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PubMed2006

Expression and localization of endothelin-converting enzyme-1 isoforms in human endothelial cells.

Endothelin-converting enzyme (ECE)-1 is a membrane-bound metalloprotease responsible for production of vasoactive endothelin (ET)-1 from inactive big ET-1. ECE-1 exists as four separate isoforms, ECE-1a, b, c, and d, which differ only in their amino-terminal regions. We investigated the expression and localization of the ECE-1 isoforms in primary human umbilical vein endothelial cells (HUVECs) and EAhy926 cells. Reverse transcriptase polymerase chain reaction showed expression of all four isoforms in both cell lines, with ECE-1d seeming, at least qualitatively, to be the predominant isoenzyme. Isoform-specific polyclonal antibodies were used to investigate isoform protein expression. ECE-1a, b, and c protein was detected in EAhy926 cells by immunoblotting; only ECE-1a and ECE-1c were detected in HUVECs. Using immunofluorescence microscopy analysis, both HUVEC and EAhy926 cells showed nuclear immunoreactivity with a monoclonal antibody recognizing all ECE-1 isoforms. The ECE-1a antibody also showed nuclear immunoreactivity in both cell lines; this seemed to colocalize with nucleolin. The ECE-1b antibody showed nuclear immunoreactivity in EAhy926 cells, but no overlap with nucleolin was seen. Intracellular immunoreactivity was seen in both cell lines using the ECE-1c antibody; this showed some colocalization with concanavalin A (an endoplasmic reticulum marker). von Willebrand Factor was used as a marker for Weibel-Palade bodies in HUVECs, but no colocalization with ECE-1 was seen during this study. The data presented here sheds new light on the localization of ECE-1a, b, and c in cultured human endothelial cells, which may further understanding of the ET system and aid design of therapeutic ECE inhibitors.

Aspartic Acid Endopeptidases↗
PubMed2006

Better practices in collaborative mental health care: an analysis of the evidence base.

OBJECTIVES: To conduct a systematic review of the experimental literature in order to identify better practices in collaborative mental health care in the primary care setting. METHODS: A review of Canadian and international literature using Medline, PsycInfo, Embase, the Cochrane Library, and other databases yielded over 900 related reports, of which, 38 studies met the inclusion criteria. A systematic review and descriptive analysis is presented, with key conclusions and best practices. RESULTS: Successful collaboration requires preparation, time, and supportive structures, building on preexisting clinical relationships. Collaborative practice is likely to be most developed when clinicians are colocated and most effective when the location is familiar and nonstigmatizing for patients. Degree of collaboration does not appear to predict clinical outcome. Enhanced collaboration paired with treatment guidelines or protocols offers important benefits over either intervention alone in major depression. Systematic follow-up was a powerful predictor of positive outcome in collaborative care for depression. A clear relation between collaborative efforts to increase medication adherence and clinical outcomes was not evident. Collaboration alone has not been shown to produce skill transfer in PCP knowledge or behaviours in the treatment of depression. Service restructuring designed to support changes in practice patterns of primary health care providers is also required. Enhanced patient education was part of many studies with good outcomes. Education was generally provided by someone other than the PCP. Collaborative interventions that are part of a research protocol may be difficult to sustain long-term without ongoing funding. Consumer choice about treatment modality may be important in treatment engagement in collaborative care (for example, having the option to choose psychotherapy vs medication). CONCLUSIONS: A body of experimental literature evaluating the impact of enhanced collaboration on patient outcomes-primarily in depressive disorders-now exists. Better practices in collaborative mental health care are beginning to emerge.

Benchmarking↗
PubMed1994

An adherens junction protein is a member of the family of lactose-binding lectins.

We previously described a pig junction protein of M(r) 37,000 found in oral epithelium but not in epidermis, limited to suprabasal cells, and colocalizing by immunofluorescence with adherens junction proteins. A 1.1-kilobase pair cDNA of the 37-kDa protein yielded an open reading frame encoding a 323-amino acid protein of 35,852 Da, and Northern analysis demonstrated a band of 1.2 kilobases in tongue RNA. Secondary structure predictions indicate that the 37% identical 16-17-kDa N- and C-terminal domains from beta-sheet-rich barrels linked by a compact proline-rich segment. The protein is 72% identical in amino acid sequence and shares symmetrical two-domain structure with L-36, a lectin of unknown function from rat intestine, indicating that the 37-kDa protein is the porcine form of L-36. Of the homologous lactose binding lectins known, two others, invertebrate lectins, share this symmetrical structure. Expression of the C-terminal domain of the pig lectin in bacteria yields a lectin which binds lactosyl-Sepharose, and binding is inhibited by lactose. The expressed protein binds a glycoprotein of 120 kDa from pig tongue epithelium on Western blots, and this is also inhibited by lactose. The findings suggest that the lectin function may be involved in the assembly of adherens junctions.

Amino Acid Sequence↗
PubMed1997

Intracellular distribution of phospholipase C gamma 1 in cell lines with different levels of transformation.

The intracellular localization of phospholipase C gamma 1 (PLC gamma 1) was studied in cell lines with different levels of cell transformation. Immunofluorescence analysis of cell lines with differently organized actin cytoskeletons (A431 cells, HeLa cells, mouse hepatoma MH 22A, Zajdela ascitic hepatoma, primary human embryo skin and lung fibroblasts) gave evidence that PLC gamma 1 is colocalized only with cortical actin and not with stress fibers. Coimmunoprecipitation experiments indicated that PLC gamma 1 was bound to actin in all cell lines investigated. Further, the nuclei of highly transformed cell lines (A431 cells, HeLa cells, mouse hepatoma MH 22A, rat Zajdela ascitic hepatoma) were labeled with the anti-PLC gamma 1 antibody. In contrast, PLC gamma 1 was not observed in the nuclei of primary human embryo skin or lung fibroblasts. Since PLC gamma 1 exists only in the nuclei of highly transformed cell lines, we propose that the distinctive intracellular localization of PLC gamma 1 in normal and highly transformed cell lines may reflect differences in cell signaling systems and mitogenic cell signal transduction.

Actin Cytoskeleton↗
PubMed2002

A novel mechanism of silicon uptake.

Crystal-like structures in vacuoles, precipitates in the cytoplasm and on the tonoplast membrane have been found to store remarkable amounts of Si in a number of higher plants. In most of the cases the final storage product is a SiO(2) gel. Accumulation inside the cells presumes a membrane and cytoplasm passage, driven by unknown transporters. Beside this uptake into the cytoplasm, Si-accumulating species possess a mechanism that does not involve a membrane and cytoplasm passage. Unusual small invaginations comprising the two membranes, plasmalemma and tonoplast, which enclose a small border of cytoplasm, were observed. The same cells contained vacuolar vesicles surrounded by two membranes, obviously derived from the invaginations. By energy-dispersive X-ray analysis and electron spectroscopic imaging, Si was shown in the invaginations and vacuolar vesicles. This novel endocytotic process allows the uptake of condensed, higher-molecular-weight Si compounds. In Zn hyperaccumulators, frequently SiO(2) precipitates were found in different cell compartments. Such plants showed the same invaginations and vacuolar vesicles, but Zn, colocalized with Si, was detected in these structures. Electron energy loss spectra confirmed the assumption that Zn-silicate is present in the vesicles. In the vacuoles the unstable Zn-silicate is degraded, forming SiO(2) precipitates, while the released Zn is bound to an unknown partner.

Cytoplasmic Vesicles↗
PubMed2000

Analysis of nucleoid morphology during germination and outgrowth of spores of Bacillus species.

After a few minutes of germination, nucleoids in the great majority of spores of Bacillus subtilis and Bacillus megaterium were ring shaped. The major spore DNA binding proteins, the alpha/beta-type small, acid-soluble proteins (SASP), colocalized to these nucleoid rings early in spore germination, as did the B. megaterium homolog of the major B. subtilis chromosomal protein HBsu. The percentage of ring-shaped nucleoids was decreased in germinated spores with lower levels of alpha/beta-type SASP. As spore outgrowth proceeded, the ring-shaped nucleoids disappeared and the nucleoid became more compact. This change took place after degradation of most of the spores' pool of major alpha/beta-type SASP and was delayed when alpha/beta-type SASP degradation was delayed. Later in spore outgrowth, the shape of the nucleoid reverted to the diffuse lobular shape seen in growing cells.

Bacillus megaterium↗
PubMed1997

Expression of the five somatostatin receptor (SSTR1-5) subtypes in rat pituitary somatotrophes: quantitative analysis by double-layer immunofluorescence confocal microscopy.

Using quantitative double-label fluorescence immunocytochemistry and confocal microscopy, we have analysed the pattern of expression of SSTR1-5 in normal rat pituitary somatotrophes. Antipeptide rabbit polyclonal antibodies were produced against the extracellular domains of SSTR1-5. SSTR antigens were colocalized in GH positive cells using rhodamine conjugated secondary antibody for SSTRs and FITC-conjugated secondary antibody for GH. SSTR5 was the predominant subtype which was expressed in 86 +/- 9.7% of GH cells followed by SSTR2 in 42 +/- 6.4% of GH positive cells. SSTR4 and SSTR3 were modestly expressed in 23 +/- 4.7% and 18 +/- 3.2% of somatotrophes respectively whereas SSTR1 was the least expressed subtype occurring in only 5 +/- 1.2% of somatotrophes. These results demonstrate variable expression of the 5 SSTRs in somatotrophes. The preponderance of the SST-28 preferring SSTR5 subtype correlates with the reported higher potency of SST-28 than SST-14 for inhibiting GH secretion.

Animals↗
PubMed1995

Evidence for apoptosis in advanced human atheroma. Colocalization with interleukin-1 beta-converting enzyme.

This study sought evidence for apoptosis, a form of programmed cell death, in human atheromatous coronary and carotid arteries. Markers for apoptotic cells included in situ terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling (TUNEL), genomic DNA electrophoresis, and morphological analysis. Intimal lesions contained more TUNEL+ cells (34 +/- 6%, n = 8) than non-atherosclerotic arterial intima (8 +/- 3%, n = 5, P < 0.05). The tunica media of the diseased arteries had a percentage of TUNEL+ cells (5 +/- 1%) similar to that in the normal vessels (3 +/- 1%, N.S.). Oligonucleosomal DNA fragments were visualized in extracts from 12 atheromatous plaques but in none of 5 non-atherosclerotic vessels. Both smooth muscle cells (SMC) and macrophages, two major cell types in the atherosclerotic intima, bore markers of apoptosis, but with different patterns, as determined by double histochemical labeling for cell types and TUNEL. The TUNEL+ SMC localized mainly in the fibrotic portion of the atheroma, whereas TUNEL+ macrophages clustered near or within the lipid-rich core of the lesion. Atheromatous lesions expressed mRNA encoding interleukin-1 beta-converting enzyme (ICE), a mammalian cell death gene, as demonstrated by reverse transcriptase polymerase chain reaction. Immunohistochemistry revealed that ICE localized in regions of TUNEL+ SMC and macrophages. TUNEL- cells showed little or no immunoreactive ICE. These data point to a role for apoptosis in regulation of cell accumulation during atherogenesis and suggest involvement of ICE in SMC death in fibrous regions of complex atheroma, and in macrophage death in the lipid-rich core of the lesion. Apoptosis of vascular cells in fibrous cap may impede maintenance or repair of the matrix in this region and affect stability of the plaques.

Apoptosis↗
PubMed1996

POMC-related products in the intermediate pituitary of the amphibian, Bufo marinus: differential subcellular processing in the Golgi and secretory granules.

In the intermediate pituitary of the anuran amphibian, Bufo marinus, the N-acetylation of ACTH(1-13)-NH2 to yield alpha-MSH occurs as a cosecretory processing event, whereas the N-acetylation of beta-endorphin occurs as a posttranslational processing event. To understand how these two N-acetylation reactions are segregated, B. marinus intermediate pituitary cells were analyzed by immunogold labeling electron microscopy, and by using an ultracentrifugation procedure. The immunogold labeling studies indicated that ACTH(1-13)-NH2-related immunoreactivity was colocalized with N-acetylated beta-endorphin-related immunoreactivity in secretory granules. Furthermore, ACTH(1-13)-NH2-related immunoreactivity was not detected in either the ER or the Golgi. N-Acetylated beta-endorphin-related immunoreactivity, however, was detected in the Golgi. Ultracentrifugation analysis revealed that in an ER/microsomal fraction, beta-LPH-sized and nonacetylated beta-endorphin-sized immunoreactive material were present in a molar ratio of 1:2. No N-acetylated forms of beta-endorphin were detected in the ER/microsomal fraction. In a Golgi/secretory granule fraction, the molar ratio of beta-LPH to beta-endorphin was 1:9 with 58% of the beta-endorphin being N-acetylated. Collectively, these data support the following hypotheses. The proteolytic cleavage of ACTH (1-39) to yield ACTH (1-13)-NH2 is a late processing event occurring in secretory granules. The cleavage of beta-LPH to yield nonacetylated beta-endorphin is an early processing event that may occur in the ER or the Golgi. Because N-acetylated beta-endorphin and nonacetylated ACTH(1-13)-NH2 are colocalized in secretory granules, it appears, therefore, that the N-acetylation of beta-endorphin is completed prior to loading into secretory granules. Thus, there is a spatial and temporal separation of the posttranslational processing events associated with the beta-LPH portion and ACTH portion of the POMC biosynthetic pathway in amphibian intermediate pituitary cells.

Acetylation↗
PubMed2001

Cathepsin K in aseptic hip prosthesis loosening: expression in osteoclasts without polyethylene wear particles.

OBJECTIVE: To investigate the expression of the bone matrix degrading cysteine proteinase cathepsin K and to determine the colocalization of cathepsin K with polyethylene (PE) particles in tissue specimens of patients with aseptic hip prosthesis loosening (AHPL). METHODS: The expression of cathepsin K was studied by immunohistochemistry in tissue specimens of 9 patients with aseptically loosened acetabular components of failed cementless total hip replacements. The expression of cathepsin K was compared to that of the macrophage marker CD68 by serial section analysis. Double labeling of the expression of cathepsin K or CD68 by immunohistochemistry and of PE particles by modified Oil Red staining method was performed. RESULTS: Cathepsin K could be predominantly detected in osteoclasts attached to the bone tissue, while only a few (CD68+) mononuclear and multinucleated foreign body giant cells (MGC) were positive for this enzyme. By double labeling with Oil Red staining we found the majority of CD68 positive cells of the periprosthetic tissue that were colocalized with PE particles. However, cathepsin K-expressing osteoclasts could not be stained with Oil Red. CONCLUSION: The present data suggest that in AHPL neither mononuclear cells nor MGC but rather osteoclasts are mainly involved in cathepsin K mediated bone matrix destruction. Using double labeling of immunohistochemistry and Oil Red staining we observed that the cathepsin K-expressing osteoclasts did not include PE particles.

Acetabulum↗
PubMed2005

Biochemical and morphologic evidence of the interaction of oligodendrocyte membrane rafts with actin filaments.

Cytoskeletal structures under the cell membrane carry out pivotal roles in the maintenance and remodeling of the cell structures. Reforming of the cytoskeletal networks after partial extraction of membrane components could be a good clue to identify molecular components pertaining the interaction of cytoskeleton with membrane. A detergent extract from 3-week-old rat brain membrane fraction was found to make an actin-based gel upon incubation at 25 degrees C. Some protein components of the gelation products were recovered in a Triton-insoluble low-density microdomain fraction (raft) after depolymerization of actin filaments. Some of these proteins were identified as 2',3'-cyclic nucleotide-3'-phosphodiesterase (CNPase), proteolipid protein (PLP), and myelin oligodendrocyte glycoprotein (MOG) through electrospray time-of-flight (ESI-TOF) analysis and Western blotting. Because these proteins are well-known marker proteins of oligodendrocytes, localization of these proteins and cholesterol, a raft-localized lipid, with actin filaments was studied using cultured oligodendrocytes. Clear colocalization of these proteins and cholesterol with actin filaments was observed after Triton treatment at 4 degrees C before fixation. These results indicate that raft microdomains participate in the formation of cell shape through interaction with microfilaments in oligodendrocytes.

2',3'-Cyclic-Nucleotide Phosphodiesterases↗
PubMed2001

Differential expression of major gap junction proteins, connexins 26 and 32, in rat mammary glands during pregnancy and lactation.

We examined the expression pattern of two major gap junction proteins, connexin 26 (Cx26) and connexin 32 (Cx32), in rat mammary glands during pregnancy and lactation. Immunohistochemically the two different Cxs were coexpressed in acinar cells and were independently modulated according to the physiological cell activity. Western blot analysis demonstrated that Cx26 gradually increased from early pregnancy, while Cx32 rapidly and dramatically increased at 16 h after parturition, and that both Cxs reached a maximum early in lactation. Increased expression of both Cxs was confirmed by Northern blot analysis showing that their mRNA transcripts were significantly induced on the day of parturition. We also analyzed double-immunofluorescent staining for Cx26 and Cx32 on a confocal laser scanning microscope, in order to examine colocalization of these Cxs in situ. Cx26 immunoreactivity mostly overlapped with Cx32-positive sites in acinar cells of lactating mammary glands, indicating that both Cxs were colocalized together in the same gap junctional plaques in lactation. These results suggest that upregulation of Cx26 and Cx32 in acinar cells at lactating stages, with colocalization in the same gap junctional plaques, may be important for control of secretion by acinar cells in rat mammary glands.

Animals↗
PubMed1993

Colocalization of enkephalin and glycine in amacrine cells of the chicken retina.

The present double-label study combines enkephalin immunocytochemistry with either autoradiography of glycine high-affinity uptake or glycine immunocytochemistry to investigate the coexistence of glycine in enkephalin-amacrine cells of the chicken retina. A regional analysis revealed that the percentage coexistence of glycine high-affinity uptake in enkephalin-amacrine cells did not vary appreciably throughout the retina. Overall, 54.9% of enkephalin-amacrine cells exhibited high-affinity glycine uptake. Double-label immunofluorescence cytochemistry revealed that 52.5% of enkephalin-amacrine cells expressed glycine immunoreactivity. These double-immunolabeled cells were observed throughout the center and periphery of the retina. The present study reveals a similar percentage of chicken enkephalin-amacrine cells expressing either glycine high-affinity uptake (54.9%) or glycine immunoreactivity (52.5%) and therefore, provides supportive evidence for identifying these cells as glycinergic. The present study also suggests a functional diversity in the population of enkephalin-amacrine cells in the chicken retina relative to their coexisting/non-coexisting relationship with glycine.

Animals↗
PubMed1992

Transient expression of GAP-43 in nonneuronal cells of the embryonic chicken limb.

Growth associated protein (GAP)-43 is a membrane-bound phosphoprotein expressed in neurons and is particularly abundant during periods of axonal outgrowth in development and regeneration of the nervous system. In previous work, we cloned a full-length chicken GAP-43 cDNA and described the expression of its corresponding mRNA during early development of the chicken nervous system. We report here that the GAP-43 mRNA is also expressed transiently in developing limbs of chicken embryos, which contain axons of spinal cord and dorsal root ganglion neurons, but do not contain neuronal cell bodies. GAP-43 mRNA was first detectable by RNA blot analysis in limbs from Embryonic Day 5 (E5) embryos, reached maximal levels between E6 and E8, and diminished by E10. In situ hybridization analysis showed that the GAP-43 mRNA was localized in distal regions of developing limbs and was particularly abundant in the mesenchyme surrounding the digital cartilage. In some regions of the limb, GAP-43 immunoreactivity colocalized in cells that were also immunoreactive for meromyosin, a muscle-specific marker. These data suggest that both GAP-43 mRNA and the protein are expressed in nonneuronal cells of the developing limb, some of which may be part of the muscle cell lineage.

Animals↗
PubMed1992

Cloning and expression of a glycine transporter reveal colocalization with NMDA receptors.

A complementary DNA clone encoding a transporter for glycine has been isolated from rat brain, and its functional properties have been examined in mammalian cells. The transporter displays high affinity for glycine (KM approximately 100 microM) and is dependent on external Na+ and Cl-. Northern blot analysis indicates that the distribution of the mRNA encoding the glycine transporter is restricted to the nervous system. In situ hybridization data are consistent with roles for the transporter in both glycine neurotransmission and glycine modulation of N-methyl-D-aspartate (NMDA) receptors in the hippocampus. The identification of this transporter therefore opens the study of the molecular mechanisms underlying both inhibitory glycinergic transmission and NMDA-mediated excitatory transmission.

Amino Acid Sequence↗
PubMed2005

Expression of human oviductin in an immortalized human oviductal cell line.

OBJECTIVE: To determine whether OE-E6/E7, an immortalized human oviductal epithelial cell line, expresses oviductin messenger RNA (mRNA) and its translated protein. DESIGN: Transmission electron microscopy was employed to characterize the morphology of OE-E6/E7 cells followed by reverse-transcription polymerase chain reaction (PCR) analysis of oviductin mRNA and sequencing of the nested-PCR product. Confocal microscopy was used, using a polyclonal antibody against human oviductin and Con A as a marker for mannose residues, to reveal the colocalization of human oviduct-specific glycoprotein with the endoplasmic reticulum and Golgi compartments. SETTING: University-based anatomy and cell biology department. PATIENT(S): Women undergoing laparoscopy for tubal ligation or hysterectomy due to uterine fibroma. INTERVENTION(S): An immortalized OE-E6/E7 cell line was previously established using human oviductal epithelial cells. Electron microscopy, RT-PCR, sequencing, immunohistochemistry and confocal microscopy were performed. MAIN OUTCOME MEASURE(S): The presence of human oviductin mRNA and protein in OE-E6/E7 cells. RESULT(S): OE-E6/E7 cells retain morphological features characteristic of secretory cells and express human oviductin mRNA and its translated protein. CONCLUSION(S): OE-E6/E7 cells were characterized for the first time by electron microscopy and shown to exhibit histological features typical of secretory cells. Reverse-transcription PCR with sequencing and confocal microscopy showed, respectively, that human oviductin mRNA and protein are expressed in OE-E6/E7 cells. Our results suggest that OE-E6/E7 could be a useful tool for future studies of the function of human oviductin.

Amino Acid Sequence↗
PubMed1999

Restricted and coordinated expression of beta3-integrin and bone sialoprotein during cultured osteoblast differentiation.

In this study, the expression of beta3-integrin was examined in relationship to the restricted expression of bone sialoprotein (BSP). Immunohistochemical analysis indicated that the alpha(v)beta3-integrin was coincident and proximal to BSP expression in the fetal mandible bovine osteoblast culture model. Alpha(v)beta3-integrin expression was expressed predominantly in a region proximal to, but not including, the substrate adherent cells. In comparison, the alpha5beta1-integrin was expressed in a generalized pattern throughout the culture layers in a coordinated fashion to fibronectin. The temporal expression of beta1- and beta3-integrin was evaluated using RT-PCR and southern blot analysis. Unlike the generalized expression of beta1-integrin, beta3-integrin was restricted to days 3 and 5 of the culture period. The previous demonstration of similar restriction of BSP expression and the present colocalization of BSP suggests the potential coordinated expression of a specific extracellular matrix ligand with a select integrin. Beta3-integrin/BSP adhesion-mediated signaling may play a significant role in the process of osteoblast morphodifferentiation.

Animals↗
PubMed2003

Interaction of L2 with beta-actin directs intracellular transport of papillomavirus and infection.

Viruses that replicate in the nucleus, including the primary causative agent of cervical cancer, human papillomavirus type 16 (HPV16), must first cross the cytoplasm. We compared the uptake of HPV16 virus-like particles (VLPs) either with or without the minor capsid protein L2. Whereas VLPs containing only the major capsid protein L1 were diffusely distributed within the cytoplasm even 6 h post-infection, VLPs comprising both L1 and L2 exhibited a radial distribution in the cytoplasm and accumulated in the perinuclear region of BPHE-1 cells within 2 h. L2 of HPV16 or bovine papillomavirus was shown to bind to a 43-kDa cellular protein that was subsequently identified as beta-actin by matrix-assisted laser desorption ionization time-of-flight analysis. A conserved domain comprising residues 25-45 of HPV16 L2 was sufficient for interaction with beta-actin. HPV16 L2 residues 25-45 fused to green fluorescent protein, but not green fluorescent protein alone, colocalized with actin and caused cell retraction and disruption of the microfilament network. Finally, wild-type L2, but not L2 with residues 25-45 deleted, facilitated HPV16 pseudovirion infection. Thus, binding of beta-actin by L2 residues 25-45 facilitates transport of HPV16 across the cytoplasm during infection, and blockade of this novel interaction may be useful for prophylaxis.

Actins↗