A pigmented calcifying cystic odontogenic tumor associated with compound odontoma: a case report and review of literature

<p>Abstract</p> <p>Background</p> <p>Pigmented intraosseous odontogenic lesions are rare with only 47 reported cases in the English literature. Among them, pigmented calcifying cystic odontogenic tumor, formerly known as calcifying odontogenic cyst, is the most common lesion with 20 reported cases.</p> <p>Methods</p> <p>A case of pigmented calcifying cystic odontogenic tumor associated with odontoma occurring at the mandibular canine-premolar region of a young Japanese boy is presented with radiographic, and histological findings. Special staining, electron microscopic study and immunohistochemical staining were also done to characterize the pigmentation.</p> <p>Results</p> <p>The pigments in the lesion were confirmed to be melanin by Masson-Fontana staining and by transmission electron microscopy. The presence of dendritic melanocytes within the lesion was also demonstrated by S-100 immunostaining.</p> <p>Conclusion</p> <p>The present case report of pigmented calcifying cystic odontogenic tumor associated with odontoma features a comprehensive study on melanin and melanocytes, including histochemical, immunohistochemical and transmission electron microscopic findings.</p

Epstein-Barr Virus Stimulates Torque Teno Virus Replication: A Possible Relationship to Multiple Sclerosis

Viral infections have been implicated in the pathogenesis of multiple sclerosis. Epstein-Barr virus (EBV) has frequently been investigated as a possible candidate and torque teno virus (TTV) has also been discussed in this context. Nevertheless, mechanistic aspects remain unresolved. We report viral replication, as measured by genome amplification, as well as quantitative PCR of two TTV-HD14 isolates isolated from multiple sclerosis brain in a series of EBV-positive and -negative lymphoblastoid and Burkitt's lymphoma cell lines. Our results demonstrate the replication of both transfected TTV genomes up to day 21 post transfection in all the evaluated cell lines. Quantitative amplification indicates statistically significant enhanced TTV replication in the EBV-positive cell lines, including the EBV-converted BJAB line, in comparison to the EBV-negative Burkitt's lymphoma cell line BJAB. This suggests a helper effect of EBV infections in the replication of TTV. The present study provides information on a possible interaction of EBV and TTV in the etiology and progression of multiple sclerosis

Primers and probes used.

a<p>- F, forward; R, reverse; Pr, probe.</p>b<p>- Underlined letters indicate restriction sites.</p

In vitro replication of TTV-HD14b and TTV-HD14c as measured by long-PCR amplification.

<p>(A) PCR amplification of full-length TTV-HD14b in P3HR-1, BJAB, BJAB/EBV and full-length TTV-HD14c in ND1 and Ramos/EBV cell lines. Days after transfection are indicated. M - DNA size marker, C1 - untransfected cells, C2 - untransfected cells with nucleofector solution, <b>+</b> - positive control for long PCR amplification consisted either of re-ligated TTV-HD14b or TTV-HD14c mixed with Ramos cell line DNA. (B) Electron micrograph of B95-8 cells 3 days after transfection with linearized TTV-HD14b DNA. TTV-like particles can be seen within the nucleus of a cell. EBV particles are indicated by short arrows. Bar = 250 nm.</p

Quantification of EBV-genomes and -replication.

<p>Real-time qPCR in the EBV positive cell lines transfected with TTV-HD14c (day 14 post-transfection) was applied to determine the EBV genome copies per cell, as well as EBV replication as measured by gp350/220 mRNA.</p

In vitro replication of TTV-HD14b and TTV-HD14c as measured by real-time quantitative PCR.

<p>Replication of (A) TTV-HD14b and (B) TTV-HD14c. qPCR values are expressed in ΔΔCt relative to BJAB (used as calibrator). Shown are mean ±95% confidence interval values of triplicate tests. A significant higher replication level of both TTV isolates was detected in all cell lines when compared to BJAB (p<%0.05).</p

Expressions of E2 and E7-HPV16 proteins in pre-malignant and malignant lesions of the uterine cervix

Continuous production of the E7 protein from different types of high risk human papilloma virus (HPV) is required for progression of malignancy. We developed antibodies against HPV type 16 E7 and E2 proteins to evaluate their utility as markers for diagnosis during early stages of cervical cancer. Forty biopsies from uterine cervices were diagnosed as low grade intraepithelial lesion (LSIL), high grade intraepithelial lesion (HSIL), squamous carcinoma (SC), in situ adenocarcinoma (ISA) and invasive adenocarcinoma (AC), all of which were infected with HPV 16. Immunohistochemistry was used to investigate the expressions of E7 and E2 (both from HPV 16) and p16. P16 was expressed in eight of 12 LSILs, in all HSILs, in 16 of 18 SC and in all ACs. E2 was expressed in six of 12 LSILs. E7 was positive in eight of 12 LSILs and in all HSIL and carcinomas. The expressions of E2 and E7 of HPV16 related to p16 expression confirmed the value of the viral oncogenic proteins as complementary to histology and support the carcinogenic model of the uterine cervix, because HPVDNA integration into cellular DNA implies the destruction of the gene encoding E2, which suppresses the expression of the E6 and E7 oncoproteins. E2 from HPV16 could be marker for LSILs, while E7 could be a marker for progression of LSILs to HSILs in patients infected by HPV16, because viral typing has little positive predictive value.Fil: Ramírez, N.. Furtwangen University; AlemaniaFil: Guerra, Fernando Andres. Universidad de Buenos Aires. Hospital de Clínicas; ArgentinaFil: Camporeale, Gabriela. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Quintana, S.. Instituto Fares Taie. Laboratorio de Biología Molecular; ArgentinaFil: Diaz, L. B.. Universidad de Buenos Aires. Hospital de Clínicas; ArgentinaFil: Cuneo, N.. Hospital de Oncología María Curie; ArgentinaFil: Villacorta Hidalgo, J.. Universidad de Buenos Aires. Hospital de Clínicas; ArgentinaFil: Tatti, S. A.. Universidad de Buenos Aires. Hospital de Clínicas; ArgentinaFil: Alonso, Leonardo Gabriel. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Borkosky, Silvia Susana. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: de Prat Gay, Gonzalo. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Palaoro, L.. Universidad de Buenos Aires. Hospital de Clínicas; Argentin

Sumoylation of ING2 regulates the transcription mediated by Sin3A.

International audienceING2 (inhibitor of growth 2) is a candidate tumor-suppressor gene involved in cell cycle control, apoptosis and senescence. Although the functions of ING2 within the chromatin remodeling complex Sin3A/histone deacetylase (HDAC) and in the p53 pathway have been described, how ING2 itself is regulated remains unknown. In this study we report for the first time that ING2 can be sumoylated by small ubiquitin-like modifier 1 (SUMO1) on lysine 195 both in vitro and in vivo. Strikingly, ING2 sumoylation enhances its association with Sin3a. We provide evidences that ING2 can bind to the promoter of genes to mediate their expression and that sumoylation of ING2 is required for this binding to some of these genes. Among them, we identified the gene TMEM71 (transmembrane protein 71), whose expression is regulated by ING2 sumoylation. ING2 must be sumoylated to bind to the promoter of TMEM71 and to recruit the Sin3A chromatin-modifying complex to this promoter, in order to regulate TMEM71 transcription. Hence, sumoylation of ING2 enhances its binding to the Sin3A/HDAC complex and is required to regulate gene transcriptions