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1.
Nanotechnology ; 20(27): 275207, 2009 Jul 08.
Article in English | MEDLINE | ID: mdl-19528679

ABSTRACT

We have studied the room-temperature non-radiative energy transfer processes in hybrid structures composed of (Ga, In)N/GaN single quantum wells and semiconducting polymer blend films placed in nanometre-scale proximity. The blends consist of three polyfluorene materials with concentrations adjusted so that they emit white light. Power-dependent photoluminescence (PL) measurements are used to investigate the process of energy transfer from the quantum wells to the different components of the polymer blend. We show that energy distribution among the hybrid structures involves competition between nanoscale range non-radiative energy transfer processes from the inorganic well to the polymer components and within the blend itself.

2.
J Autoimmun ; 24(4): 337-45, 2005 Jun.
Article in English | MEDLINE | ID: mdl-15869863

ABSTRACT

A hybridoma secreting a human monoclonal autoantibody to the islet cell autoantigen IA-2 was prepared from peripheral lymphocytes of a patient with type 1 diabetes and Graves' disease using EBV infection followed by fusion with a mouse/human hybrid cell line. The monoclonal antibody (M13) is an IgG1/kappa and in an immunofluorescence test M13 at 1 microg/mL showed islet cell antibody reactivity equivalent to 40 JDF units. M13 IgG bound (35)S-labelled IA-2 (26% at 100 microg/mL) and (125)I-labelled IA-2 (34% at 100 microg/mL) in an immunoprecipitation assay and reacted well with IA-2 in western blotting analysis. Amino acids 777-808 in the PTP domain of IA-2 were found to be important for M13 binding in an analysis using modified (35)S-labelled IA-2 proteins. M13 V region genes were from VH1-3, D3-22, JH4b, VKI DPK8/Vd+ and JK3 genes and showed a high replacement/silent mutation ratio for both the heavy (11.0) and the light (6.0) chain genes. Mouse monoclonal antibodies (mMAbs) reactive with at least three different epitopes within IA-2 aa 604-686 corresponding to the juxtamembrane domain were also obtained. F(ab')(2) or Fab from the mMAbs inhibited serum IA-2 autoantibody binding to IA-2 in 20/22 diabetic sera whereas M13 F(ab')(2) caused inhibition in only 6/22 sera. M13 is representative of some patient serum IA-2 autoantibodies and as such provides a useful tool to study autoimmune responses to IA-2.


Subject(s)
Antibodies, Monoclonal/immunology , Antibody Specificity/immunology , Autoantibodies/immunology , Autoantigens/immunology , Membrane Proteins/immunology , Protein Tyrosine Phosphatases/immunology , Animals , Antibodies, Monoclonal/chemistry , Autoantibodies/chemistry , Autoantigens/chemistry , Diabetes Mellitus, Type 1/immunology , Epitope Mapping , Humans , Hybridomas , Membrane Proteins/chemistry , Mice , Protein Tyrosine Phosphatase, Non-Receptor Type 1 , Protein Tyrosine Phosphatases/chemistry , Receptor-Like Protein Tyrosine Phosphatases, Class 8
3.
Eur J Immunogenet ; 31(5): 201-6, 2004 Oct.
Article in English | MEDLINE | ID: mdl-15379751

ABSTRACT

The possible role of the K469E polymorphism in the intercellular adhesion molecule-1 (ICAM-1) gene in the susceptibility to ischaemic heart disease (IHD) was investigated in a well-defined Irish population using two recently described family-based tests of association. One thousand and twelve individuals from 386 families with at least one member prematurely affected with IHD were genotyped for the ICAM-1 K469E polymorphism. Using the combined transmission disequilibrium test (TDT)/sib-TDT and the pedigree disequilibrium test (PDT), no association between the ICAM-1 K469E polymorphism and IHD was found. Our data demonstrate that, in an Irish population, the ICAM-1 K469E polymorphism is not associated with IHD.


Subject(s)
Amino Acid Substitution , Intercellular Adhesion Molecule-1/genetics , Myocardial Ischemia/genetics , Polymorphism, Single Nucleotide , Adult , Age of Onset , Codon/genetics , Family Health , Female , Gene Frequency , Genetic Predisposition to Disease , Genotype , Humans , Ireland/epidemiology , Linkage Disequilibrium , Male , Middle Aged , Myocardial Ischemia/epidemiology , Pedigree , Risk Factors , Siblings , White People/genetics
4.
Tissue Antigens ; 64(2): 199-203, 2004 Aug.
Article in English | MEDLINE | ID: mdl-15245376

ABSTRACT

Using two recently described family-based tests of association, the possible role of the functional -2518G/A polymorphism in the promoter region of the monocyte chemoattractant protein-1 (MCP-1) gene in the susceptibility to ischaemic heart disease (IHD) was investigated in a well-defined Irish population. One thousand and twelve individuals from 386 families with at least one member prematurely affected with IHD were genotyped for the MCP-1 -2518G/A polymorphism. Using the combined transmission disequilibrium test and the pedigree disequilibrium test, no association between the MCP-1 -2518G/A polymorphism and IHD was found. Our data demonstrate that, in an Irish population, the MCP-1 -2518G/A polymorphism is not strongly associated with IHD.


Subject(s)
Chemokine CCL2/genetics , Myocardial Ischemia/genetics , Polymorphism, Genetic , Female , Genetic Predisposition to Disease , Humans , Ireland , Male , Middle Aged , Promoter Regions, Genetic/genetics , Promoter Regions, Genetic/physiology
5.
Infect Immun ; 69(11): 6731-7, 2001 Nov.
Article in English | MEDLINE | ID: mdl-11598045

ABSTRACT

Mitogen-activated protein (MAP) kinase pathways are key factors in host signaling events and can also play important roles in the internalization of pathogenic bacteria by host cells. Porphyromonas gingivalis, a periodontal pathogen, can efficiently invade human gingival epithelial cells (GECs). In this study, we examined the activation of MAP kinase pathways in GECs infected with P. gingivalis. c-Jun N-terminal kinase (JNK) was activated after 5 min of infection with P. gingivalis, whereas noninvasive Streptococcus gordonii did not have a significant effect on JNK activation. In contrast, extracellular signal-regulated kinase (ERK) 1/2 was downregulated in a dose-dependent manner by P. gingivalis, but not by S. gordonii, after a 15-min exposure. Nonmetabolically active P. gingivalis cells were unable to modulate MAP kinase activity. U0126, a specific inhibitor of MEK1/2 (ERK1/2 kinase), and toxin B, a specific inhibitor of Rho family GTPases, had no effect on P. gingivalis invasion. Genistein, a tyrosine protein kinase inhibitor, blocked uptake of P. gingivalis. The transcriptional regulator NF-kappaB was not activated by P. gingivalis. These results suggest that P. gingivalis can selectively target components of the MAP kinase pathways. ERK1/2, while not involved in P. gingivalis invasion of GECs, may be downregulated by internalized P. gingivalis. Activation of JNK is associated with the invasive process of P. gingivalis.


Subject(s)
Gingiva/enzymology , MAP Kinase Signaling System , Porphyromonas gingivalis/immunology , Butadienes/pharmacology , Cells, Cultured , Down-Regulation , Enzyme Activation , Enzyme Inhibitors/pharmacology , Epithelial Cells/cytology , Epithelial Cells/immunology , Epithelial Cells/microbiology , Gingiva/cytology , Gingiva/immunology , Gingiva/microbiology , Humans , JNK Mitogen-Activated Protein Kinases , Mitogen-Activated Protein Kinase 1/metabolism , Mitogen-Activated Protein Kinase 3 , Mitogen-Activated Protein Kinases/metabolism , NF-kappa B/metabolism , Nitriles/pharmacology , Porphyromonas gingivalis/pathogenicity , p38 Mitogen-Activated Protein Kinases
6.
Cell Microbiol ; 1(3): 215-23, 1999 Nov.
Article in English | MEDLINE | ID: mdl-11207554

ABSTRACT

We have developed a fluorescence imaging technique using a DNA-binding dye to visualize, over time, the physical interactions between Porphyromonas gingivalis and human gingival epithelial cells in vitro. The results extend previous observations of P. gingivalis invasion of gingival epithelial cells based on indirect measurements. An intracellular location for P. gingivalis was established by optical sectioning of images in the z-plane. Kinetic analysis showed that P. gingivalis invasion of epithelial cells is a rapid and efficient process, reaching completion after 12 min. Imaging of infected monolayers revealed that over 90% of a population of gingival epithelial cells contained bacteria. Furthermore, only vital bacteria were capable of invasion, and intracellular bacteria congregated in the perinuclear region of the epithelial cells. P. gingivalis remained inside the epithelial cells over a 24 h period and induced rearrangement of the actin cytoskeleton along with alteration of the size and shape of the epithelial cells. These findings provide direct evidence that entry rates of P. gingivalis into gingival epithelial cells are high and rapid, and that internalized bacteria initially localize in a specific region of the epithelial cells.


Subject(s)
Endocytosis , Epithelial Cells/microbiology , Gingiva/microbiology , Microscopy, Fluorescence , Porphyromonas gingivalis/pathogenicity , Cell Nucleus/microbiology , Cell Size , Cells, Cultured , Colony Count, Microbial , Cytoskeleton/ultrastructure , DNA, Bacterial/chemistry , Epithelial Cells/cytology , Epithelial Cells/ultrastructure , Fluorescent Dyes/chemistry , Host-Parasite Interactions , Humans , Image Processing, Computer-Assisted , Kinetics
7.
Infect Immun ; 66(4): 1660-5, 1998 Apr.
Article in English | MEDLINE | ID: mdl-9529095

ABSTRACT

Periodontitis, which is widespread in the adult population, is a persistent bacterial infection associated with Porphyromonas gingivalis. Gingival epithelial cells are among the first cells encountered by both P. gingivalis and commensal oral bacteria. The chemokine interleukin 8 (IL-8), a potent chemoattractant and activator of polymorphonuclear leukocytes, was secreted by gingival epithelial cells in response to components of the normal oral flora. In contrast, P. gingivalis was found to strongly inhibit IL-8 accumulation from gingival epithelial cells. Inhibition was associated with a decrease in mRNA for IL-8. Antagonism of IL-8 accumulation did not occur in KB cells, an epithelial cell line that does not support high levels of intracellular invasion by P. gingivalis. Furthermore, a noninvasive mutant of P. gingivalis was unable to antagonize IL-8 accumulation. Invasion-dependent destruction of the gingival IL-8 chemokine gradient at sites of P. gingivalis colonization (local chemokine paralysis) will severely impair mucosal defense and represents a novel mechanism for bacterial colonization of host tissue.


Subject(s)
Interleukin-8/antagonists & inhibitors , Periodontal Diseases/etiology , Porphyromonas gingivalis/pathogenicity , Dental Plaque/microbiology , Humans , Interleukin-8/genetics , Interleukin-8/metabolism , KB Cells , RNA, Messenger/analysis
8.
J Histochem Cytochem ; 45(7): 965-73, 1997 Jul.
Article in English | MEDLINE | ID: mdl-9212822

ABSTRACT

The objective of this study was to localize rap1 in the rat parotid gland. Rap1 is a small GTP-binding protein that has been linked to phagocytosis in neutrophils and various functions in platelets. In this study, we used [alpha-32P]-GTP-blot overlay analysis, immunoblot analysis, and immunohistochemistry to identify rap1 in rat parotid gland. The immunohistochemical techniques included immunoperoxidase and widefield microscopy with image deconvolution. Rap1 was identified in the secretory granule membrane (SGM), plasma membrane (PM), and cytosolic (CY) fractions, with the largest signal being in the SGM fraction. The tightly bound vs loosely adherent nature of SGM-associated rap1 was determined using sodium carbonate, and its orientation on whole granules was assessed by trypsin digestion. Rap1 was found to be a tightly bound protein rather than a loosely adherent contaminant protein of the SGM. Its orientation on the cytosolic face of the secretory granule (SG) is of significance in postulating a function for rap1 because exocytosis involves the fusion of the cytoplasmic face of the SG with the cytoplasmic face of the PM, with subsequent release of granule contents (CO). Therefore, the localization and high concentration of rap1 on the SGM and its cytosolic orientation suggest that it may play a role in the regulation of secretion.


Subject(s)
Cytoplasmic Granules/chemistry , GTP-Binding Proteins/isolation & purification , Membrane Proteins/isolation & purification , Parotid Gland/chemistry , Animals , Cell Fractionation , Cytoplasmic Granules/ultrastructure , Guanosine Triphosphate/metabolism , Immunoblotting , Immunohistochemistry , Male , Parotid Gland/ultrastructure , Rats , Rats, Sprague-Dawley , rap GTP-Binding Proteins
9.
Infect Immun ; 65(1): 313-6, 1997 Jan.
Article in English | MEDLINE | ID: mdl-8975930

ABSTRACT

Porphyromonas gingivalis is a periodontal pathogen capable of invading primary cultures of normal human gingival epithelial cells (NHGEC). Involvement of P. gingivalis fimbriae in the invasion process was examined. Purified P. gingivalis 33277 fimbriae blocked invasion of this organism into NHGEC in a dose-dependent manner. DPG3, a P. gingivalis fimbria-deficient mutant, was impaired in its invasion capability approximately eightfold compared to its parent, strain 381. However, adherence of the mutant was only 50% reduced compared to the parent. Biotin labeling of NHGEC surface proteins revealed that two fimbriated strains, but not DPG3, bound a 48-kDa NHGEC protein. Adhesin-receptor interactions, such as fimbriae binding to a 48-kDa NHGEC surface receptor, may trigger activation of eukaryotic proteins involved in signal transduction and/or provoke the generation of surface P. gingivalis molecules required for internalization.


Subject(s)
Fimbriae, Bacterial , Gingiva/microbiology , Porphyromonas gingivalis/pathogenicity , Bacterial Adhesion , Binding, Competitive , Cells, Cultured , Epithelial Cells , Epithelium/microbiology , Fimbriae, Bacterial/genetics , Gingiva/cytology , Humans , Membrane Proteins/analysis , Mutation , Porphyromonas gingivalis/genetics , Protein Binding , Receptors, Immunologic/metabolism , Signal Transduction
10.
FEMS Microbiol Lett ; 144(2-3): 145-50, 1996 Nov 01.
Article in English | MEDLINE | ID: mdl-8900057

ABSTRACT

Porphyromonas gingivalis, a periodontal pathogen can invade primary cultures of gingival epithelial cells. This invasion was significantly inhibited (74-81%) by thapsigargin and 1,2-bis(2-aminophenoxy)ethane-N,N,N1,N1-tetraacetic acid, acetoxymethyl ester (BAPTA/AM), but not by EDTA or amiloride. Release of Ca2+ from an intracellular store and the subsequent increase in cytosolic [Ca2+] may, therefore, be involved in the invasion process, while Ca2+ influx is not. Moreover, cytosolic [Ca2+] was found to increase transiently in about 30% of gingival epithelial cells acutely exposed to P. gingivalis, but not in unexposed cells, or in cells exposed to noninvasive Escherichia coli. These findings indicate that P. gingivalis invasion of epithelial cells is correlated with activation of [Ca2+]-dependent host cell signaling systems.


Subject(s)
Calcium/physiology , Gingiva/microbiology , Porphyromonas gingivalis/physiology , Second Messenger Systems/physiology , Actin Cytoskeleton/physiology , Amiloride/pharmacology , Bacterial Adhesion , Cells, Cultured , Chelating Agents/pharmacology , Cytoskeleton/ultrastructure , Edetic Acid/pharmacology , Egtazic Acid/analogs & derivatives , Egtazic Acid/pharmacology , Epithelial Cells , Epithelium/microbiology , Escherichia coli/physiology , Gingiva/cytology , Microtubules/physiology , Porphyromonas gingivalis/pathogenicity , Thapsigargin/pharmacology
11.
In Vitro Cell Dev Biol Anim ; 32(6): 361-5, 1996 Jun.
Article in English | MEDLINE | ID: mdl-8842750

ABSTRACT

The relations between K+ channel and Cl- channel currents and mycoplasma infection status were studied longitudinally in HSG cells, a human submandibular gland cell line. The K+ channel currents were disrupted by the occurrence of mycoplasma infection: muscarinic activation of K+ channels and K+ channel expression as estimated by ionomycin- or hypotonically induced K+ current responses were all decreased. Similar decreases in ionomycin- and hypotonically induced responses were observed for Cl- channels, but only the latter decrease was statistically significant. Also, Cl- currents could be elicited more frequently than K+ currents (63% of cases versus 0%) in infected cells when tested by exposure to hypotonic media, indicating that mycoplasma infection affects K+ channels relatively more than Cl- channels. These changes occurred in the originally infected cells, were ameliorated when the infection was cleared with sparfloxacin, and recurred when the cells were reinfected. Such changes would be expected to result in hyposecretion of salivary fluid if they occurred in vivo.


Subject(s)
Chloride Channels/physiology , Fluoroquinolones , Mycoplasma Infections/physiopathology , Potassium Channels/physiology , Submandibular Gland/microbiology , Antitubercular Agents/pharmacology , Calcium/metabolism , Calcium/pharmacology , Cell Line , Cytosol/metabolism , Electric Conductivity , Humans , Hypotonic Solutions , Ionomycin/pharmacology , Quinolones/pharmacology
12.
Infect Immun ; 63(10): 3878-85, 1995 Oct.
Article in English | MEDLINE | ID: mdl-7558295

ABSTRACT

Porphyromonas gingivalis, a periodontal pathogen, can invade primary cultures of gingival epithelial cells. Optimal invasion occurred at a relatively low multiplicity of infection (i.e., 100) and demonstrated saturation at a higher multiplicity of infection. Following the lag phase, during which bacteria invaded poorly, invasion was independent of growth phase. P. gingivalis was capable of replicating within the epithelial cells. Invasion was an active process requiring both bacterial and epithelial cell energy production. Invasion was sensitive to inhibitors of microfilaments and microtubules, demonstrating that epithelial cell cytoskeletal rearrangements are involved in bacterial entry. P. gingivalis, but not epithelial cell, protein synthesis was necessary for invasion. Invasion within the epithelial cells was not blocked by inhibitors of protein kinase activity. Invasion was inhibited by protease inhibitors, suggesting that P. gingivalis proteases may be involved in the invasion process. Low-passage clinical isolates of P. gingivalis invaded with higher efficiency than the type strain. Serum inhibited invasion of the type strain but had no effect on the invasion of a clinical isolate. Invasion of gingival epithelial cells by P. gingivalis may contribute to the pathology of periodontal diseases.


Subject(s)
Gingiva/microbiology , Porphyromonas gingivalis/pathogenicity , Blood Bactericidal Activity , Cells, Cultured , Epithelium/microbiology , Gingiva/ultrastructure , Humans , Microscopy, Electron , Periodontal Diseases/etiology , Porphyromonas gingivalis/growth & development , Protease Inhibitors/pharmacology , Time Factors
13.
J Membr Biol ; 142(2): 181-93, 1994 Nov.
Article in English | MEDLINE | ID: mdl-7884810

ABSTRACT

Hypotonically induced changes in whole-cell currents and in cell volume were studied in the HSG cloned cell line using the whole-cell, patch clamp and Coulter counter techniques, respectively. Exposures to 10 to 50% hypotonic solutions induced dose-dependent increases in whole-cell conductances when measured using K+ and Cl- containing solutions. An outward current detected at 0 mV, corresponded to a K+ current which was transiently activated, (usually preceding activation of an inward current and had several characteristics in common with a Ca(2+)-activated K+ current we previously described in these cells. The hypotonically induced inward current had characteristics of a Cl- current. This current was inhibited by NPPB (5-nitro-2-(3-phenyl-propylamino)-benzoate) and SITS (4-acetamido-4'-isothiocyanostilbene), and its reversal potentials corresponded to the Cl- equilibrium potentials at high and low external Cl- concentrations. The induced current inactivated at voltages greater than +80 mV, and the I-V curve was outwardly rectifying. The current was unaffected by addition of BAPTA or removal of GTP from the patch pipette, but was inhibited by removal of ATP or by the presence of extracellular arachidonic acid, quinacrine, nordihydroguairetic acid, and cytochalasin D. Moreover, exposure of HSG cells to hypotonic media caused them to swell and then to undergo a regulatory volume decrease (RVD) response. Neither NPPB, SITS or quinine acting alone could inhibit RVD, but NPPB and quinine together totally inhibited RVD. These properties, plus the magnitudes of the induced currents, indicate that the hypotonically induced K+ and Cl- currents may underlie the RVD response. Cytochalasin D also blocked the RVD response, indicating that intact cytoskeletal F-actin may be required for activation of the present currents. Hence, our results indicate that hypotonic stress activates K+ and Cl- conductances in these cells, and that the activation pathway for the K+ conductance apparently involves [Ca2+], while the activation pathway for the Cl- conductance does not involve [Ca2+] nor lipoxygenase metabolism, but does require intact cytoskeletal F-actin.


Subject(s)
Chloride Channels/physiology , Hypotonic Solutions/pharmacology , Submandibular Gland/cytology , Submandibular Gland/physiology , 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid/pharmacology , Actins/physiology , Arachidonic Acid/pharmacology , Calcium/metabolism , Cell Line , Cell Membrane/drug effects , Cell Membrane/physiology , Cell Membrane/ultrastructure , Chloride Channels/antagonists & inhibitors , Chloride Channels/drug effects , Cytochalasin D/pharmacology , Cytoskeleton/physiology , Dose-Response Relationship, Drug , Egtazic Acid/analogs & derivatives , Egtazic Acid/pharmacology , Guanosine Triphosphate/pharmacology , Humans , Nitrobenzoates/pharmacology , Patch-Clamp Techniques , Potassium Channels/physiology , Quinacrine/pharmacology , Submandibular Gland/ultrastructure
14.
J Histochem Cytochem ; 42(1): 41-7, 1994 Jan.
Article in English | MEDLINE | ID: mdl-7505300

ABSTRACT

The GTP-binding protein G(o) was localized immunohistochemically in the rat parotid gland and in other exocrine glands with specific G(o) antibodies. Immunohistochemical studies revealed that affinity-purified G(o alpha) polyclonal antibody (GO/85) immunoreacted primarily with duct cells of the rat parotid gland; immunoreactivity was also noted in duct cells of the rat submandibular, mouse parotid, and mouse submandibular glands. Light labeling of rat parotid and submandibular gland acinar cells was also noted. G(o alpha) antiserum (9072) differing in specificity for epitopes within G(o alpha) produced similar results. This antiserum also immunoreacted with rat submandibular duct cell secretory granule membranes. In contrast, in rat and mouse pancreas G(o alpha) antibodies immunoreacted primarily with islet cells. Duct cells were negative but there was light labeling of rat pancreatic acinar cells. The apparent duct specificity of G(o alpha) staining was further verified by demonstrating that G(o alpha) antibodies immunoreacted with HSG-PA cells, a human transformed salivary duct cell line. Specificity in immunohistochemical labeling of HSG-PA cells was confirmed by Western blot analysis. The results demonstrate that G(o) appears to be selectively expressed in the duct cells of rat parotid gland and other salivary glands. The selective enrichment of G(o) in duct cells suggests that this G-protein plays an important role in duct cell physiology.


Subject(s)
GTP-Binding Proteins/analysis , Pancreas/chemistry , Parotid Gland/chemistry , Salivary Glands/chemistry , Submandibular Gland/chemistry , Animals , Antibody Specificity , Blotting, Western , Cells, Cultured , Epitopes , GTP-Binding Protein alpha Subunits, Gi-Go , Immunohistochemistry , Male , Mice , Pancreas/cytology , Parotid Gland/cytology , Rats , Salivary Glands/cytology , Submandibular Gland/cytology
15.
Am J Physiol ; 266(1 Pt 1): C58-66, 1994 Jan.
Article in English | MEDLINE | ID: mdl-8304431

ABSTRACT

Whole cell currents were measured in HSG-PA cells (a proposed model for salivary gland duct cells) after muscarinic receptor activation or exposure to known signaling agents. Exposure to carbachol or oxotremorine M produced large and often oscillatory increases in outward current whose reversal potentials indicated a K current. The current was sensitive to extracellular atropine, charybdotoxin, and quinine, but not apamin, and to 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid in the pipette. The response was prolonged or increased by guanosine 5'-O-(3-thiotriphosphate) and mimicked by D-myo-inositol 1,4,5-trisphosphate (IP3) or heparin in the pipette and by extracellular Ca ionophores. Tetraethylammonium indirectly inhibited the response via the muscarinic receptor. Fura 2 in cell suspensions showed that muscarinic agonists increased cytosolic Ca ion concentration ([Ca2+]i) five- to sevenfold, and measurements with indo 1 in individual cells showed that the oscillatory changes in outward current were tightly correlated with parallel changes in [Ca2+]i. The results indicate that muscarinic receptor stimulation of HSG-PA cells activates Ca(2+)-activated K channels through a signaling pathway involving a G protein, IP3 production, and increased [Ca2+]i levels. These findings are similar to those in salivary gland acinar cells.


Subject(s)
Parasympathomimetics/pharmacology , Potassium/physiology , Salivary Glands/physiology , Calcium/physiology , Carbachol/pharmacology , Cell Line , Electrophysiology , Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology , Humans , Oxotremorine/antagonists & inhibitors , Oxotremorine/pharmacology , Potassium Channel Blockers , Salivary Glands/cytology , Salivary Glands/drug effects , Signal Transduction , Tetraethylammonium , Tetraethylammonium Compounds/pharmacology
16.
Atherosclerosis ; 68(1-2): 95-103, 1987 Nov.
Article in English | MEDLINE | ID: mdl-3689486

ABSTRACT

Both random (U.C. Davis) and inbred ("Sea") Japanese quail were fed 8.6% dietary supplements of lard (SF) or fish oil (FO) Maxepa (38% of calories from fat) and 9 months later selected blood vessels were subjected to light and electron microscopy. Serum lipids were measured by means of automatic enzymatic analyses (Beckman Astra and Dupont ACA) following fasting (12-14 h) bleeding times taken at autopsy. VLDL and LDL were determined indirectly. Fatty acid profiles were done on pericardial fat from selected animals. All FO-fed quail averaged 22-48% increase in bleeding time when compared to diet controls or animals fed saturated fat (P less than 0.005). There was a 20% decrease in triacyglycerol (TG) and very low density lipoprotein (VLDL) in the random bred group (P less than 0.01). TG rose in the Sea Quail (NS). Low density lipoprotein (LDL) increased in both random (P less than 0.05) and inbred quail (P less than 0.05), but total cholesterol (TC) significantly increased only in the inbred birds (P less than 0.01). The HDL/LDL ratios in the FO groups were lower than in the controls. SF-fed animals had some fatty streak and/or fatty point formation in their coronary arteries and great vessels. FO-fed birds showed some fat deposits in their coronary arteries and greater accumulation (foam cells) within their great vessels with subendothelial protrusions into the lumen. It is suggested that these latter results may be a response to the relatively higher levels of cholesterol in FO (600 mg/100 g oil) versus SF (95 mg/100 g fat).(ABSTRACT TRUNCATED AT 250 WORDS)


Subject(s)
Arteries/drug effects , Docosahexaenoic Acids , Eicosapentaenoic Acid , Fatty Acids, Unsaturated/pharmacology , Lipids/blood , Animals , Arteries/ultrastructure , Arteriosclerosis/prevention & control , Bleeding Time , Coturnix , Drug Combinations , Fish Oils/pharmacology , Male , Microscopy, Electron , Triglycerides/blood
17.
J Oral Pathol ; 15(9): 493-9, 1986 Oct.
Article in English | MEDLINE | ID: mdl-3100750

ABSTRACT

Ten instances of a white plaque of the lateral tongue unique to homosexual males and referred to as oral hairy leukoplakia were analysed ultrastructurally. The surface epithelial layer exhibited extracellular, intracellular and intranuclear penetration by hyphae of Candida albicans, sometimes accompanied by coccobacilli in the extracellular space. The subcorneal epithelial layer included koilocytoid ballooned cells which had a paucity of cytoplasmic organelles and displayed condensation and emargination of the chromatin. Cells that exhibited these nuclear changes were found to be infected by a herpes-type virus which was visualized by electron microscopy in all ten cases. Clusters of nucleocapsids (86-110 nm in diameter) occurred in the nuclei and enveloped virions (111-175 nm in diameter) occurred in the cytoplasm and extracellular spaces. Virions showed budding from the nuclear envelope. Bundles of tubular structures (20 nm diameter) arranged in parallel occurred in the cytoplasm of some koilocytoid cells. There was no evidence by electron microscopy of the presence of papilloma virus within koilocytotic nuclei.


Subject(s)
Leukoplakia, Oral/ultrastructure , Tongue Neoplasms/ultrastructure , Candida albicans/isolation & purification , Humans , Leukoplakia, Oral/microbiology , Male , Mouth Mucosa/ultrastructure , Tongue Neoplasms/microbiology
18.
J Oral Pathol ; 14(8): 603-14, 1985 Sep.
Article in English | MEDLINE | ID: mdl-3930670

ABSTRACT

Clear cell odontogenic tumor, a rare epithelial jaw lesion of putative odontogenic origin, histologically resembles clear cell adenocarcinomas. Ultrastructural and histochemical features are described and support a non-glandular derivation. The intraosseous neoplasm is characterized by ovoid nests of clear or finely stippled cells with a mature collagenous stroma. These cells are PAS-positive, diastase labile and fail to bind alcian blue. Enzyme histochemical reactions disclose dehydrogenase, non-specific esterase, and acid phosphatase positivity. Fine structural characteristics include plasma membrane microvilli, desmosomes, endoplasmic reticulum, free ribosomes, glycogen rosettes and lysosomes. Many cells exhibit a paucity of cytoplasmic organelles with prominent vacuolization. Centrioles and annulate lamellae are also encountered. Summarily, clinical, radiographic, histochemical and ultrastructural features indicate that this neoplasm is probably of epithelial odontogenic origin with cytodifferentiation emulating glycogen-rich presecretory ameloblasts.


Subject(s)
Jaw Neoplasms/ultrastructure , Odontogenic Tumors/ultrastructure , Adenocarcinoma/ultrastructure , Cell Membrane/ultrastructure , Cell Nucleus/ultrastructure , Diagnosis, Differential , Histocytochemistry , Humans , Jaw Neoplasms/metabolism , Odontogenic Tumors/metabolism , Organoids/ultrastructure
19.
N Z Med J ; 95(701): 89, 1982 Feb 10.
Article in English | MEDLINE | ID: mdl-6952113
20.
N Z Med J ; 94(698): 470, 1981 Dec 23.
Article in English | MEDLINE | ID: mdl-6950302
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