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PubMed2007

Immunohistochemical localization of aromatic L-amino acid decarboxylase in mouse taste buds and developing taste papillae.

Aromatic L-amino acid decarboxylase (AADC) catalyses the decarboxylation of all aromatic L-amino acids. In mammals, AADC is expressed in many tissues besides the nervous system, and is associated with additional regulatory roles of dopamine and serotonin in a wide range of tissues. We examined the expression of AADC by using reverse transcription-polymerase chain reaction (RT-PCR) and immunohistochemistry. RT-PCR analysis showed that mRNA of AADC was detected in the taste bud-containing epithelium of the circumvallate papilla of mice. By immunohistochemical analyses, AADC was detected in a subset of taste bud cells of fungiform, foliate, and circumvallate papillae. Double-label studies showed that AADC colocalized with serotonin, NCAM, PLCbeta2, and PGP9.5. On the other hand, AADC never colocalized with alpha-gustducin. Our results of double staining with AADC and taste cell markers indicate that only the type III cells could convert 5-hydroxytryptophan (5-HTP) to serotonin within taste buds. Taken together with previous studies, the properties of the type III cell of taste buds exactly fit into the APUD (amine and amine precursor uptake and decarboxylation) cell scheme. Furthermore, in the developing circumvallate papilla, AADC are first detected in a small number of papillary epithelial cells at E14.5. By E18.5, AADC-positive epithelial cells also express PGP9.5, which is one of marker of taste cells, and these cells have been contacted by developing nerve fibers. These results suggest that AADC expression begins at early stages of taste bud cell differentiation, and biogenic amines may act on taste bud differentiation of tongue epithelial cells, and further may regulate innervation of taste bud progenitor cells.

Animals↗
PubMed2004

MAP, a protein interacting with a tumor suppressor, merlin, through the run domain.

Merlin (or schwannomin) is a tumor suppressor encoded by the neurofibromatosis type 2 gene. Many studies have suggested that merlin is involved in the regulation of cell growth and proliferation through interactions with various cellular proteins. To better understand the function of merlin, we tried to identify the proteins that bind to merlin using the yeast two-hybrid screening. Characterization of the positive clones revealed a protein of 749 amino acids named merlin-associated protein (MAP), which showed wide tissue distribution in Northern blot analysis. Sequence analysis revealed that MAP is a potential homologue of a yeast check-point protein, BUB2, and contains TBC, SH3, and RUN domains, thereby implicating its role in the Ras-like GTPase signal pathways. MAP and merlin were directly associated in vitro and in vivo, and colocalized in NIH3T3 cells. The RUN domain of MAP and the C-terminus of merlin appeared to be responsible for their interaction. MAP decreased the AP-1-dependent promoter activity additively with merlin in NIH3T3 cells. In addition, merlin and MAP synergistically reduced the colony formation of NIH3T3 cells. These results suggest that MAP may play a cooperative role in the merlin-mediated growth suppression of cells.

3T3 Cells↗
PubMed2004

Presence of translation elongation factor-1A (eEF1A) in the excitatory postsynaptic density of rat cerebral cortex.

The postsynaptic density (PSD) is a proteinaceous cellular structure that is specialized for postsynaptic signal transduction. Here, we show that eukaryotic translation factor-1A (eEF1A; formerly known as eEF-1alpha) is associated with the excitatory PSD in rat forebrain. Immunoblot analysis showed that eEF1A in the PSD fraction is enriched over homogenate. Salt (1.0M NaCl), but not non-ionic detergents such as Triton X-100 (1.0%) and n-octyl glucoside (1.0%), could dissociate eEF1A from the PSD core. In cultured cortical neurons, eEF1A was colocalized with postsynaptic markers (PSD95 and SynGAPalpha), but not with a presynaptic marker (synaptophysin). These results indicate that eEF1A is present in the PSD of the excitatory synapses.

Animals↗
PubMed2005

Novel rab GAP-like protein, CIP85, interacts with connexin43 and induces its degradation.

Gap junctions play critical roles in tissue function and homeostasis. Connexin43 (Cx43) is a major gap junction protein expressed in the mammalian heart and other tissues and may be regulated by its interaction with other cellular proteins. Using the yeast two-hybrid screen, we identified a novel Cx43-interacting protein of 85-kDa, CIP85, which contains a single TBC, SH3, and RUN domain, in addition to a short coiled coil region. Homologues containing this unique combination of domains were found in human, D. melanogaster, and C. elegans. CIP85 mRNA is expressed ubiquitously in mouse and human tissues. In vitro interaction assays and in vivo co-immunoprecipitation experiments confirmed the interaction of endogenous CIP85 with Cx43. In vitro interaction experiments using CIP85 mutants with in-frame deletions of the TBC, SH3, and RUN domains indicated that the SH3 domain of CIP85 is involved in its interaction with Cx43. Conversely, analysis of Cx43 mutants with proline to alanine substitutions in the two proline-rich regions of Cx43 revealed that the P(253)LSP(256) motif is an important determinant of the ability of Cx43 to interact with CIP85. Laser-scanning confocal microscopy showed that CIP85 colocalized with Cx43 at the cell periphery, particularly in areas reminiscent of gap junction plaques. The functional importance of the interaction between CIP85 and Cx43 was suggested by the observation that CIP85 appears to induce the turnover of Cx43 through the lysosomal pathway.

Amino Acid Sequence↗
PubMed1994

Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast.

The Saccharomyces cerevisiae Wbp1 protein is an endoplasmic reticulum (ER), type I transmembrane protein which contains a cytoplasmic dilysine (KKXX) motif. This motif has previously been shown to direct Golgi-to-ER retrieval of type I membrane proteins in mammalian cells (Jackson, M. R., T. Nilsson, and P. A. Peterson. 1993. J. Cell Biol. 121: 317-333). To analyze the role of this motif in yeast, we constructed a SUC2-WBP1 chimera consisting of the coding sequence for the normally secreted glycoprotein invertase fused to the coding sequence of the COOH terminus (including the transmembrane domain and 16-amino acid cytoplasmic tail) of Wbplp. Carbohydrate analysis of the invertase-Wbp1 fusion protein using mannose linkage-specific antiserum demonstrated that the fusion protein was efficiently modified by the early Golgi initial alpha 1,6 mannosyltransferase (Och1p). Subcellular fractionation revealed that > 90% of the alpha 1,6 mannose-modified fusion protein colocalized with the ER (Wbp1p) and not with the Golgi Och1p-containing compartment or other membrane fractions. Amino acid changes within the dily sine motif (KK-->QK, KQ, or QQ) did not change the kinetics of initial alpha 1,6 mannose modification of the fusion protein but did dramatically increase the rate of modification by more distal Golgi (elongating alpha 1,6 and alpha 1,3) mannosyltransferases. These mutant fusion proteins were then delivered directly from a late Golgi compartment to the vacuole, where they were proteolytically cleaved in a PEP4-dependent manner. While amino acids surrounding the dilysine motif played only a minor role in retention ability, mutations that altered the position of the lysines relative to the COOH terminus of the fusion protein also yielded a dramatic defect in ER retention. Collectively, our results indicate that the KKXX motif does not simply retain proteins in the ER but rather directs their rapid retrieval from a novel, Och1p-containing early Golgi compartment. Similar to observations in mammalian cells, it is the presence of two lysine residues at the appropriate COOH-terminal position which represents the most important features of this sorting determinant.

Amino Acid Sequence↗
PubMed1994

Confocal imaging of time-dependent internalization and localization of NBD-PC in intact rat lungs.

Morphological localization of a fluorescent analogue of phosphatidylcholine (PC), C12-NBD-PC ([1-palmitoyl-2-[12-(7-nitro-2-1,3-benzoxadiazol-4-yl) amino] dodecanoyl]PC) was evaluated in adult rat lung. Fluorescence was observed at various times after intratracheal liposome instillation. Fluorometric analysis of C12-NBD-PC in lung homogenate showed an initial rapid uptake followed by a more gradual uptake phase. Microscopic observation of fixed lung slices showed C12-NBD-PC uptake in alveolar type II cells (identified by surfactant protein A and Maclura pomifera agglutinin colocalization), nonciliated distal airway epithelial cells, but not in subepithelial tissue. Macrophages showed an initial uptake that did not increase with time. Fluorescence measured in type II cells was diffuse at 5 min, became punctate, and intensified gradually by 2 h. Isolation of type II cells and lamellar bodies from instilled lung confirmed localization of fluorophore in them. This study shows time-dependent uptake of C12-NBD-PC by type II and bronchiolar cells and preferential internalization to lung lamellar bodies as previously described for surfactant PC.

4-Chloro-7-nitrobenzofurazan↗
PubMed2000

Similarities and differences in the subcellular localization of hamartin and tuberin in the kidney.

Tuberous sclerosis complex (TSC) is an autosomal dominant disorder characterized by hamartomas in multiple organs, notably the brain and kidneys. The disease is caused by mutations in TSC1 or TSC2 genes, coding hamartin and tuberin, respectively. Immunofluorescence analysis of tuberin and hamartin performed here demonstrates that both proteins are specifically expressed in the distal urinary tubule, comprising the distal tubules, connecting segment, and collecting ducts. Hamartin, distinct from tuberin, is expressed in the thick ascending limbs of Henle and in juxtaglomerular cells, where it colocalizes with renin. In positive epithelial cells, tuberin localizes to the cytoplasm as well as the apical membrane. Hamartin, however, preferentially localizes to the apical membrane. The two proteins colocalize at the apical membrane of type A intercalated cells and connecting tubule cells, whereas in type B intercalated cells they reveal a variable pattern of expression. The cell-specific expression of tuberin and hamartin described here will provide critical insight into the cell types that give rise to kidney lesions, and the tumor suppressor role of these proteins in TSC.

3T3 Cells↗
PubMed2004

Expression of the forkhead transcription factor FOXP1 is associated with estrogen receptor alpha and improved survival in primary human breast carcinomas.

PURPOSE: The FOXP1 protein belongs to a functionally diverse family of winged-helix or forkhead transcription factors that have diverse roles in cellular proliferation, differentiation, and neoplastic transformation. The FOXP1 gene, which maps to 3p14, shows common loss of heterozygosity in breast tumors and is a candidate tumor suppressor gene. However, its role in breast cancer is unknown. EXPERIMENTAL DESIGN: We have therefore investigated the pattern of FOXP1 expression in whole sections from normal (n = 16) and neoplastic (n = 90) breast tissues and correlated the level of expression in 283 invasive breast carcinomas on tissue microarrays with clinicopathological factors and survival. Because a relationship with estrogen receptor (ER) was identified, estrogen (17beta-estradiol) regulation and ER/FOXP1 colocalization was also investigated. RESULTS: Expression of FOXP1 was significantly positively associated with ER (P = 0.03) and negatively with epidermal growth factor receptor (P = 0.01) but no association with age (P = 0.91), lymph node status (P = 0.94), size (P = 0.76), or grade (P = 0.22). In a multivariate analysis of survival, FOXP1 expression was associated with a significantly improved relapse-free (P = 0.03) and borderline overall (P = 0.09) survival. Unlike normal breast, there was common coexpression of FOXP1 and ER in cell lines and tumors, but no 17beta-estradiol (10(-9) m) regulation of FOXP1 in MCF-7 cells was demonstrated. CONCLUSIONS: Our findings support a role for FOXP1 as a potential ER coregulator in human breast carcinoma and suggest that it may also independently regulate additional important pathways that control the progression of breast cancer.

Adult↗
PubMed1997

Localization of a novel 210 kDa protein in Xenopus tight junctions.

The tight junction is the most apical member of the intercellular junctional complex. It functions as a permeability barrier between epithelial cells and maintains the integrity of the apical and basolateral membrane domains. In order to study tight junctions in Xenopus laevis, a polyclonal antibody was raised which recognized Xenopus ZO-1. Monoclonal antibody 19B1 (mAb 19B1) was generated in rats using a crude membrane preparation from Xenopus lung as antigen. mAb 19B1 gave immunofluorescent staining patterns identical to those seen with anti-ZO-1 on monolayers of Xenopus A6 kidney epithelial cells and on frozen sections of Xenopus kidney, liver, and embryos. Electron microscopy showed that the 19B1 antigen colocalized with ZO-1 at the tight junction. Western blotting and immunoprecipitation demonstrated that ZO-1 is an approximately 220 kDa protein in Xenopus, while mAb 19B1 identified an approximately 210 kDa antigen on immunoblots. Immunoprecipitates of ZO-1 were not recognized by mAb 19B1 by western analysis. The solubility properties of the 19B1 antigen suggested that it is a peripheral membrane protein. Thus, the antigen recognized by the new monoclonal antibody 19B1 is not ZO-1 and represents a different Xenopus tight junction associated protein.

Animals↗
PubMed1999

Plakophilin-3, a novel armadillo-like protein present in nuclei and desmosomes of epithelial cells.

We report on a novel Armadillo-like protein, termed plakophilin-3. The human protein, which is encoded by a 2.8 kb messenger RNA, has a predicted molecular mass of 87 kDa. The protein comprises 10 Armadillo-like repeats, preceded by an amino-terminal region of 293 amino acid residues and followed by a short carboxy-terminal region of 27 amino acid residues. Plakophilin-3 is classified as a member of the p120(ctn)/plakophilin subfamily of Armadillo proteins based on the number and organization of the Armadillo repeats and its high sequence similarity to other members of this family. CLUSTAL W alignment of p120(ctn)/plakophilin subfamily members showed the plakophilin-3 protein to be most similar to plakophilin-1 and -2. Western blot analysis of plakophilin-3 revealed expression in all epithelial cell lines tested but not in foreskin fibroblasts and various sarcoma-derived cell lines. This is unlike most other members of the p120(ctn)/plakophilin subfamily, which are widely expressed. By immunofluorescence, the plakophilin-3 protein was colocalized with desmoglein in desmosomes of epithelial cells. In addition, an intriguing speckle-like nuclear staining was observed. Hence, like plakophilin-1 and -2, plakophilin-3 displays a dual intracellular location, i.e. in the desmosomal plaque and in the nucleus. These results suggest the involvement of plakophilin-3 in both desmosome-dependent adhesion and signaling pathways. Furthermore, the human plakophilin-3 gene was mapped on the chromosomal locus 11p15 by fluorescent in situ hybridization.

Amino Acid Sequence↗
PubMed2005

Na+/H+ exchanger 3 affects transport property of H+/oligopeptide transporter 1.

Oligopeptide transporter PEPT1 is thought to be involved in the intestinal absorption and renal reabsorption of peptides and therapeutic agents. The driving force of PEPT1 is H+ gradient, a part of which is supplied by Na+/H+ exchanger (NHE) expressed on the apical surface of the epithelium although molecular identification of NHE has not yet been fully clarified. Here we examined the effect of NHE3 coexpression on the function of PEPT1 to support the hypothesis that NHE3 regulates PEPT1 function by supplying its driving force. HEK293 cells expressing PEPT1 alone exhibited Na+-independent but pH-dependent uptake of glycylsarcosine (GlySar), whereas those coexpress PEPT1 and NHE3 showed an increase in GlySar uptake and conferred Na+-dependence on the uptake of GlySar. The increase in GlySar transport by PEPT1 depended on the expression level of NHE3 and was found at various levels of PEPT1 expression. Kinetic analysis of GlySar uptake in HEK293 cells expressing both PEPT1 and NHE3 or those expressing PEPT1 alone revealed an approximately 3 times increase in the transport capacity in the presence of NHE3, as normalized by PEPT1 mRNA expression. Confocal microscopy indicated that both PEPT1 and NHE3 are colocalized on the cell-surface of HEK293 cells. Thus, the present findings are the first to specify that NHE3 exerts post-transcriptional stimulation of PEPT1-mediated transport and can affect cellular uptake of the substrates by PEPT1 expressed on apical membranes in the body.

Antibodies, Monoclonal↗
PubMed2003

Expression of a splice variant of KAI1, a tumor metastasis suppressor gene, influences tumor invasion and progression.

KAI1 (CD82) belongs to the transmembrane 4 superfamily in which members have inhibitory effects on tumor cell motility and metastasis. During reverse transcription-PCR analysis, we found a splice variant of KAI1 (spliced-KAI1) in which exon 7 was deleted. This exon encodes the 28 amino acids that span from the distal part of the second extracellular loop to the proximal part of the fourth transmembrane region. Expression of spliced-KAI1 was observed in metastatic tissues of gastric cancer patients with poor prognosis after operation. Genomic DNA analysis revealed that this variant was derived from the alternative splicing of exon 7. Immunoprecipitation showed that the interaction of spliced-KAI1 with integrin alpha(3)beta(1) was weaker than that of wild-type KAI1. Wild-type KAI1, but not spliced-KAI1, colocalized with E-cadherin, an adherens junction protein. Also, mouse colon adenocarcinoma cells stably expressing spliced-KAI1 (CT-26/spliced-KAI1) showed increased in vivo tumorigenicity, as well as increased in vitro invasive potential and cell-extracellular matrix adhesion compared with wild-type KAI1-expressing cells. In metastatic lung and liver tissues from mice inoculated with CT-26/spliced-KAI1 cells, the expression of wild-type KAI1 was nearly absent and spliced-KAI1 was dominant, and weak interaction of KAI1 with integrin alpha(3)beta(1) was observed. These results indicate that there is a functional difference between wild-type KAI1 and spliced-KAI1 in respect to cell motility, adhesion, tumor growth and metastasis, and expression of spliced-KAI1 may be a marker for poor prognostic factors in gastric and other cancers.

Adenocarcinoma↗
PubMed1995

The oculocerebrorenal syndrome gene product is a 105-kD protein localized to the Golgi complex.

The oculocerebrorenal syndrome of Lowe (OCRL) is a multisystem disorder affecting the lens, kidney, and CNS. The predicted amino acid sequence of the OCRL gene, OCRL-1, was used to develop antibodies against the OCRL-1 protein. Western blot analysis using affinity-purified serum against the amino terminus of the OCRL-1 gene product (ocrl-1) demonstrates a single protein of 105 kD in fibroblasts of a normal individual that is absent in fibroblasts of an OCRL patient who lacks OCRL-1 transcript. A single protein with the same electrophoretic mobility is found by western analysis in various human cultured cell lines, and approximately the same size protein is also found in all mouse tissues tested. Northern analysis of various human and mouse tissues demonstrate that OCRL-1 transcript is expressed in nearly all tissues examined. By immunofluorescence, the ocrl-1 antibody stains a juxtanuclear region in normal fibroblast cells, while no specific staining is evident in the OCRL patient who produces no transcript. Colocalization of the ocrl-1 protein to the Golgi complex was demonstrated using a known monoclonal antibody against a Golgi-specific coat protein, beta-COP (beta coatomer protein).

Adult↗
PubMed1997

Cloning and characterization of phorbol ester differentiation-resistant U937 cell variants.

Differentiation-resistant U937 cells were derived from parental U937 human promonocytic leukemia cells by selecting for a nonadherent phenotype in cell cultures continuously exposed to 12-O-tetradecanoylphorbol-13-acetate (TPA). Subsequent analysis indicated no differences between wildtype (wt) and resistant U937 cells with respect to protein kinase C (PKC) isozyme expression, activation, or down-modulation. The subcellular localization of PKCs is identical in wt and resistant cells with the exception of PKC beta 2, which no longer colocalizes with microtubules in the TPA-resistant cell lines. In contrast to wt-U937 cells, the resistant cells do not express beta 2-integrin adhesion molecules, cd11b and cd11c, on the cell surface following TPA treatment but do express cd11b and cd11c in intracellular vesicles. TPA stimulates the translocation of these vesicles to the cell surface in wt U937 cells but not in the resistant cells. These results suggest that events downstream of PKC activation may mediate cytoskeletal reorganization and beta 2-integrin transport to the cell surface in wt-U937 cells but not in the differentiation-resistant cells.

CD18 Antigens↗
PubMed2006

Expression of Nogo-A and NgR in the developing rat brain after hypoxia-ischemia.

Nogo-A and its receptor, NgR, have been shown to inhibit neurite growth in the adult rat. Therefore, we hypothesized that Nogo-A and NgR will be upregulated and thus play a similar role in the damage in developing rat brain following hypoxia-ischemia (HI). To test this hypothesis, we subjected postnatal day 7 (P7) rats to HI by permanently ligating the right common carotid artery, followed by exposure to 8%O2/92% N2 for 3 h. Rat brains at 0 h, 6 h, 12 h, 24 h and 72 h after HI, as well as from sham controls, were collected to determine histopathological damage and expression levels of Nogo-A and NgR using hematoxylin and eosin (H&E) staining, immunohistochemistry, fluorescence immunolabeling, Western blot analysis and reverse transcriptase-polymerase chain reaction (RT-PCR). We found neuronal degeneration and edema in the ischemic cortex, becoming most prominent at 24 h following HI in this model. Accordingly, the expression of Nogo-A and NgR protein was significantly upregulated at 24 h compared with the sham controls (p<0.01). The upregulated Nogo-A and NgR immunoreactive cells were mainly located in the core of the ischemic cortex and colocalized to neurons. Meanwhile, we found the expression of both Nogo-A and NgR mRNA was increased at 6 h and peaked at 12 h in the ischemic cortex after HI, compared with sham controls. Our findings of upregulation of neurite growth inhibitor Nogo-A and its receptor NgR in ischemic cortex suggest that Nogo-A and NgR may participate in the pathology seen after HI in neonatal rats.

Analysis of Variance↗
PubMed2001

Stereological cell counts of GABAergic neurons in rat dentate hilus following transient cerebral ischemia.

We have previously demonstrated a 60-80% ischemic loss of somatostatinergic neurons in the dorsal dentate hilus of the rat. However, several studies have failed to demonstrate ischemic loss of GABAergic neurons in hilus, although one study reports that 96% of the somatostatinergic neurons in the dorsal hilus colocalize GABA. In order to understand this paradox, we have now estimated, using unbiased stereology, the total number of neurons immunohistochemically stained against glutamic acid decarboxylase-65 (GAD65) and GAD67 in the dorsal dentate hilus. Rats were divided into groups subjected to either sham operation (n=8) or 8 min of transient global ischemia during systemic hypotension (n=8) and allowed to survive for 7-9 days. Results from cell counts (mean +/- SD) in sham rats demonstrated that the dorsal hilus contains 9,189+/-3,957 GAD65 neurons and 6,991+/-2,784 GAD67 neurons. After ischemia, corresponding cell counts demonstrated 10,216+/-4,866 GAD65 neurons and 10,119+/-5,906 GAD67 neurons, and these results were not significantly different (P>0.05) from results in sham rats. Power analysis of the t-test informs that losses less than 80% are not significant and reflects the excessive variance in our material. For comparison, we estimated a total of 21% ischemic neuron death in the dorsal hilus on cresyl violet-stained sections from other corresponding sham (n=7) and ischemic rats (n=7). This explains why ischemic loss of hilar GABAergic neurons can only be detected by counts of the vulnerable subpopulation colocalizing somatostatin. Our investigation has demonstrated a surprisingly high variation between rats in a number of GAD-immunopositive neurons located in the dorsal dentate hilus, which is related to variations between the individual rats and neurons in their endogenous GAD expression.

Animals↗
PubMed2004

Molecular-cytogenetic characterization of non-Hodgkin's lymphoma with double and cryptic translocations of the immunoglobulin heavy chain gene.

The present study aimed to characterize the clinical and molecular-cytogenetic features of non-Hodgkin's lymphoma (NHL) with double translocation of the immunoglobulin heavy chain (IGH) gene. G-banding analysis, fluorescence in situ hybridization (FISH) with the IGH (Cgamma and VH) and oncogene (c-MYC, BCL1, BCL2, and BCL6) probes, and long-distance polymerase chain reaction (LD-PCR) were performed on 6 patients with B-cell lymphoma, one with angioimmunoblastic T-cell lymphoma, and one with acute lymphoblastic leukemia (ALL) with B-cell phenotype. G-banding analysis detected two different 14q32 translocations, t(14,18) and add (14)(q32) in a patient with ALL. Two distinct partners of double IGH translocation identified by FISH were as follows: c-MYC + BCL2 in 3 patients, c-MYC + BCL1 in 2, c-MYC + BCL6 in one, BCL2 + 9q22 in one, and 1q21 + 6q27 in one. Colocalization of BCL1 and c-MYC probes was demonstrated in a patient with mantle cell lymphoma. LD-PCR detected c-MYC/Cmu, c-MYC/Calpha and BCL6/Cmu, and c-MYC/Calpha fusion in each one patient. Seven of 8 patients showed high serum LDH. Central nervous system and leukemic involvement was observed in 5 and 6 patients, respectively. Median survival time of patients with c-MYC/IGH translocation was 9 months. The results defined a clinical subset of B-cell lymphoma/leukemia showing extremely poor prognosis. C-MYC/IGH translocation is possibly an evolutionary alteration following the primary IGH translocation with BCL1, BCL2, or BCL6. Furthermore, FISH identified one novel (9q22) and one cryptic chromosomal breakpoints (6q27) involved in IGH translocation.

Adult↗
PubMed1993

Cellular colocalization of calcium/calmodulin-dependent protein kinase II and calcineurin in the rat cerebral cortex and hippocampus.

An immunoperoxidase technique was used to locate multifunctional Ca2+/calmodulin-regulated protein phosphatase (calcineurin) and kinase (CaM-kinase II) in the rat cerebral cortex and hippocampus. Immunoreactivities for both enzymes were highly concentrated in the brain regions, where pyramidal-shaped neurons revealed strong immunoreactivities in their perikarya and dendrites. Serial thin section analysis using the polyethylene glycol embedding procedure disclosed that the cellular distribution of calcineurin immunolabelling in the cerebral cortex and hippocampus was similar to that of CaM-kinase II. The present findings suggest that the phosphatase and kinase may interact with each other in such neuronal subsets.

Animals↗