Applied immunohistochemistry & molecular morphology : AIMM最新文献

{"title":"Sorting Nexin 2 (SNX2): a potential marker of active thyrocytes in normal and hyperfunctioning thyroid disorders.","authors":"Maki Kanzawa,&nbsp;Shigeo Hara,&nbsp;Shuho Semba,&nbsp;Hiroshi Yokozaki,&nbsp;Mitsuyoshi Hirokawa,&nbsp;Tomoo Itoh","doi":"10.1097/PAI.0b013e31828badd3","DOIUrl":"https://doi.org/10.1097/PAI.0b013e31828badd3","url":null,"abstract":"<p><p>Sorting nexins (SNXs) are a large, diverse group of cytoplasmic and membrane-associated proteins that function in a variety of cellular processes, including endocytosis, protein trafficking, and the retrieval of transmembrane proteins. In this study, we demonstrated that SNX2 is expressed in columnar and active thyroid follicular cells but not in flattened inactive thyrocytes. Morphometric analysis revealed a significant correlation between SNX2 positivity and columnar cell morphology. Immunohistochemical staining of serial sections of the thyroid tissue indicated that SNX2 localization was similar to sortilin, a protein expressed by active thyrocytes. Expression of SNX2 in thyrocytes is particularly marked and extensive in most hyperstimulated thyroid disorders, including Graves disease (diffusely SNX2 positive in 73.3% patients) and functioning nodules (93.8% patients). SNX2 immunolocalization in hyperstimulated follicular epithelial cells was specific among the SNXs family members examined. These results support the utility of SNX2 as a novel marker of active thyrocytes and reflect the endosomal trafficking activity in these cells. </p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"302-7"},"PeriodicalIF":1.6,"publicationDate":"2014-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0b013e31828badd3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40228334","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Whole-slide, quadruple immunofluorescence labeling of routinely processed paraffin sections.","authors":"Serena Buscone,&nbsp;Maria C Argentieri,&nbsp;Daniela Pilla,&nbsp;Giorgio Cattoretti","doi":"10.1097/PAI.0b013e31829928e7","DOIUrl":"https://doi.org/10.1097/PAI.0b013e31829928e7","url":null,"abstract":"<p><p>Whole-slide images (WSI) have acquired a stable place in diagnostic histopathology and immunohistochemistry. Immunofluorescence (IF) techniques hold a limited and selective role in diagnostics (eg, renal and cutaneous pathology) and so far remain excluded from the digital pathology evolution, with notable exceptions, such as quantitative immunopathology. We explored the ability of a commercial fluorescent slide scanner to provide 4-color IF WSI from routinely processed tissues. With minor modifications and a careful match between filters and fluorochromes, we show that 4-color IF WSI can be obtained from routine material with negligible autofluorescence, good sensitivity, and diagnostic power. </p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"e1-7"},"PeriodicalIF":1.6,"publicationDate":"2014-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0b013e31829928e7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40267376","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The association of urocortin expression with clinicopathologic parameters of gastric adenocarcinomas.","authors":"Ming-Fang Cheng,&nbsp;Wen-Chiuan Tsai,&nbsp;Lin Yu-Chieh,&nbsp;Kan-Tai Hsia,&nbsp;Jong-Shiaw Jin","doi":"10.1097/PAI.0b013e31828adbfa","DOIUrl":"https://doi.org/10.1097/PAI.0b013e31828adbfa","url":null,"abstract":"<p><p>Gastric adenocarcinoma is a lethal disease with high incidence in Chinese people. The purpose of this study was to evaluate the expression of urocortin (UCN) in normal gastric mucosa and gastric adenocarcinomas. Immunohistochemical analysis of UCN was performed in 112 surgical specimens (21 normal gastric mucosa specimens and 91 gastric adenocarcinoma specimens varying in histologic grade and pathologic stage). Immunostain intensity was scored on a scale ranging from 0 (absence of staining) to 3 (strong staining). The percentage of UCN stained cells was scored on a scale ranging from 0 (<5%) to 4 (75% to 100%). The UCN immunoscore (ranging from 0 to 12) was the product of the above 2 scores. The UCN immunoscore was high in all 9 normal gastric mucosa specimens, significantly lower in poorly differentiated gastric adenocarcinoma than in well and moderately differentiated tumors (P=0.018), and significantly lower in more advanced pathologic stages of gastric adenocarcinomas than in the early stages of these tumors. Moreover, UCN expression was higher in gastric adenocarcinomas with neuroendocrine differentiation than in mucinous adenocarcinomas and signet-ring cell carcinomas. In conclusion, UCN is expressed in most non-neoplastic gastric glandular epithelia. However, UCN expression inversely correlates with higher tumor grade and advanced TNM stage in gastric adenocarcinomas. </p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"288-94"},"PeriodicalIF":1.6,"publicationDate":"2014-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0b013e31828adbfa","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40228330","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Performance evaluation comparison of 3 commercially available PCR-based KRAS mutation testing platforms.","authors":"Julia A Adams,&nbsp;Kristin M Post,&nbsp;Sarah A Bilbo,&nbsp;Xiaoyan Wang,&nbsp;Joyashree D Sen,&nbsp;Anita J Cornwell,&nbsp;Amanda J Malek,&nbsp;Liang Cheng","doi":"10.1097/PDM.0b013e3182a127f9","DOIUrl":"https://doi.org/10.1097/PDM.0b013e3182a127f9","url":null,"abstract":"<p><p>The identification of KRAS mutations in patients with certain types of cancer, including colonic adenocarcinoma and non-small cell lung carcinoma, has become increasingly important as these patients are contraindicated from receiving epidermal growth factor receptor-targeted therapies. Several polymerase chain reaction (PCR)-based tests are commercially available for KRAS mutation testing including Applied Biosystems KRAS Mutation Analysis on the ABI3130xl, Qiagen therascreen KRAS RGQ PCR on the Rotor-Gene Q MDx, and Qiagen KRAS Pyro on the PyroMark Q24; however, these tests have not been compared side by side. The purpose of this study was to evaluate the performance characteristics and workflow for 3 PCR-based methods of detecting KRAS mutation status. We evaluated the performance characteristics and workflow for 3 commercially available KRAS mutation detection platforms. All of the 188 samples run were successful, with 29% being positive for the KRAS mutation. Of the positive tests, Applied Biosystems detected 84% of the positive cases, whereas Qiagen therascreen RGQ and Qiagen KRAS Pyro detected 100% of the positive cases. In cases of discrepancy between Applied Biosystems and therascreen RGQ, Pyro agreed with therascreen RGQ 95% of the time. Qiagen therascreen RGQ and Pyro were comparable in terms of sensitivity, specificity, positive predictive value, negative predictive value, and accuracy, with all values being 100%. All 3 techniques accurately identified the appropriate mutation in the known control specimens. In summary, all 3 tests are relatively comparable for detecting the KRAS mutation, with Applied Biosystems having a slightly lower sensitivity, negative predictive value, and accuracy than therascreen RGQ and Pyro. </p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"231-5"},"PeriodicalIF":1.6,"publicationDate":"2014-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PDM.0b013e3182a127f9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40297116","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correlation of the Rac1/RhoA pathway with ezrin expression in osteosarcoma.","authors":"Caterina Chiappetta,&nbsp;Martina Leopizzi,&nbsp;Fabiana Censi,&nbsp;Chiara Puggioni,&nbsp;Vincenzo Petrozza,&nbsp;Carlo D Rocca,&nbsp;Claudio Di Cristofano","doi":"10.1097/PDM.0000000000000033","DOIUrl":"https://doi.org/10.1097/PDM.0000000000000033","url":null,"abstract":"<p><p>Osteosarcoma is the most common malignant tumor of the bone. The major cause of death in osteosarcoma is the increase in metastatic potential, and the ezrin expression has been correlated with the metastasis development. Ezrin interacts with RhoGDI by dissociating it from RhoGTPases, which allow GTPases to load with GTP, activate RhoA to increase cell migration, and invasion. RhoGTPases have been found to contribute to pathologic processes including cancer cell migration, invasion, and metastasis and overexpression of either the GTPase itself or some elements of Rho signaling that have been detected in many human tumors, including Rac1 and RhoA. We have analyzed Rac1 and RhoA expression in the osteosarcoma tissues to understand the role of the ezrin-Rho family pathway in osteosarcoma metastatic progression. Moreover, we have blocked the ezrin expression using siRNA assay to investigate a possible correlation with RAC1 and RHOA expression in the osteosarcoma cell lines. Our immunohistochemical data showed that many osteosarcomas presented cytoplasmatic positivity for both Rac1 and RhoA and cases, both ezrin positive than ezrin negative, revealed the protein expression of Rac1 and RhoA. The results obtained by ezrin siRNA transfection showed that ezrin expression in the osteosarcoma cell lines might modulate, mainly, the Rac1 expression. It is possible that the mechanism of cell motility mediated by Rac1 and RhoA is maintained in osteosarcomas, and since the expression of ezrin, Rac1 and RhoA do not correlate with metastatic progression in osteosarcoma. However, osteosarcomas without metastasis displayed a positivity for Rac1 and RhoA expression compared with metastatic osteosarcomas and this could be a protective factor. </p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"162-70"},"PeriodicalIF":1.6,"publicationDate":"2014-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PDM.0000000000000033","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40297948","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A study of alveolar rhabdomyosarcoma copy number alterations by single nucleotide polymorphism analysis.","authors":"Miriam Lynn,&nbsp;Naisha Shah,&nbsp;Judith Conroy,&nbsp;Sean Ennis,&nbsp;Thomas Morris,&nbsp;David Betts,&nbsp;Maureen O'Sullivan","doi":"10.1097/PDM.0000000000000030","DOIUrl":"https://doi.org/10.1097/PDM.0000000000000030","url":null,"abstract":"<p><p>Rhabdomyosarcoma, the most common pediatric soft tissue malignancy arises in 2 major histologic forms: embryonal and alveolar. Classically, the alveolar subtype is characterized by a chromosomal translocation t(2;13)(q35;q14) or t(1;13)(p36;q14) fusing the PAX3 or PAX7 gene, respectively, to the FOXO1 gene, although fusion-negative cases of alveolar rhabdomyosarcoma (ARMS) occur; these share considerably more with the genomic profiles and biological behavior of embryonal rhabdomyosarcoma than with fusion-positive ARMS. The current understanding of any additional genetic aberrations in fusion-positive ARMS is limited. In this study, we evaluated tumor-specific copy number alterations in a cohort of fusion-positive ARMSs using high-resolution technology. The results presented here include previously described changes as well as completely novel findings of copy number alterations in BCR and DICER. The study furthermore highlights associations between fusion type and genotype, as well as outcomes and genotype. Rearrangement of PAX7 is strongly associated with copy number alteration of Glypican 5 (GPC5) and moderately with amplification of IGF1R. There is a moderate association between death from/relapse of disease and, on the one hand, amplification of 12q13.3 (DDIT3; Gli1), and on the other hand, copy number alteration of Wnt6 or LRP1B. Gains of both LRP1B and Gli1 in turn are strongly associated with MycN amplification. </p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"213-21"},"PeriodicalIF":1.6,"publicationDate":"2014-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PDM.0000000000000030","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40297115","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Negative reagent controls in diagnostic immunohistochemistry: do we need them? An evidence-based recommendation for laboratories throughout the world.","authors":"Richard W Cartun","doi":"10.1097/PAI.0000000000000043","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000043","url":null,"abstract":"During the development and application of immunohistochemical techniques to diagnostic pathology, controls have played an important role in ensuring that the appropriate result has been obtained. The positive control is a tissue or collection of cells that contains the target protein (antigen) and confirms that the primary antibody and detection system have worked properly. The negative control, used primarily for primary antibody validation, is a specimen that does not contain the target protein and, as a result, should show no immunoreactivity. The negative reagent control (NRC) is an additional tissue section (frozen or paraffin) or cytology smear prepared from the patient specimen that is treated identically to that of the test slide(s) except for the omission of the primary antibody. Its primary purpose is to identify nonspecific reactivity due to factors or components other than the primary antibody. In the early days of diagnostic immunohistochemistry, the NRC was important because of the use of crude detection systems that often showed cross-reactivity with endogenous immunoglobulins (Fig. 1A) or with other proteins present in the test specimen that could be confused with specific immunoreactivity. In addition, with the introduction of avidin-biotin–based detection, nonspecific reactivity with endogenous biotin was frequently observed, especially following heat-induced epitope retrieval complicating interpretation (Fig. 1B). The introduction of sensitive and specific polymer-based detection systems has eliminated most of these issues.1 A critical examination of the use of NRCs in diagnostic immunohistochemistry today reveals several issues in play. First and foremost, they consume precious tissue or cells that could be used for additional testing. This is especially true today, when laboratories are seeing more fine-needle aspirate biopsy specimens and diagnostic needle cores that require ancillary immunohistochemical and/or molecular testing for targeted therapies for patients with cancer. Second, depending on the type of laboratory running the immunohistochemical tests (eg, general surgical pathology vs. a specialty laboratory such as urology, GI, or GYN), NRCs can represent as much as 50% of the slides in a given run (personal observation). This overwhelming volume can be a major burden on the staff and the instruments processing these slides. Finally, laboratories incur a major expense in terms of labor, supplies, and reagents for running these additional slides, for which there is no reimbursement. As a result, the routine use of NRCs in diagnostic immunohistochemistry has been challenged.2 In 2008, I made a decision to stop running NRCs routinely except for antibodies requiring avidin-biotin detection. My decision was based on 3 factors: (1) the","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"159-61"},"PeriodicalIF":1.6,"publicationDate":"2014-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000043","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40293297","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Overexpression of survivin and caspase 3 in oral carcinogenesis.","authors":"Sopee Poomsawat,&nbsp;Jirapa Punyasingh,&nbsp;Paisarn Vejchapipat","doi":"10.1097/PAI.0b013e31828a0d0c","DOIUrl":"https://doi.org/10.1097/PAI.0b013e31828a0d0c","url":null,"abstract":"Survivin is an inhibitor of apoptosis protein that inhibits caspase 3 function. While cytoplasmic survivin suppresses apoptosis, nuclear survivin regulates cell division. Little is known about the subcellular localization of survivin in oral carcinogenesis. This study examined the subcellular distribution of these 2 proteins in oral squamous cell carcinoma (OSCC) and premalignant lesions including oral leukoplakia (OL) with and without dysplasia. Expression of survivin and caspase 3 were immunohistochemically analyzed in 114 samples including OSCC, OL with and without dysplasia, and normal oral mucosa (NM). Cytoplasmic and nuclear positive cells were counted separately. The results were presented as the frequency of positive cases. The positive expression rates of cytoplasmic and nuclear survivin in OSCC were significantly higher than in NM, OL with and without dysplasia. NM showed a low rate of cytoplasmic survivin expression compared to OL with and without dysplasia. The numbers of cytoplasmic and nuclear expression of caspase 3 in OSCC were significantly higher than that of NM, OL with and without dysplasia. In conclusion, the overexpression of cytoplasmic survivin in OSCC and premalignant lesions suggest that suppression of apoptosis by survivin occurs at early and late stages of oral carcinogenesis. The elevated expression of nuclear survivin and caspase 3 in OSCC indicate that at the late stage survivin increases cell proliferation whereas caspase 3 promotes apoptosis.","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"65-71"},"PeriodicalIF":1.6,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0b013e31828a0d0c","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40227371","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Significant expression of thyroid transcription factor-1 in pulmonary squamous cell carcinoma detected by SPT24 monoclonal antibody and CSA-II system.","authors":"Kenji Kashima,&nbsp;Hisashi Hashimoto,&nbsp;Haruto Nishida,&nbsp;Motoki Arakane,&nbsp;Naomi Yada,&nbsp;Tsutomu Daa,&nbsp;Shigeo Yokoyama","doi":"10.1097/PAI.0b013e31828acad2","DOIUrl":"https://doi.org/10.1097/PAI.0b013e31828acad2","url":null,"abstract":"<p><p>In contrast to the usefulness of thyroid transcription factor-1 (TTF-1) in distinguishing primary adenocarcinoma of the lung from metastatic lesions, TTF-1 expression in pulmonary squamous cell carcinoma is reported to be at low level and not a suitable immunohistochemical marker. We hypothesized that the highly sensitive detection system, CSA-II, can visualize even faint expression of TTF-1 in pulmonary squamous cell carcinoma. In this study, 2 commercially available clones of TTF-1 monoclonal antibody, 8G7G3/1 and SPT24, were used for staining 38 cases of pulmonary squamous cell carcinoma, in combination with the CSA-II and the conventional detection system, EnVision. The combined use of the 8G7G3/1 clone with EnVision and CSA-II showed a positive reaction in only 1 and 4 cases, respectively. The use of SPT24 clone showed positive staining in 5 cases with EnVision and in 20 of 38 cases (52.6%) with the CSA-II. Interestingly, positive staining by the SPT24-CSA-II technique of samples from tissue blocks preserved for <2 years was 73.6% compared with only 31.5% in those preserved for >2 years. In addition, a 6-month preservation of the cut sections resulted in stain fading and decreased positivity (50%), compared with freshly cut sections. We conclude that the use of the SPT24 monoclonal antibody with the CSA-II system can detect even weak expression of TTF-1 in pulmonary squamous cell carcinoma. This staining technique can potentially allow the discrimination of primary squamous cell carcinoma of the lung from metastatic lesions, especially in freshly prepared paraffin sections. </p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"119-24"},"PeriodicalIF":1.6,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0b013e31828acad2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40228329","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Practicing pathology in the era of big data and personalized medicine.","authors":"Jiang Gu,&nbsp;Clive R Taylor","doi":"10.1097/PAI.0000000000000022","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000022","url":null,"abstract":"<p><p>The traditional task of the pathologist is to assist physicians in making the correct diagnosis of diseases at the earliest possible stage to effectuate the optimal treatment strategy for each individual patient. In this respect surgical pathology (the traditional tissue diagnosis) is but a tool. It is not, of itself, the purpose of pathology practice; and change is in the air. This January 2014 issue of Applied Immunohistochemistry and Molecular Morphology (AIMM) embraces that change by the incorporation of the agenda and content of the journal Diagnostic Molecular Morphology (DMP). Over a decade ago AIMM introduced and promoted the concept of \"molecular morphology,\" and has sought to publish molecular studies that correlate with the morphologic features that continue to define cancer and many diseases. That intent is now reinforced and extended by the merger with DMP, as a logical and timely response to the growing impact of a wide range of genetic and molecular technologies that are beginning to reshape the way in which pathology is practiced. The use of molecular and genomic techniques already demonstrates clear value in the diagnosis of disease, with treatment tailored specifically to individual patients. Personalized medicine is the future, and personalized medicine demands personalized pathology. The need for integration of the flood of new molecular data, with surgical pathology, digital pathology, and the full range of pathology data in the electronic medical record has never been greater. This review describes the possible impact of these pressures upon the discipline of pathology, and examines possible outcomes. There is a sense of excitement and adventure. Active adaption and innovation are required. The new AIMM, incorporating DMP, seeks to position itself for a central role in this process.</p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"1-9"},"PeriodicalIF":1.6,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000022","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31944097","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}