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Introduction : As HIV-infected patients get older more non-AIDS-related malignancies are to be seen. Cancer now represents almost one third of all causes of deaths among HIV-infected patients [1]. Albeit bladder cancer is one of the most common malignancy worldwide [2], only 13 cases of bladder cancer in HIV-infected patients have been reported in the literature so far [3]. Materials and Methods : We conducted a monocentric study in our hospital. We selected all patients who were previously admitted (from 1998 to 2013) in our hospital with diagnoses of HIV and bladder cancer. The objective was to assess the prevalence and characteristics of bladder cancers in HIV-infected patients in our hospital. Results : Based on our administrative HIV database (6353 patients), we found 15 patients (0.2%) with a bladder cancer. Patients’ characteristics are presented in Table 1. Patients were mostly men and heavy smokers. Their median nadir CD4 cell count was below 200 and most had a diagnosis of AIDS. A median time of 14 years was observed in those patients, between the diagnosis of HIV-infection and the occurrence of bladder cancer, although in patients much younger (median age 56) than those developing bladder cancer without HIV infection (71.1 years) [4]. Haematuria was the most frequent diagnosis circumstance in HIV-infected patients who had relatively preserved immune function on highly active antiretroviral therapy (HAART). Histopathology showed relatively advanced cancers at diagnosis with a high percentage of non transitional cell carcinoma (TCC) tumor and of TCC with squamous differentiation, suggesting a potential role for human papilloma virus (HPV) co-infection. Death rate was high in this population. Conclusions : Bladder cancers in HIV-infected patients remain rare but occur in relatively young HIV-infected patients with a low CD4 nadir, presenting with haematuria, most of them being smokers, and have aggressive pathological features that are associated with severe outcomes. (Published: 2 November 2014) Citation : Chawki S et al. Journal of the International AIDS Society 2014, 17(Suppl 3) :19647 http://www.jiasociety.org/index.php/jias/article/view/19647 | http://dx.doi.org/10.7448/IAS.17.4.19647

Objective To investigate the prognostic value of loss of heterozygosity (LOH) at chromosome 9p in patients with non–muscle-invasive bladder cancer (NMI-BC). Methods Between 2000 and 2006, we included in the study 84 patients with NMI-BC. LOH analyses were performed on tumor tissue using 3 microsatellite markers at chromosome 9p. Associations of LOH with recurrence and progression of the tumors were evaluated. Results Frequency of LOH at 9p was 11.1%, 29.0%, and 31.6% in pTaG1, pTaG2, and pT1G3 tumors, respectively. Recurrence occurred in 27 patients. None of the markers was able to predict recurrence. Progression occurred in 9.5% of the cases, with progression to muscle-invasive bladder cancer (MI-BC) in 4.8% of the cases. LOH at IFN-α was significantly associated with progression to MI-BC (P = .006). In the case of LOH at IFN-α, 2-year progression-free survival and progression-free survival to MI-BC were both 59.3%, compared with 97.1% and 98.6%, respectively, in case of conservation of LOH in multivariable analysis, LOH at IFN-α remained statistically associated with progression and progression to MI-BC. LOH at IFN-α was a significant and independent predicting factor of progression and progression to MI-BC, with P = .05 and 0.01 (HR 4.8 for progression; HR 24.2 for muscle invasion). Conclusions Our study suggests that LOH at IFN-α is an independent prognostic factor for progression to MI-BC. LOH analysis of bladder tumors may help in the management of NMI-BC. Specifically, it could be of use in selecting patients for early aggressive treatment and/or in planning close follow-up schedule.

Longtemps considérée comme une maladie unique, l'amylose est aujourd'hui reconnue comme la marque histologique d'un ensemble de maladies, les amyloses. L'amylose est la voie finale commune, chez l'homme et dans de nombreuses espèces animales, de l'agrégation pathologique de plus de vingt protéines appartenant à des familles dénuées de relation fonctionnelle ou structurale. Les mécanismes de formation de ces agrégats commencent à être mieux connus. L'étape centrale, que l'on peut artificiellement reproduire in vitro, est un changement de conformation d'une protéine native en une protéine apte à l'auto-agrégation, sous une forme essentiellement formée de feuillets β. Le traitement actuel des amyloses, qui consiste à réduire la disponibilité en protéine amyloïde, n'est pas pleinement satisfaisant. La reconnaissance progressive des différentes étapes de ce phénomène pathologique a conduit à la conception de cibles thérapeutiques nouvelles : stabilisation de la protéine native, désagrégation des structures déjà β-plissées ou, encore, inhibition des liaisons avec certains composants du tissu conjonctif. Différentes approches, pharmacologiques et immunologiques, sont à l'étude sur des systèmes cellulaires et des modèles animaux, et certaines molécules sont parvenues au stade de l'essai clinique chez l'homme., Amyloidosis bears many characteristics of orphan diseases. Its diagnosis is difficult and often delayed. The main reasons thereof are its quite various clinical presentation: amyloidosis behaves as a new great masquerader, and the need to get a tissue sample to submit to specific dyes. Although we have been able for a long time to recognize amyloid, its intimate nature has remained quite completely enigmatic until recently. In fact, major advances in this way have appeared only in the last decade and it is now possible to consider the mechanisms of amyloidosis as a multistep phenomenon. Amyloidosis is no more thought only as a « storage disease » of the extracellular space. This archaic viewpoint has shifted to the emerging paradigm of misfolded protein disorders. Amyloid proteins thus appear as a subgroup of misfolded proteins, where misfolding leads to subsequent aggregation. This aggregation may be a generic property of polypeptide chains possibly linked to their common peptide backbone that does not depend on specific amino acid sequences. And, in fact, many proteins can in vitro form amyloid-like aggregates, while in vivo, only 20 amyloid proteins have been so far identified. Although misfolding and aggregation are quite well studied in vitro, the last step of amyloid deposition, i.e. anchorage to the extracellular matrix, can not be so easily approached. Proteoglycans and serum amyloid P component have nevertheless been identified as key elements involved in extracellular deposition of amyloid proteins. These advances have opened new avenues in the therapeutic of amyloid disorders. Current treatment consists of support or replacement of impaired organ function and measures to reduce the production of amyloidogenic precursor proteins. Potential novel therapeutic strategies include stabilisation of the native fold of precursor proteins with targeted small molecules, reversion of misfolded proteins to their native state with « beta-sheet breakers », inhibition of amyloid fibril propagation and enhancement of amyloid clearance either through immunotherapy or by reducing the stability of deposits through depletion of serum amyloid P component, and breaking the anchorage to the extracellular matrix with glycosaminoglycan analogs.