouse synapsin 2 (Syn2) gene. A similar organization is common to all four human/mouse TIMP and SYN genes and to the single synapsin/Timp locus in Drosophila. The highest levels of TIMP-4 mRNA were seen in postnatal mouse heart, ovary and brain. Determination of the spatial expression pattern of TIMP-4 mRNA by in situ hybridization in the heart revealed a diffuse distribution in cardiac muscle cells. In the ovary, cyclic variation was observed in TIMP-4 mRNA levels. In situ hybridization demonstrated the strongest expression of TIMP-4 mRNA in the corpus luteum. The data suggest that TIMP-4 plays a role in the normal physiology of the heart and the ovary, most likely related to maintenance of the delicate balance between MMPs and TIMPs.

Animals↗
PubMed2003

Duplication, degeneration and subfunctionalization of the nested synapsin-Timp genes in Fugu.

The genes encoding synapsin (Syn) and the tissue inhibitor of metalloproteinase (Timp) exhibit a nested organization that is conserved in fruit fly and vertebrates. Analysis of the human and Fugu genomes show that the evolution of Syn-Timp gene families is characterized by duplications, secondary loss and the partitioning of ancestral functions. Of particular interest are two duplicate Syn-Timp loci in Fugu that have accumulated complementary degenerate mutations such that each Syn duplicate produces one of the two transcripts generated from the single ancestral gene, and one of the Timp genes is lost.

Alternative Splicing↗
PubMed2000

Translocational changes of localization of synapsin in axonal sprouts of regenerating rat sciatic nerves after ligation crush injury.

Time-dependent translocational changes of Synapsin I (SyI), a synaptic vesicle-associated phosphoprotein and its involvement in the axonal transport were investigated in the regenerating axonal sprouts. A weak SyI immunoreactivity (IR) was found in the axoplasm of normal axons. Rat sciatic nerves were crush-injured by ligating with 1-0 silk thread at the mid-thigh level and released from the ligation 24 h later. At various times after release, immunocytochemistry was performed. SyI was translocated from the proximal to the distal site of ligation and also involved in the sprouting of regenerating axons. The distribution patterns of SyI IR were changed in the crush-injured nerves. SyI immunoreactive thin processes were strongly appeared in the proximal region from 1 h after release. After 3 h, a very strong IR was expressed. The intense SyI immunoreactive thin processes were elongated distally and were changed the distribution pattern by time-lapse. After 12 h, strong immunoreactive processes were extended to the ligation crush site. At 1 day, a very intense IR was expressed. At 2 days, immunoreactive thin processes extended into the distal region over the ligation crush site and strong IR was observed after 3 days. SyI was accumulated in the proximal region at the early phases after release. These results suggest that SyI may be related to the translocation of vesicles to the elongated membranes by a fast axonal transport in the regenerating sprouts.

Animals↗
PubMed1988

Secretory function of the vestibular nerve calyx suggested by presence of vesicles, synapsin I, and synaptophysin.

Type I sensory hair cells of the vestibular epithelium are nearly completely ensheathed by an afferent nerve ending, the vestibular nerve calyx. We have recently reported that the nerve calyx, and, in particular, its apical portions surrounding the neck of the hair cell, are immunoreactive for synapsin I (Favre et al., 1986), a major membrane component of small synaptic vesicles of axonal endings. We have now found, by electron microscopy, that the same region of the calyx is densely populated by microvesicles morphologically similar to typical presynaptic small synaptic vesicles. Furthermore, we have established by light microscopy immunocytochemistry that this region of the calyx also contains a high concentration of synaptophysin, another well-characterized major component of small synaptic vesicle membranes. These results suggest that the upper portion of the calyx is equipped with the machinery that in presynaptic terminals is involved in the release of neurotransmitters and raise the possibility that the calyx, via secretion of neurotransmitterlike substances, might modulate the function of type I hair cells.

Animals↗