Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “colocalization”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 289 records · Page 16Linked to original sources
PubMedDate not supplied

Substance P and neurokinin A are codistributed and colocalized in the porcine gastrointestinal tract.

Immunoreactive substance P and neurokinin A were measured with radioimmunoassay in extracts of different segments of porcine gastrointestinal tract using C-terminally directed antisera. In all segments, the concentrations of substance P and neurokinin A were similar. The largest concentrations of both peptides were found in the mid-colon. By gel chromatography and reversed-phase high pressure liquid chromatography the immunoreactivity in extracts from ileum eluted as homogenous peptides at the positions of synthetic substance P and neurokinin A, respectively. No neurokinin B was found. By immunohistochemistry of porcine duodenum, jejunum, ileum and mid-colon, identical localization patterns were found for substance P and neurokinin A, and the two peptides demonstrated by double immunofluorescence to be colocalized in the enteric nervous system of the ileum. We conclude that the tachykinins substance P and neurokinin A are codistributed and colocalized in the procine gastrointestinal tract and suggest that the two peptides are produced from a common precursor, beta- and/or gamma-preprotachykinin, in the same neurons.

Animals↗
PubMedDate not supplied

Colocalization of endothelin, vasopressin and serotonin in cultured endothelial cells of rabbit aorta.

The localization and colocalization of endothelin-1, arginine-vasopressin and serotonin in the endothelial cells of rabbit aorta in primary culture were investigated by preembedding and postembedding immunocytochemistry. These three substances were localized in the same population of cells, where they appeared in high proportions (greater than 60%). These findings indicate: 1) that the cell population is heterogeneous, and 2) that these substances are colocalized in some of the cultured endothelial cells. Double labeling in single cells has demonstrated the simultaneous presence of 1) endothelin and vasopressin, 2) vasopressin and serotonin, and 3) endothelin and serotonin. The immunolabeling dominated in the cytoplasmic matrix.

Animals↗
PubMed1993

Glucocorticoid receptor colocalization with pituitary hormones in the rat pituitary gland.

The presence of glucocorticoid receptor (GR) in the anterior lobe of the pituitary gland has previously been demonstrated, but the exact cell types expressing GR have not yet been characterized. In this study, we demonstrate the colocalization of GR and pituitary hormones in the rat pituitary gland by using an immunocytochemical double-labelling method. The majority of anterior lobe corticotropin-immunoreactive and growth hormone-immunoreactive cells contained GR-like immunoreactivity. Cells of the intermediate lobe showed intensive ACTH-like immunoreactivity but did not express GR. The glycoprotein hormones thyroid-stimulating hormone, follicle-stimulating hormone and luteinizing hormone were colocalized with GR to a lesser degree; approximately one-half of the cells exhibited immunoreactivity to these hormones contained GR. By contrast, only a minority of the prolactin-immunoreactive cells expressed GR. Our results suggest that glucocorticoids may differentially regulate the secretion and/or synthesis of these pituitary hormones by directly affecting the hormone-producing cells of the anterior pituitary.

Animals↗
PubMed1987

Colocalization of GABA and tyrosine hydroxylase immunoreactivities in the axons innervating the neurointermediate lobe of the rat pituitary: an ultrastructural immunogold study.

Distribution of the gamma-aminobutyric acid (GABA)ergic and dopaminergic innervations was studied in the rat neurointermediate lobe using antibodies against GABA and tyrosine hydroxylase. In light microscopy, immunoperoxidase staining revealed similar distribution patterns of the axons reacting with both antibodies. Diffusely scattered in both lobes, they were more concentrated along the marginal zone of the neural lobe. Application of a double, recto-verso, immunogold labelling method in electron microscopy revealed systematic colocalization of GABA and tyrosine hydroxylase (TH) immunoreactivities in the axons innervating the intermediate lobe; in the neural lobe, almost all GABA-immunoreactive axons were also labelled for TH. Thus, GABA and dopamine, hitherto reported to occur in distinct axons, in fact colocalize in the axonal systems which innervate the pituitary neurointermediate lobe. These observations suggest possible interactions (pre- or postsynaptic) of both transmitters in the functional regulation of the intermediate and neural lobes.

Animals↗
PubMed1989

Evidence for colocalization of substance P and 5-hydroxytryptamine in spinally projecting neurons from the cat medulla oblongata.

Substance P (SP)- and 5-hydroxytryptamine (5-HT)-like immunoreactivities were localized in bulbospinal neurons of the raphe nuclei and ventrolateral medulla (VLM). In raphe pallidus and raphe obscurus virtually all of the spinally projecting neurons contained SP and/or 5-HT. Furthermore, SP and 5-HT were colocalized in half of these spinal-raphe neurons. In raphe magnus few spinally projecting neurons contained either SP or 5-HT. Half of the bulbospinal neurons in the caudal VLM contained SP and/or 5-HT and in 50% of these SP and 5-HT were colocalized. However, no SP-containing neurons in the rostral VLM projected to the spinal cord.

Animals↗
PubMed1994

Colocalization of NADPH-diaphorase with neuropeptides in the intrapancreatic neurons of the chicken.

Colocalization of nitric oxide with neuropeptides was investigated in the chicken pancreas by use of double staining combined with the indirect immunofluorescence technique and histochemistry for NADPH-diaphorase, a specific marker for neural nitric oxide synthase. NADPH-diaphorase positive ganglia were easily detected in the interlobular connective tissue. Many NADPH-diaphorase positive ganglion cells also showed immunoreactivity for VIP (80.9%) or galanin (76.2%). Some ganglion cells showed enzyme activity only (about 20%). Very few neurons were NADPH-diaphorase negative, but immunopositive for VIP (2.0%) or galanin (3.7%). The present study provides evidence that nitric oxide colocates with VIP and galanin in the chicken pancreas.

Animals↗
PubMed1996

EM colocalization of AMPA and NMDA receptor subunits at synapses in rat cerebral cortex.

Electrophysiology and light microscopy suggest that a single excitatory synapse may use both amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) and N-methyl-D-aspartate (NMDA) receptors. Using immunogold electron microscopy, we here provide direct evidence for colocalization at individual synapses in sensorimotor cortex of adult rats. Colocalization was most commonly observed on dendritic spines; subunits of the two classes of receptors seemed to be independently distributed within the synaptic active zone.

Animals↗
PubMed1996

Ontogenetic changes in neuropeptide Y-like-immunoreactivity in the terminal nerve of the chum salmon and the cloudy dogfish, with special reference to colocalization with gonadotropin-releasing hormone-immunoreactivity.

We observed ontogenetic changes of neuropeptide Y (NPY)-like-immunoreactivity in the terminal nerve (TN) of the chum salmon, a teleost, and the cloudy dogfish, an elasmobranch. In the chum salmon, NPY-like-immunoreactive (NPY-IR) cells first appeared in the olfactory placode of embryos at 16 days after fertilization, and then extended sequentially and centrally in the olfactory system. Colocalization of NPY- and gonadotropin-releasing hormone (GnRH)-like-immunoreactivities was also observed in TN ganglion cells. In the cloudy dogfish, NPY-IR cells first appeared in the rudimental TN ganglion of the embryo at the 40 mm stage. Then, the NPY-IR cells and fibers in the TN system increased in density during late embryonic periods. Colocalization of NPY- and GnRH-like-immunoreactivities in TN ganglion cells was not found in the developing or the adult dogfish.

Age Factors↗
PubMed1989

The colocalization of cholecystokinin and tyrosine hydroxylase mRNAs in mesencephalic dopaminergic neurons in the rat brain examined by in situ hybridization.

The colocalization of cholecystokinin and tyrosine hydroxylase mRNAs was studied with a cellular resolution in the mesencephalic dopaminergic neurons of the rat brain by in situ hybridization using synthetic oligonucleotides. An extensive colocalization of cholecystokinin-expressing cells, greater than that seen previously by immunohistochemistry, was found in the ventral tegmental area and in the substantia nigra pars compacta. We observed in these regions that cholecystokinin and tyrosine hydroxylase mRNAs coexisted in the same neurons but not all dopamine cells expressed cholecystokinin mRNA. 6-Hydroxydopamine-induced destruction of mesostriatal dopaminergic neurons resulted in a complete loss of cholecystokinin and tyrosine hydroxylase mRNA expression throughout the substantia nigra pars compacta, indicating that all cholecystokinin expressing cells are 6-hydroxydopamine-sensitive. While increased enkephalin mRNA expression in the striatum ipsilateral to the lesion was detected, no change of cholecystokinin mRNA expression was observed in any forebrain on the lesioned side, suggesting that cholecystokinin expression in the forebrain is not under dopaminergic control. These results show the usefulness of the in situ hybridization approach for the precise localization of cells in rat brain which express mRNAs for cholecystokinin and tyrosine hydroxylase and for the study of the effects of neurotoxic lesions on these cells.

Animals↗
PubMed1989

A peptide histidine isoleucine/peptide histidine methionine-like peptide in the rabbit retina: colocalization with vasoactive intestinal peptide, synaptic relationships and activation of adenylate cyclase activity.

Antisera against peptide histidine isoleucine and peptide histidine methionine were found to label a subpopulation of amacrine and displaced amacrine cells in the rabbit retina with processes ramifying in sublaminas 1, 3 and 5 of the inner plexiform layer. Preadsorption controls demonstrated that this immunoreactivity was specific for a peptide histidine isoleucine- or peptide histidine methionine-like (peptide histidine isoleucine/peptide histidine methionine-like) peptide, and was not caused by cross-reactivity of the peptide histidine isoleucine or peptide histidine methionine antibodies with vasoactive intestinal peptide vasoactive intestinal peptide. In double-label studies, vasoactive intestinal peptide and peptide histidine isoleucine/peptide histidine methionine-like immunoreactivity were colocalized in the same population of retinal neurons. Electron microscopic analysis revealed that the peptide histidine isoleucine/peptide histidine methionine-labelled cells interacted with processes of bipolar cells, amacrine cells and ganglion cells. Peptide histidine methionine and peptide histidine isoleucine were slightly less potent than vasoactive intestinal peptide in stimulating adenylate cyclase activity in the rabbit retina, while the related peptides secretin, glucagon, and the C-terminal vasoactive intestinal peptide fragment, vasoactive intestinal peptide (10-28), showed little or no stimulatory activity. Stimulation of adenylate cyclase by high concentrations of vasoactive intestinal peptide and peptide histidine methionine were non-additive. These results suggest that a peptide histidine isoleucine/peptide histidine methionine-like peptide may function as a neuroactive peptide in the mammalian retina, and that this peptide appears to be cosynthesized and colocalized with vasoactive intestinal peptide and to mimic the activity of vasoactive intestinal peptide through interaction with vasoactive intestinal peptide receptor-adenylate cyclase complexes.

Adenylyl Cyclases↗
PubMed1990

Use of enhanced silver staining combined with electron microscopical immunolabelling to demonstrate the colocalization of neuropeptide Y and vasoactive intestinal polypeptide in cerebrovascular nerves.

The combination of immunolabelling at the electron microscope level and enhanced silver staining has been used to demonstrate the colocalization of neuropeptide Y and vasoactive intestinal polypeptide in perivascular nerves supplying cerebral arteries of the rat. This has been shown in control tissue, but it is easier to demonstrate after long-term sympathectomy since that leads to an enhancement of neuropeptide Y in vasoactive intestinal polypeptide-containing parasympathetic nerves supplying these vessels. Immunolabelling of the antigens for these peptides was performed sequentially with the biotin streptavidin diaminobenzidine method, and the end product to the first antiserum was gold-silver intensified before the visualization of the second antigen. Using this technique, it was shown that all the neuropeptide Y immunoreactivity present in the rat cerebral vessels after long-term sympathectomy with guanethidine was localized in vasoactive intestinal polypeptide-containing nerves. Furthermore, an immunohistochemical analysis of the parasympathetic pterygopalatine ganglia in guanethidine-treated rats showed an increase in the percentage of neurons displaying neuropeptide Y immunoreactivity. In order to clarify if the pterygopalatine ganglion was the origin of those neuropeptide Y/vasoactive intestinal polypeptide-immunoreactive cerebrovascular nerves, which had increased in number after sympathectomy, a fluorescent neuronal tracer (Fast Blue) was applied to the right middle cerebral artery of rats which had undergone guanethidine treatment for six weeks. Immunohistochemical analysis of the ipsilateral ganglion 72 h after application of the tracer revealed the presence of immunoreactivity to both these peptides in retrogradely labelled neurons. It is concluded that neuropeptide Y and vasoactive intestinal polypeptide are colocalized in perivascular parasympathetic nerves supplying the middle cerebral artery of the rat, which have their origin in the pterygopalatine ganglion. Furthermore, long-term sympathectomy with guanethidine leads to an increase in the expression of neuropeptide Y in these vasoactive intestinal polypeptide-immunoreactive neurons.

Animals↗
PubMed1995

Secretoneurin-immunoreactivity in nerve terminals apposing identified preganglionic sympathetic neurons in the rat: colocalization with substance P and enkephalin.

Preganglionic sympathetic neurons projecting to the superior cervical ganglion are innervated by nerve fibers containing classical neurotransmitters as well as neuropeptides. In this study we examined the possible participation of a novel peptide, secretoneurin (a cleavage product of secretogranin II), in regulation of sympathetic outflow to head and neck by using a retrograde labelling-technique combined with immunohistochemistry. In addition, the coexistence of secretoneurin with substance P and leu-enkephalin, peptides known to innervate preganglionic neurons, was investigated. The majority of retrogradely labeled neurons were localized in the nucleus intermediolateralis of spinal cord segments T1-T3 (maximum at T2). Nearly all of Fast Blue positive neuronal perikarya were apposed by nerve fibers and terminals exhibiting immunoreactivity to secretoneurin. The main secretoneurin-immunoreactive form found in the upper thoracic segments corresponded to the free peptide secretoneurin as revealed by chromatography and radioimmunoassay. More than half of labeled neurons were surrounded by nerve endings containing in addition substance P or leu-enkephalin which were also, however, less frequently colocalized. Our results suggest that secretoneurin influences the activity of preganglionic sympathetic neurons projecting to the superior cervical ganglion. Regarding their frequent colocalization with substance P and leu-enkephalin, functional interactions of these peptides on preganglionic sympathetic nerve activity have to be considered.

Animals↗
PubMed2003

Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line.

Previously we have reported that in vitro muscle aldolase binds to muscle FBPase [Biochem. Biophys. Res. Commun. 275 (2000) 611-616] which results in the changes of regulatory properties of the latter enzyme. In the present paper, the evidence that aldolase binds to FBPase in living cell is presented. The colocalization experiment, in which aldolase was diffused into skinned fibres that had been pre-incubated with FBPase, has shown that aldolase in the presence of FBPase binds predominantly to the Z-line. The existence of a triple aldolase-FBPase-alpha-actinin complex was confirmed through a real-time interaction analysis using the BIAcore biosensor. The colocalization of FBPase and aldolase on alpha-actinin of the Z-line indicates the existence of glyconeogenic metabolon in vertebrates' myocytes.

Actinin↗
PubMed2004

Drosophila cohesins DSA1 and Drad21 persist and colocalize along the centromeric heterochromatin during mitosis.

Sister chromatid cohesion in eukaryotes is maintained mainly by a conserved multiprotein complex termed cohesin. Drad21 and DSA1 are the Drosophila homologues of the yeast Scc1 and Scc3 cohesin subunits, respectively. We recently identified a Drosophila mitotic cohesin complex composed of Drad21/DSA1/DSMC1/DSMC3. Here we study the contribution of this complex to sister chromatid cohesion using immunofluorescence microscopy to analyze cell cycle chromosomal localization of DSA1 and Drad21 in S2 cells. We observed that DSA1 and Drad21 colocalize during all cell cycle stages in cultured cells. Both proteins remain in the centromere until metaphase, colocalizing at the centromere pairing domain that extends along the entire heterochromatin; the centromeric cohesion protein MEI-S332 is nonetheless reported in a distinct centromere domain. These results provide strong evidence that DSA1 and Drad21 are partners in a cohesin complex involved in the maintenance of sister chromatid arm and centromeric cohesion during mitosis in Drosophila.

Animals↗
PubMed2004

Neuropeptide-containing neurons in the endopiriform region of the rat: morphology and colocalization with calcium-binding proteins and nitric oxide synthase.

The endopiriform nucleus, further divided into dorsal and ventral parts, and the neighbouring pre-endopiriform (pEn) nucleus form a region of highly heterogeneous structure involved in numerous physiological and pathological processes. Nonpyramidal neurons of this region containing three neuropeptides-somatostatin (SOM), neuropeptide Y (NPY), and vasoactive intestinal peptide (VIP)-were examined in this study. Their colocalization with three calcium-binding proteins-parvalbumin (PV), calbindin D28k (CB), calretinin (CR), and with nitric oxide synthase (NOS), was investigated by qualitative and quantitative methods. The results are summarized as follows: (1) all studied substances are distributed in neurons of the entire region, (2) SOM-ir neurons constitute the most numerous neuropeptide-containing population, whereas NOS-ir neurons make up the largest population of all studied, (3) colocalizations are found in the endopiriform region (Enr) (SOM with CB, PV and NOS; VIP with CR; NPY with NOS and NOS with CR), (4) heterogeneity of the endopiriform region appears in the differences of cells' shape distributions of single-labeled (SOM-, CR-PV-ir) and double-labeled (SOM/CB-, SOM/PV-, NPY/NOS- and NOS/CR-ir) neurons, as well as in differentiated percentage values of SOM/NOS, NPY/NOS and VIP/CR double-labeled neurons in three studied parts; additionally, differences in distribution of immunoreactive neuropil elements between parts of the region are observed. Numerous regional differences concerning neuronal morphology and immunocytochemical characteristics justify further division of the endopiriform region into distinguished parts. Some immunocytochemical features of the neurons in studied region may contribute to the role in epileptogenesis.

Animals↗
PubMed2005

Genetic evidence that mycobacterial FtsZ and FtsW proteins interact, and colocalize to the division site in Mycobacterium smegmatis.

We provide genetic evidence to show that the Mycobacterium tuberculosis FtsZ and FtsW proteins interact, and that these interactions are biologically relevant. Furthermore, we show by fluorescence microscopy that Mycobacterium smegmatis FtsW is part of its septasomal complex and colocalizes with FtsZ to the midcell sites. Colocalization experiments reveal that approximately 27% of the cells with septal Z-rings contain FtsW whereas 93% of the cells with FtsW bands are associated with FtsZ indicating that FtsW is late recruit to the septum, as in Escherichia coli. Our results suggest that mycobacterial FtsZ can localize to the septum independent of FtsW, and that interactions of FtsW with FtsZ are critical for the formation of productive FtsZ-rings and the cell division process in mycobacteria.

Aspartic Acid↗
PubMed2004

Missense mutations in cancer suppressor gene TP53 are colocalized with exonic splicing enhancers (ESEs).

Mutation databases can be viewed as footprints of functional organization of a gene and thus can be used to infer its functional organization. We studied the association of exonic splicing enhancers (ESEs) with missense mutations in the tumor suppressor gene TP53 using the International Agency for Research on Cancer (IARC) mutation database. The goals of the study were: (i) to verify the hypothesis that deleterious missense mutations are colocalized with ESEs; (ii) to identify potentially functional ESE sites in the open reading frame (ORF) of the TP53. If some sequence functions as a splicing enhancer, then nucleotide substitutions in the site will disturb splicing, abrogate p53 function, and cause an increased susceptibility to cancer. Therefore, among cancers showing p53 mutations, more missense mutations are expected within functional ESE sites as compared to non-functional ESE motifs. Using several statistical tests, we found that missense mutations in TP53 are strongly colocalized with ESEs, and that only a small fraction of ESE sites contributes to the association. There are usually one or two ESEs per exon showing a statistically significant association with missense mutations--so-called significant ESE sites. In many respects significant ESE sites are different from those that do not show association with missense mutations. We found that positions of significant ESE sites are codon-dependent--significant ESEs preferentially start from the first position of a codon, whereas non-significant ESEs show no position dependence. Significant ESEs showed a more limited set of sequences compared to non-significant ESEs. These findings suggest that there is a limited number of missense mutations that influence ESE sites and our analysis provides further insight into the types of sites that harbor exonic enhancer elements.

CpG Islands↗
PubMed2004

DSCR1 gene expression is dependent on NFATc1 during cardiac valve formation and colocalizes with anomalous organ development in trisomy 16 mice.

The Down syndrome critical region 1 (DSCR1) gene is present in the region of human chromosome 21 and the syntenic region of mouse chromosome 16, trisomy of which is associated with congenital heart defects observed in Down syndrome. DSCR1 encodes a regulatory protein in the calcineurin/NFAT signal transduction pathway. During valvuloseptal development in the heart, DSCR1 is expressed in the endocardium of the developing atrioventricular and semilunar valves, the muscular interventricular septum, and the ventricular myocardium. Human DSCR1 contains an NFAT-rich calcineurin-responsive element adjacent to exon 4. Transgenic mice generated with a homologous regulatory region of the mouse DSCR1 gene linked to lacZ (DSCR1(e4)/lacZ) show gene activation in the endocardium of the developing valves and aorticopulmonary septum of the heart, recapitulating a specific subdomain of endogenous DSCR1 cardiac expression. DSCR1(e4)/lacZ expression in the developing valve endocardium colocalizes with NFATc1 and, endocardial DSCR1(e4)/lacZ, is notably reduced or absent in NFATc1(-/-) embryos. Furthermore, expression of the endogenous DSCR1(e4) isoform is decreased in the outflow tract of NFATc1(-/-) hearts, and the DSCR1(e4) intragenic element is trans-activated by NFATc1 in cell culture. In trisomy 16 (Ts16) mice, expression of endogenous DSCR1 and DSCR1(e4)/lacZ colocalizes with anomalous valvuloseptal development, and transgenic Ts16 hearts have increased beta-galactosidase activity. DSCR1 and DSCR1(e4)/lacZ also are expressed in other organ systems affected by trisomy 16 in mice or trisomy 21 in humans including the brain, eye, ear, face, and limbs. Together, these results show that DSCR1(e4) expression in the developing valve endocardium is dependent on NFATc1 and support a role for DSCR1 in normal cardiac valvuloseptal formation as well as the abnormal development of several organ systems affected in individuals with Down syndrome.

Animals↗