66 research outputs found
Non-hormonal strategies for managing menopausal symptoms in cancer survivors: an update
Vasomotor symptoms, particularly hot flushes (HFs), are the most frequently reported symptom by menopausal women. In particular, for young women diagnosed with breast cancer, who experience premature ovarian failure due to cancer treatments, severe HFs are an unsolved problem that strongly impacts on quality of life. The optimal management of HFs requires a personalised approach to identify the treatment with the best benefit/risk profile for each woman. Hormonal replacement therapy (HRT) is effective in managing HFs but it is contraindicated in women with previous hormone-dependent cancer. Moreover, many healthy women are reluctant to take HRT and prefer to manage symptoms with non-hormonal strategies. In this narrative review, we provide an update on the current available non-oestrogenic strategies for HFs management for women who cannot, or do not wish to, take oestrogens. Since isoflavones have oestrogenic properties and it is not known if they can be safely consumed by women with previous hormonedependent cancer, they were excluded. Selective serotonin reuptake inhibitors/selective serotonin-norepinephrine reuptake inhibitors, as well as other neuroactive agents, some herbal remedies and behavioural strategies are considered
Joint recommendations for the diagnosis and treatment of vulvo-vaginal atrophy in women in the peri- and post-menopausal phases from the Società Italiana per la Menopausa (SIM) and the Società Italiana della Terza Età (SIGiTE)
Spleen cell proliferation during and after skin myiasis by human bot fly Dermatobia hominis
Prediction of Protein Binding Regions in Disordered Proteins
Many disordered proteins function via binding to a structured partner and undergo
a disorder-to-order transition. The coupled folding and binding can confer
several functional advantages such as the precise control of binding specificity
without increased affinity. Additionally, the inherent flexibility allows the
binding site to adopt various conformations and to bind to multiple partners.
These features explain the prevalence of such binding elements in signaling and
regulatory processes. In this work, we report ANCHOR, a method for the
prediction of disordered binding regions. ANCHOR relies on the pairwise energy
estimation approach that is the basis of IUPred, a previous general disorder
prediction method. In order to predict disordered binding regions, we seek to
identify segments that are in disordered regions, cannot form enough favorable
intrachain interactions to fold on their own, and are likely to gain stabilizing
energy by interacting with a globular protein partner. The performance of ANCHOR
was found to be largely independent from the amino acid composition and adopted
secondary structure. Longer binding sites generally were predicted to be
segmented, in agreement with available experimentally characterized examples.
Scanning several hundred proteomes showed that the occurrence of disordered
binding sites increased with the complexity of the organisms even compared to
disordered regions in general. Furthermore, the length distribution of binding
sites was different from disordered protein regions in general and was dominated
by shorter segments. These results underline the importance of disordered
proteins and protein segments in establishing new binding regions. Due to their
specific biophysical properties, disordered binding sites generally carry a
robust sequence signal, and this signal is efficiently captured by our method.
Through its generality, ANCHOR opens new ways to study the essential functional
sites of disordered proteins
Effect of steriles states on lepton magnetic moments and neutrinoless double beta decay
Comparisons of Allergenic and Metazoan Parasite Proteins:Allergy the Price of Immunity
Allergic reactions can be considered as maladaptive IgE immune responses towards environmental antigens. Intriguingly, these mechanisms are observed to be very similar to those implicated in the acquisition of an important degree of immunity against metazoan parasites (helminths and arthropods) in mammalian hosts. Based on the hypothesis that IgE-mediated immune responses evolved in mammals to provide extra protection against metazoan parasites rather than to cause allergy, we predict that the environmental allergens will share key properties with the metazoan parasite antigens that are specifically targeted by IgE in infected human populations. We seek to test this prediction by examining if significant similarity exists between molecular features of allergens and helminth proteins that induce an IgE response in the human host. By employing various computational approaches, 2712 unique protein molecules that are known IgE antigens were searched against a dataset of proteins from helminths and parasitic arthropods, resulting in a comprehensive list of 2445 parasite proteins that show significant similarity through sequence and structure with allergenic proteins. Nearly half of these parasite proteins from 31 species fall within the 10 most abundant allergenic protein domain families (EF-hand, Tropomyosin, CAP, Profilin, Lipocalin, Trypsin-like serine protease, Cupin, BetV1, Expansin and Prolamin). We identified epitopic-like regions in 206 parasite proteins and present the first example of a plant protein (BetV1) that is the commonest allergen in pollen in a worm, and confirming it as the target of IgE in schistosomiasis infected humans. The identification of significant similarity, inclusive of the epitopic regions, between allergens and helminth proteins against which IgE is an observed marker of protective immunity explains the 'off-target' effects of the IgE-mediated immune system in allergy. All these findings can impact the discovery and design of molecules used in immunotherapy of allergic conditions
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