Shoplifting Behavior Among Patients With an Eating Disorder at a Medical Correctional Center in Japan: A Cross-Sectional Study.

Purpose: In Japan, the incarceration of patients with eating disorders (EDs) owing to repeated shoplifting has become a social issue. This study examined the shoplifting behavior of inmates with EDs at our medical correctional center, with the objective of delineating their characteristics, identifying an adequate treatment plan, and preventing recidivism. Methods: The participants consisted of 32 incarcerated patients with EDs (22 females, 10 males) charged with shoplifting, from a medical correctional center in East Japan. A cross-sectional study was employed. Data were collected by retrieving the patients' medical records and through individual interviews conducted by psychiatrists. Results: The food-specific shoplifting ED group (those who had never shoplifted anything other than food) had a core pathology of the binge-purge type of anorexia nervosa with juvenile onset (p = 0.044). Furthermore, they demonstrated an average gap of 8 years between the onset of ED and their first shoplifting episode. The non-specific shoplifting ED group (those who shoplifted food and other items) typically shoplifted before the onset of ED (p = 0.001). They experienced the onset of ED after incarceration (p = 0.004) and had comorbid disorders (p = 0.024). The food-specific group required a psychosocial approach focusing on maintaining healthy body weight and mental stability, whereas the non-specific group required multiple forms of support for substance abuse and behavioral addiction, as well as interventions to reduce impulsive behavior. Conclusion: Early intervention is necessary to improve the prognosis of patients with EDs and shoplifting behavior.

Identification of allergens in the box jellyfish Chironex yamaguchii that cause sting dermatitis.

BACKGROUND: Jellyfish stings cause painful, papular-urticarial eruptions due to the immediate allergic, acute toxic and persistent inflammatory responses. In spite of many marine accidents and their economic impact, modes of first-aid treatment remain conventional and specific allergen and medical treatment are not yet available. The purpose of this study was to define the specific allergen of the box jellyfish Chironex yamaguchii and to study the precise mechanism of the resulting dermatitis. METHODS: We comprehensively studied the immunoglobulin-binding molecules from the box jellyfish C. yamaguchii with a purification procedure and Western blotting, using sera from 1 patient and from several controls. RESULTS: From the nematocyst wall and spine, we detected IgG-binding acidic glycoprotein (of 66 and 30 kDa) as determined by Western blot and ion-exchange chromatography. In addition, the 66-kDa protein was found to be an asparagine residue-coupled N-linked glycoprotein and the epitope resided in the protein fraction. We found that CqTX-A, the major toxic protein of the nematocyst, is also a heat-stable IgE-binding allergen. This was confirmed as a 45-kDa protein by Western blot from both nematocyst extracts and purified CqTX-A. CONCLUSIONS: The detection of these proteins may, in part, explain the combined immediate allergic-toxic and persistent allergic responses. Hopefully, our findings will lead to the development of specific venom immunotherapy for marine professional workers and tourists for jellyfish-sting dermatitis and anaphylaxis.

Inhibitory effect of ganglioside on mastoparan-induced cytotoxicity and degranulation in lipid raft of connective tissue type mast cell.

Antihistamine, the most important drug for Hymenoptera stinging, cannot attenuate cytotoxicity and mast cell direct activation by mastoparan that is the most abundant polypeptides in the venoms of social wasps. The aim of this study was to investigate whether gangliosides inhibit the effect of mastoparan on mast cells activation. The degranulation and cytotoxicity in canine cutaneous mastocytoma cells (CM-MC) were done by measurement of ß-hexosaminidase release and MTT assay. Lipid raft was isolated with discontinuous sucrose gradient centrifuge for the analysis of distribution of Gα(q) and Gα(i) protein by western blotting. We found that mastoparan induced the degranulation in (CM-MC) via direct activation of Gα(i) and Gα(q) with a decrease in their amount in lipid raft. Ganglioside G(D1a) (disialoganglioside) and G(M1) (monosialoganglioside) strongly reduced the degranulation and cytotoxicity through stabilizing the structure of lipid raft domain. In addition, mastoparan generated intracellular reactive oxygen species (ROS) independently from cytotoxicity, through arachidonic cascade but not G-protein activations. Crude wasp venom showed cytotoxicity and induction of the release from CM-MC, which were potently reduced by gangliosides. We show here that mastoparan activates both Gα(i) and Gα(q) protein and that the exogenous ganglioside G(D1a) and G(M1) inhibit the degranulation and cytotoxicity through stabilizing lipid raft. Gangliosides have potentials to be therapeutic tool or clinical prophylaxis for wasp stinging.

Gangliosides inhibit bee venom melittin cytotoxicity but not phospholipase A(2)-induced degranulation in mast cells.

Sting accident by honeybee causes severe pain, inflammation and allergic reaction through IgE-mediated anaphylaxis. In addition to this hypersensitivity, an anaphylactoid reaction occurs by toxic effects even in a non-allergic person via cytolysis followed by similar clinical manifestations. Auto-injectable epinephrine might be effective for bee stings, but cannot inhibit mast cell lysis and degranulation by venom toxins. We used connective tissue type canine mast cell line (CM-MC) for finding an effective measure that might inhibit bee venom toxicity. We evaluated degranulation and cytotoxicity by measurement of ß-hexosaminidase release and MTT assay. Melittin and crude bee venom induced the degranulation and cytotoxicity, which were strongly inhibited by mono-sialoganglioside (G(M1)), di-sialoganglioside (G(D1a)) and tri-sialoganglioside (G(T1b)). In contrast, honeybee venom-derived phospholipase A(2) induced the net degranulation directly without cytotoxicity, which was not inhibited by G(M1), G(D1a) and G(T1b). For analysis of distribution of Gα(q) and Gα(i) protein by western blotting, lipid rafts were isolated by using discontinuous sucrose gradient centrifuge. Melittin disrupted the localization of Gα(q) and Gα(i) at lipid raft, but gangliosides stabilized the rafts. As a result from this cell-based study, bee venom-induced anaphylactoid reaction can be explained with melittin cytotoxicity and phospholipase A(2)-induced degranulation. Taken together, gangliosides inhibit the effect of melittin such as degranulation, cytotoxicity and lipid raft disruption but not phospholipase A(2)-induced degranulation in mast cells. Our study shows a potential of gangliosides as a therapeutic tool for anaphylactoid reaction by honeybee sting.

Tea catechins have dual effect on mast cell degranulation induced by compound 48/80.

Green tea catechins are emerging as one of the most efficient and safest ingredient in health promoting food. We investigated catechin's effects on intracellular ROS generation in mast cell activation and degranulation. Compound 48/80, receptor mimetic basic secretagogues for mast cell, induced ROS generation dose-dependently with bell-shaped degranulation pattern in canine cutaneous mastocytoma cells (CM-MC). When intracellular ROS level was relatively low, catechins decreased both ROS and the degranulation. However, when intracellular ROS level was remarkably high, catechins decreased ROS level but increased the degranulation paradoxically. Gallocatechins showed the stronger effects than non-gallated catechins. Exogenous H(2)O(2) also shows dual effect on degranulation dose-dependently. EGCG shows the dual effect on the tyrosine and threonine phosphorylation depending on the concentration of compound 48/80. Particularly, 60 kDa protein tyrosine-phosphorylated by EGCG with 3 microg/ml of compound 48/80 might be a negative regulator for the degranulation. Taken together, there is an optimal level of ROS for the degranulation, and the catechins have a dual function by controlling ROS level.

Inhibition of NADPH oxidase subunits translocation by tea catechin EGCG in mast cell.

The inhibitory mechanism of tea catechins for allergy remains undefined. We studied the effect of catechins, mainly EGCG, on the activation of mast cell line canine cutaneous mastocytoma cells (CM-MC). Compound 48/80 induced the degranulation in CM-MC dose dependently, whereas its release of beta-hexosaminidase was inhibited by EGCG and O-methylated EGCG (EGCG-Me). Both catechins were found to inhibit intracellular ROS generation dose dependently together with DPI. Intracellular ROS generation in human polymorphonuclear leukocytes was also inhibited by EGCG. Neither L-NAME, ebeselen nor NAC inhibited ROS generation. From the Western blot analysis of the subunits components of NADPH oxidase, we detected cytosolic subunits; p47(phox), p67(phox), p40(phox), rac2 and membrane subunits; gp91(phox), p22(phox) in CM-MC. Cytosolic subunits were translocated from cytosol to membrane time dependently after stimulation with compound 48/80. EGCG and DPI inhibited cytosolic subunits from translocating into membrane. These data suggest that EGCG inhibits the activation of NADPH oxidase in CM-MC.

Enhanced expression of CD69 and CD25 antigen on human peripheral blood mononuclear cells by prolactin.

Several clinical reports have suggested that prolactin (PRL) plays an important role in the pathogenesis of autoimmune diseases such as rheumatoid arthritis (RA) or systemic lupus erythematosus (SLE). We have investigated the influence of PRL on immune system, by evaluating the effects of PRL on the expression of CD69 and CD25 on human peripheral blood mononuclear cells (PBMCs). Human PBMCs obtained from healthy female volunteers were incubated with phytohemagglutinin (PHA) in the presence or absence of various concentrations of PRL. The expression of CD69 and CD25 was monitored using immunofluorescence staining and flow cytometry. PRL significantly enhanced the expression of CD69 and CD25 on activated PBMCs compared with that in the absence of PRL (p<0.05, paired t-test). Increasing doses of PRL enhanced the expression of CD69 up to 2 microg/ml and CD25 up to 1 microg/ml. The enhanced expression of CD69 was observed on CD8+ T lymphocytes but not on CD4+ T lymphocytes. Our data suggest that PRL can significantly enhance the expression of CD69 and CD25 molecule on human PBMCs when induced by PHA. However, PRL would have to be at optimal concentration in order to enhance their expression.

Canine mast cell activation via human IgG1 and IgG4.

BACKGROUND: We have reported that canine mastocytoma-derived CM-MC cells are activated via canine IgG and express a high-affinity IgG receptor (canine FcgammaRI). The predicted amino acid sequence of the canine FcgammaRI alpha subunit was found to be 72% similar to that of humans. These results suggest that canine FcgammaRI have binding activity with human IgG and led us to investigate CM-MC activation via canine FcgammaRI and human IgG. METHODS: The binding of human IgG to canine FcgammaRI was examined by flow cytometry using FITC-conjugated human IgG. [Ca2+]i increase or histamine release via canine FcgammaRI and the four human IgG subclasses was measured following aggregation of IgG-bound FcgammaRIs by anti-human IgG. To determine the binding activity of canine FcgammaRI with human IgG1 or IgG3, the displacement of 125I-labeled canine IgG from canine FcgammaRI was examined by unlabeled human IgG1 or IgG3. RESULTS: The fluorescence intensity of CM-MC cells was markedly (about 50 times) elevated by incubation with FITC-human IgG compared with the fluorescence of the control cells. A significant (p < 0.01) calcium response and histamine release were observed following aggregation of canine FcgammaRIs bound with human IgG1 or IgG4. 125I-labeled canine IgG was displaced from canine FcgammaRI by preincubation with unlabeled total human IgG or human IgG1 dose-dependently, whereas no displacement was detected by preincubation with human IgG3. CONCLUSIONS: Canine FcgammaRI possesses a significant binding activity with human IgG1 or IgG4, while IgG2 or IgG3 did not significantly react with canine FcgammaRI on CM-MC cells.

Presence and primary sequence of a high-affinity IgG receptor on canine mastocytoma (CM-MC) cells.

Mast cells play a central role in IgE-dependent allergic responses. Although they have been reported to express only low-affinity IgG receptors and no high-affinity receptors (FcgammaRI), our recent study showed that canine mastocytoma CM-MC cells are activated by monomeric canine IgG, suggesting the presence of FcgammaRI on CM-MC cells. In the present study, we measured the affinity of canine IgG with CM-MC cells, determined the presence of the FcgammaRI protein and mRNA, and identified the cDNA sequence of it. The results showed that (7.5+/-3.1)x10(4) receptor molecules are expressed on a CM-MC cell with a Ka of (9.1+/-1.6)x10(7)M(-1) for binding to monomeric canine IgG. Canine IgG-conjugated beads precipitated an approximately 72-kDa surface protein, whose size is consistent with that of the FcgammaRI alpha subunit of humans and mouse. The expression of FcgammaRI mRNA was detected by reverse transcriptase polymerase chain reaction (RT-PCR), and the cDNA encoding the FcgammaRI alpha subunit was found to be 84% and 78% similar to that of humans and the mouse, respectively. The predicted amino acid sequence was 72% and 63% identical, respectively. Canine mastocytoma CM-MC cells are therefore very useful for studying FcgammaRI-mediated signal transduction in mast cells.

The canine mast cell activation via CRP.

We report here canine mastocytoma-derived cell (CMMC) activation via two pentraxin, limulus- and human-CRP. Mast cell chemotaxis was measured by Boyden's blindwell chamber. To confirm that the cell migration was chemotactic, "checkerboard" analysis was performed. We used Fura-2 to investigate CRP-mediated cytosolic calcium elevation. To examine whether CRP-induced stimulation is mediated through G-proteins, CMMC were incubated with pertussis toxin (PTx) before use in chemotaxis assay and Ca(2+) mobilization. CMMC migration in response to CRP was both chemokinetic and chemotactic. Limulus-CRP induced a transient Ca(2+)-mobilization dose-dependently. Preincubation of the cells with PTx inhibited CRP chemotaxis and Ca(2+)-mobilization, suggesting that G-proteins of the Gi-class are involved in the chemotaxis. We suggest that CRP may participate in the migration of mast cells to inflamed tissues during an acute-phase response. CRP-mediated recruitment of mast cells might play an important role in hypersensitivity and inflammatory processes.

IgG-mediated signal transduction in canine mastocytoma-derived cells.

BACKGROUND: We have reported canine cutaneous mastocytoma-derived cells named CM-MC sensitized with monomeric IgG released histamine upon anti-IgG stimulation. However, IgG or IgE-mediated signal transduction in the cells remains to be examined. METHODS: Monomeric IgG-binding to cells was measured by flow cytometry using FITC-anti-IgG. IgG-mediated protein tyrosine phosphorylation was studied by Western blotting using anti-phosphotyrosine antibody. We monitored the intracellular Ca(2+) concentration ([Ca(2+)](i)) when IgG-primed cells were activated with anti-canine IgG. Release of Ca(2+) from intracellular stores was analyzed with thapsigargin in the absence of extracellular Ca(2+). The Ca(2+) entry via store-operated Ca(2+) channel from the external environment was characterized using Ba(2+), Ni(2+) and EGTA. Cells sensitized with canine serum abundant in IgG and IgE or heat-inactivated serum were activated by anti-canine IgG or anti-canine IgE. The effect of extracellular Ca(2+) and reaction time on IgG-mediated histamine release was examined. Staurosporine and ER-27319 were used to clarify the IgG-mediated protein tyrosine phosphorylation. RESULTS: Abundant IgG-binding sites on the cell were detected by FACS analysis. Anti-IgG induced rapid protein tyrosine phosphorylation and [Ca(2+)](i) elevation. When extracellular Ca(2+) was excluded by EGTA, a mild and transient increase in [Ca(2+)](i) was observed, indicating the release of Ca(2+) from anti-IgG-sensitive intracellular Ca(2+) stores. The constant Ba(2+) entry from external environment proved the Ca(2+) influx occurred mainly via a store-operated Ca(2+) channel which was inhibited by Ni(2+) and EGTA. Canine serum-sensitized cells showed a rapid and sustained increase in [Ca(2+)](i) upon both anti-IgG and anti-IgE stimulation. The [Ca(2+)](i) elevation induced by anti-IgE was decreased in the cells sensitized with heat-inactivated serum. Histamine release from CM-MCs was absolutely dependent on extracellular Ca(2+), and reached equilibrium within 5 min. Staurosporine inhibited the tyrosine phosphorylation of 38-, 65-, 70-, 80-kD proteins. ER-27319 inhibited the tyrosine phosphorylation of 38- and 70-kD proteins. Staurosporine also inhibited IgG-mediated [Ca(2+)](i) elevation and histamine release in a dose-dependent manner. CONCLUSIONS: Canine cutaneous mastocytoma-derived (CM-MC) cells were activated by both IgG- and IgE-mediated mechanisms. IgG-mediated protein tyrosine phosphorylation and Ca(2+) influx were similar to those mediated by IgE. CM-MC cells are useful for the study of allergic inflammation caused by IgG-dependent mechanisms.