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      The use of variations in proteomes to predict, prevent, and personalize treatment for clinically nonfunctional pituitary adenomas

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          Abstract

          Pituitary adenomas account for ∼10% of intracranial tumors, and they cause the compression of nearby structures and the inappropriate expression of pituitary hormones. Unlike functional pituitary adenomas, nonfunctional (NF) pituitary adenomas account for ∼30% of pituitary tumors, and are large enough to cause blindness; because they do not cause any clinical hormone hypersecretion, they are difficult to detect at an early stage; and hypopituitarism results. No effective molecular biomarkers or chemical therapy have been approved for the clinical setting. Because an NF pituitary adenoma is highly heterogeneous, differences in the proteins (the proteome) can distinguish among those heterogeneity structures. The components of a proteome dynamically change as an NF adenoma progresses. Changes in protein expression and protein modifications, individually or in combination, might be biomarkers to predict the disease, monitor the tumor progression, and develop an accurate molecular classification for personalized patient treatment. The modalities of proteomic variation might also be useful in the interventional prevention and personalized treatment of patients to halt the occurrence and progression of NF pituitary adenomas.

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          Most cited references85

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          Mitogen-activated protein kinases in apoptosis regulation.

          Cells are continuously exposed to a variety of environmental stresses and have to decide 'to be or not to be' depending on the types and strength of stress. Among the many signaling pathways that respond to stress, mitogen-activated protein kinase (MAPK) family members are crucial for the maintenance of cells. Three subfamilies of MAPKs have been identified: extracellular signal-regulated kinases (ERKs), c-Jun N-terminal kinases (JNKs), and p38-MAPKs. It has been originally shown that ERKs are important for cell survival, whereas JNKs and p38-MAPKs were deemed stress responsive and thus involved in apoptosis. However, the regulation of apoptosis by MAPKs is more complex than initially thought and often controversial. In this review, we discuss MAPKs in apoptosis regulation with attention to mouse genetic models and critically point out the multiple roles of MAPKs.
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            Use of proteomic patterns in serum to identify ovarian cancer.

            New technologies for the detection of early-stage ovarian cancer are urgently needed. Pathological changes within an organ might be reflected in proteomic patterns in serum. We developed a bioinformatics tool and used it to identify proteomic patterns in serum that distinguish neoplastic from non-neoplastic disease within the ovary. Proteomic spectra were generated by mass spectroscopy (surface-enhanced laser desorption and ionisation). A preliminary "training" set of spectra derived from analysis of serum from 50 unaffected women and 50 patients with ovarian cancer were analysed by an iterative searching algorithm that identified a proteomic pattern that completely discriminated cancer from non-cancer. The discovered pattern was then used to classify an independent set of 116 masked serum samples: 50 from women with ovarian cancer, and 66 from unaffected women or those with non-malignant disorders. The algorithm identified a cluster pattern that, in the training set, completely segregated cancer from non-cancer. The discriminatory pattern correctly identified all 50 ovarian cancer cases in the masked set, including all 18 stage I cases. Of the 66 cases of non-malignant disease, 63 were recognised as not cancer. This result yielded a sensitivity of 100% (95% CI 93--100), specificity of 95% (87--99), and positive predictive value of 94% (84--99). These findings justify a prospective population-based assessment of proteomic pattern technology as a screening tool for all stages of ovarian cancer in high-risk and general populations.
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              Global analysis of protein activities using proteome chips.

              To facilitate studies of the yeast proteome, we cloned 5800 open reading frames and overexpressed and purified their corresponding proteins. The proteins were printed onto slides at high spatial density to form a yeast proteome microarray and screened for their ability to interact with proteins and phospholipids. We identified many new calmodulin- and phospholipid-interacting proteins; a common potential binding motif was identified for many of the calmodulin-binding proteins. Thus, microarrays of an entire eukaryotic proteome can be prepared and screened for diverse biochemical activities. The microarrays can also be used to screen protein-drug interactions and to detect posttranslational modifications.
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                Author and article information

                Contributors
                +1-901-4482976 , +1-901-4487842 , xzhan@uthsc.edu
                Journal
                EPMA J
                EPMA J
                The EPMA Journal
                Springer Netherlands (Dordrecht )
                1878-5077
                1878-5085
                29 June 2010
                September 2010
                : 1
                : 3
                : 439-459
                Affiliations
                [1 ]Charles B. Stout Neuroscience Mass Spectrometry Laboratory, The University of Tennessee Health Science Center, 847 Monroe Avenue, Room 117, Memphis, TN 38163 USA
                [2 ]Department of Neurology, The University of Tennessee Health Science Center, 847 Monroe Avenue, Room 117, Memphis, TN 38163 USA
                [3 ]Clinical and Translational Science Institute, The University of Tennessee Health Science Center, 847 Monroe Avenue, Room 117, Memphis, TN 38163 USA
                [4 ]Department of Molecular Science, The University of Tennessee Health Science Center, 847 Monroe Avenue, Room 117, Memphis, TN 38163 USA
                [5 ]University of Tennessee Cancer Institute, The University of Tennessee Health Science Center, 847 Monroe Avenue, Room 117, Memphis, TN 38163 USA
                [6 ]The Charles B. Stout Neuroscience Mass Spectrometry Laboratory, Department of Neurology, University of Tennessee Health Science Center, 847 Monroe Avenue, Room 108, Memphis, TN 38163 USA
                Article
                28
                10.1007/s13167-010-0028-z
                3405333
                23199087
                4b850b13-77bb-4d44-82b9-6a300b98f677
                © European Association for Predictive, Preventive and Personalised Medicine 2010
                History
                : 10 April 2010
                : 19 May 2010
                Categories
                Review Article
                Custom metadata
                © European Association for Predictive, Preventive and Personalised Medicine 2010

                Molecular medicine
                clinical nonfunctional pituitary adenoma,proteomic variation,predictive diagnosis,tumor progression monitoring,interventional prevention,personalized patient treatment

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