Applied immunohistochemistry & molecular morphology : AIMM最新文献

{"title":"Human Epidermal Growth Factor Receptor-2 Promotes Invasion and Metastasis in Gastric Cancer by Activating Mitogen-activated Protein Kinase Signaling.","authors":"Feng Hou,&nbsp;Duan-Bo Shi,&nbsp;Yun-Qing Chen,&nbsp;Peng Gao","doi":"10.1097/PAI.0000000000000672","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000672","url":null,"abstract":"<p><p>Increasing evidence supports an important role for the human epidermal growth factor receptor-2 (HER2) gene and mitogen-activated protein kinase (MAPK) signaling pathways in the progression of human cancers by enhancing cancer cell metastasis and proliferation. However, the relationship between HER2 and MAPK signaling pathways in gastric cancer (GC) remains unclear. In the present study, dual in situ hybridization was performed to detect HER2 gene amplification and reverse transcription-quantitative polymerase chain reaction was used to investigate the mRNA expression of members of the MAPK signaling pathway, including rapidly accelerated fibrosarcoma (RAF), extracellular regulated signal-activated kinase (ERK), p38, and c-Jun N-terminal kinase (JNK), in 112 primary GC tissue samples. The results revealed that 19/112 (17%) of tissue samples showed positive amplification of HER2, which was correlated with tumor invasion and metastasis. Upregulation of RAF, ERK, p38, and JNK was also observed in samples associated with metastasis. Moreover, the expression levels of RAF and ERK in samples with HER2 gene amplification were significantly increased compared with those without HER2 amplification. However, the expression levels of both p38 and JNK were not significantly correlated with HER2 gene amplification. Our results simultaneously showed the association between HER2 gene amplification and the expression levels of MAPK signaling pathway proteins and clinicopathologic characteristics in GC. These findings provide the basis for investigating the regulation of MAPK signaling pathways by HER2 and potential therapeutic targets for inhibiting metastasis and invasion in GC.</p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"529-534"},"PeriodicalIF":1.6,"publicationDate":"2019-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000672","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40548521","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":"Gastrointestinal Stromal Tumor With Multiple Primary Tyrosine Kinase Mutations-Clinicopathologic and Molecular Characterization.","authors":"Newton A C S Wong,&nbsp;Philippe Taniere,&nbsp;Shaun Walsh,&nbsp;Andrew Wallace,&nbsp;Daisuke Nonaka,&nbsp;Thomas Jones,&nbsp;David Gonzalez","doi":"10.1097/PAI.0000000000000660","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000660","url":null,"abstract":"<p><p>A unique cohort of chemo-naive gastrointestinal stromal tumors (GISTs) with double-primary tyrosine kinase mutations was characterized particularly to determine whether coexistent mutations represent a single mutational event. Up to 2013, 4 UK centers reported 9 GISTs with 2 primary tyrosine kinase mutations. In each of 8 cases validated by next generation sequencing, both mutations were present in the same allele of the same exon (KIT exon 11 or 17, or PDGFRA exon 18). One case showed the second mutation only on some of the mutant alleles. Seven cases showed both mutations in all the reads, but in 2 cases, additional variants were found only in some reads. Clinicopathologic features of the 8 cases were similar to GISTs with single-primary mutations. When GIST genotyping rarely uncovers multiple tyrosine kinase variants in an exon, they occur in the same allele but are likely to represent separate mutational events and lack clinical significance.</p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"461-465"},"PeriodicalIF":1.6,"publicationDate":"2019-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000660","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39965558","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 Royal College of Pathologists of Australasia Quality Assurance Program: Immunohistochemistry Breast Marker Audit Overview 2005-2015.","authors":"Zenobia Ayesha Mohamed Haffajee,&nbsp;Beena Kumar,&nbsp;Glenn Francis,&nbsp;Martyn Peck,&nbsp;Tony Badrick","doi":"10.1097/PAI.0000000000000621","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000621","url":null,"abstract":"<p><p>The Royal College of Pathologists of Australasia Quality Assurance Program (RCPAQAP) Anatomical Pathology provides a comprehensive External Quality Assurance (EQA) exercise to review the reporting of immunohistochemistry (IHC) and in-situ hybridization (ISH) breast markers through an audit of clinical results. The aim of this exercise was to provide information regarding the quality of breast marker testing within clinical laboratories from 2005 to 2015. This comprehensive audit included estrogen, progesterone, and HER2 marker reporting. This was an important quality assurance activity established in response to ongoing difficulties experienced in laboratories in this area of testing.</p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"339-344"},"PeriodicalIF":1.6,"publicationDate":"2019-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000621","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35297229","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 Comprehensive Evaluation of Special AT-rich Sequence-binding Protein 2 (SATB2) Immunohistochemical Staining in Mucinous Tumors From Gastrointestinal and Nongastrointestinal Sites.","authors":"Benjamin D Ramos,&nbsp;Stefan Brettfeld,&nbsp;Ryan S Berry,&nbsp;Joshua K Routh,&nbsp;David R Martin,&nbsp;Joshua A Hanson","doi":"10.1097/PAI.0000000000000627","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000627","url":null,"abstract":"<p><p>Special AT-rich sequence-binding protein 2 (SATB2) is an accurate marker for conventional colorectal carcinoma (CRC), although its sensitivity and specificity in mucinous tumors from the colon and other sites remains unknown. The objective of this study is to evaluate the accuracy of SATB2 expression detected by immunohistochemical assay, as a marker of primary CRC in mucinous adenocarcinomas. SATB2 immunohistochemical stains were performed on whole sections from 63 conventional CRCs (controls), 47 mucinous CRCs (mCRC), and 182 noncolorectal mucinous tumors. SATB2 intensity was scored as 1 to 3 based on the estrogen receptor/progesterone receptor grading system, and the percent positive cells was scored in broad categories as follows: 0 (negative)≤5%, 1=5% to 49%, 2≥50%. An optimal sensitivity/specificity pairing (83% and 95%, respectively) was achieved in the mCRCs when the additive intensity and percent score was ≥3 (ie, intensity score+percent score=total score). Defining this total score (histologic score/\"H score\") as a \"positive\" result, the sensitivity of SATB2 for conventional CRC was 98% (62/63) versus 83% (39/47) for mCRCs (P=0.02); whereas 5% (9/182) of all noncolorectal mucinous tumors were considered positive. SATB2 especially demonstrated reduced specificity when applied to mucinous gastroesophageal and breast carcinomas, which showed significant expression in 27% and 9% of cases, respectively. In summary, SATB2 is a less sensitive marker of colorectal origin in mCRC compared with conventional CRC and shows significantly reduced specificity in mucinous gastroesophageal and breast primaries.</p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"378-385"},"PeriodicalIF":1.6,"publicationDate":"2019-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000627","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35683255","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 Biotin Tagging Immunoelectron Microscopy for Paraffin-embedded Sections.","authors":"Haruto Nishida,&nbsp;Kenji Kashima,&nbsp;Shinji Yano,&nbsp;Tsutomu Daa,&nbsp;Motoki Arakane,&nbsp;Yuzo Oyama,&nbsp;Takahiro Kusaba,&nbsp;Hiroko Kadowaki,&nbsp;Shigeo Yokoyama","doi":"10.1097/PAI.0000000000000735","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000735","url":null,"abstract":"<p><p>We herein introduce a novel method of biotin tagging immunoelectron microscopy for formalin-fixed, paraffin-embedded sections. This method was developed to utilize the antigenicity of biotin on epoxy-embedded ultrathin sections that could readily be recovered by a previously established antigen retrieval method as most monoclonal antibodies failed to recognize their targets by immunoelectron microscopy following antigen retrieval. The biotin tagging method was composed of preembedding immunostaining, epoxy-embedding and sectioning, and postembedding immunostaining steps. The preembedding step utilized the streptavidin-biotin-peroxidase complex method for immunohistochemistry to tag every antigen with a biotin in 3-μm thick paraffin-embedded sections. Next, fixation and processing for transmission electron microscopy (TEM) were performed on sections on glass slides, and ultrathin sections were prepared in epoxy-embedded blocks. In the postembedding step, antigen retrieval was followed by serial incubations with an antibiotin monoclonal antibody and anti-mouse IgG-labeled gold particles. The results obtained using antibodies against a variety of intracellular targets were satisfactory; positive gold particles were observed corresponding to targeted intracellular structures. This study demonstrated that the biotin tagging method was a convenient approach for successful labeling of paraffin-embedded sections for TEM using monoclonal antibodies, although it has relatively poor subcellular labeling quality.</p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"e42-e47"},"PeriodicalIF":1.6,"publicationDate":"2019-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000735","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37098268","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 Commentary: Quality Assurance in Immunohistochemistry.","authors":"Mogens Vyberg","doi":"10.1097/PAI.0000000000000771","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000771","url":null,"abstract":"A and reliable biomarker testing is essential to provide personalized medicine for cancer patients. Suboptimal immunohistochemical (IHC) assays may result in suboptimal diagnoses and treatment decisions. The rapid development of new methodologies, the introduction of novel predictive markers, and increasing quality expectations, make it of the utmost importance for laboratories continuously to focus on providing optimal staining results and identifying methodological errors. In contrast to most other laboratory methods, IHC is a qualitative, or at best a semiquantitative, method where the interpretation of diagnostic assays in cancer specimens typically is performed in the context of clinical information, tumor morphology, etc. Unexpected staining reactions may indicate a need for reevaluation of the staining quality, readout, and diagnosis, before concluding that the staining reaction is “aberrant.” Often a panel of IHC assays is used in tumor classification, making it easier to discover aberrant staining patterns, but the cause of these aberrations, whether technical errors or biological phenomena, due to unusual tumor expression, may not always be identified, for example, by restaining, especially if the diagnostic issue has been resolved by results of the other assays in the panel. In contrast, predictive assays for critical biomarkers, like HER2 and PD-L1, are standalone tests, where unidentified errors or wrong readouts have direct negative consequences for the patients. In this issue of AIMM, Steven Bogen’s paper, “A root cause analysis into the high error rate in clinical immunohistochemistry,”1 points out that clinical IHC is beset with a higher error rate than other types of clinical laboratory testing. In part, this is due to the inherent limitations in IHC, including the absence of standards, traceable units of measure, and true quantitative monitoring. However, it can be questioned if a comparison between IHC and other, strictly quantitative laboratory testing procedures is fair. Nevertheless, Bogen’s article is relevant for pathology laboratories, which may rely too much on judging their assay quality solely on “routine” and internal quality control, with inconsistent use of external quality assurance (EQA) programs, which often do not challenge the laboratories with sufficient rigor, for example, by failing to utilize EQA test tissues with low level of epitope expression that provide a truer test of assay sensitivity. Some EQA schemes do not utilize a central assessment of staining results in the QA sample (by an expert pathology panel), but leave it to the laboratories to assess their own staining results, introducing a further uncontrolled and unknown variable, namely interpretation by separate pathologists. This approach effectively denies the opportunity for different laboratories to compare their technical results with others in order to discover suboptimal assay performance. EQA or laboratory proficiency testing is, or should","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"327-328"},"PeriodicalIF":1.6,"publicationDate":"2019-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000771","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37162379","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":"Tissue Thickness Effects on Immunohistochemical Staining Intensity of Markers of Cancer.","authors":"Adrienne S McCampbell,&nbsp;Varun Raghunathan,&nbsp;May Tom-Moy,&nbsp;Richard K Workman,&nbsp;Rick Haven,&nbsp;Amir Ben-Dor,&nbsp;Ole F Rasmussen,&nbsp;Lars Jacobsen,&nbsp;Martin Lindberg,&nbsp;N Alice Yamada,&nbsp;Carol Schembri","doi":"10.1097/PAI.0000000000000593","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000593","url":null,"abstract":"<p><p>High-quality patient samples are required for reliable immunohistochemistry test outcomes that provide a significant benefit for patient care. Among the preanalytic variables in tissue handling, tissue thickness is thought to be easily controlled; however, whether the thickness of the tissue effects the staining intensity for antibody immunohistochemistry has not been quantitatively demonstrated. To investigate, we cut multiblock tissue sections of tonsil, liver, and kidney at 2, 4, 6, and 8 μm thicknesses. Interferometry measurements of the sectioned paraffin showed a <1 μm variation within a preset microtome thickness. Sections were then immunostained with antibodies targeting different cellular localizations; Ki-67 and BCL6 (nuclear), CD7 (membranous), and cytokeratin (cytoplasmic). A pathologist annotated regions of interest for each marker and performed brightfield and whole-slide visual scoring. Then a pixel-wise processing algorithm determined intensity of each pixel in these regions of interest and binned them into predetermined 0, 1+, 2+, or 3+ intensities. Visual scores from brightfield and whole-slide images were highly correlated to the percentage of pixels in each intensity bin. A stepwise increase was observed in pathologist scores and algorithmically defined percentage of pixels in each bin with increasing thickness demonstrating that changes in preset section thickness impacts staining intensity. The use of tissue thickness outside vendors' recommendations might change the intensity including the proportion of positive and negative cells and eventually the overall diagnosis outcome. Therefore, we recommend that tissue be consistently cut within the middle of thickness range specified by the assay manufacturer.</p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"345-355"},"PeriodicalIF":1.6,"publicationDate":"2019-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000593","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35650226","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":"Immunohistochemistry: Growing Pains, From a Stain to an Assay.","authors":"Clive R Taylor","doi":"10.1097/PAI.0000000000000770","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000770","url":null,"abstract":"T primary focus of AIMM (Applied Immunohistochemistry and Molecular Morphology) is intrinsic to its title, namely the use of immunohistochemical (IHC) and molecular methods for diagnostic purposes in a morphologic context. Accepted manuscripts fall generally into 2 classes: those that describe the detection of one or more analytes (biomarkers) in tissues (normal and diseased) as applied to diagnosis in anatomic pathology (AP), and those that focus on the underlying methods, rather than the potential value of individual biomarkers. In recent years the policy of AIMM has been to seek out and publish manuscripts from investigators whose work relates to improving the quality, reproducibility, and utility of the methods. The current issue of the Journal contains, by specific invitation, a thoughtful and thought-provoking review by Steven Bogen, bearing the title “A Root Cause Analysis Into The High Error Rate In Clinical Immunohistochemistry.”1 Dr Bogen is a clinical pathologist and the paper borrows from his extensive experience in the clinical laboratory, where error rates are very low. Dr Bogen delivers a novel perspective and analysis of many of the reasons for the observed discrepant error rates in IHC and offers some possible solutions, including novel standard controls. There is also an accompanying invited commentary by Mogens Vyberg, who is the founder of NordiQC, one of the foremost and most comprehensive AP external QC (Quality Control) programs. Dr Vyberg has penned a thoughtful response from the AP perspective.2 Dr Vyberg questions whether the comparison of IHC in the AP laboratory to high performance clinical laboratory assays is “fair.” It is a very good question, one that goes directly to the core of how IHC is used in the AP laboratory, and how its use increasingly must be considered in a modern “fit for purpose” context. Why are we doing this particular IHC test? In short, the question posed by Drs Bogen and Vyberg is “Can we convert an IHC stain to an assay, that purports actually to measure something?” The question is a good one because in seeking an answer, there is much to be learned, not least of which is that having learned, the learning is of no value unless applied in daily practice in AP. In addition, both process and outcome must be closely monitored, issues raised by both Drs Bogen and Vyberg. As an example, AIMM in the past several years has published a “control series” of papers3,4 with recommendations, that if universally adopted, would certainly lead to major overall improvements within and across AP laboratories. But adoption is slow. Then there is another problem, of even greater in import. Not only is there much to be learned, but also there is much to be “unlearned”: the AP laboratory is handicapped by its legacy; it performs stains, not assays, and we in AP have acquired many bad habits. The first use of IHC (immunoperoxidase) method performed on formalin-fixed paraffin embedded tissues for the express purpose of ","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"325-326"},"PeriodicalIF":1.6,"publicationDate":"2019-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000770","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37136874","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":"Androgen Receptors in Resected Ductal Carcinoma In Situ of Breast: Novel Insights With Possible Implications for Testing and Targeted Endocrine Chemoprevention Trials.","authors":"Olaronke Oshilaja,&nbsp;Laila Nomani,&nbsp;Benjamin C Calhoun,&nbsp;Alberto J Montero,&nbsp;Charles D Sturgis","doi":"10.1097/PAI.0000000000000625","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000625","url":null,"abstract":"<p><p>Mammary ductal carcinoma in situ (DCIS) is classically treated by combinations of excision, radiation, and endocrine therapy, based upon the specific needs of individual patients. Estrogen receptor (ER) status is generally assessed by immunohistochemistry (IHC) in newly diagnosed cases of DCIS, and endocrine therapy in this setting is thought to be chemopreventive. The potential impact of androgens on mammary carcinogenesis has been studied in recent years, and several authors have proposed androgen receptor (AR) IHC testing and targeted antiandrogenic therapy in patients with locally advanced or metastatic triple-negative invasive breast cancer (ie, negative for ER and progesterone receptor and HER-2). Very little has been published on AR in DCIS. We report results of AR IHC on archival tissue blocks from 221 adult female patients, each of whom underwent definitive breast resection of DCIS. Of the 221 cases, 72 (33%) were shown to express AR in their DCIS at or above the 10% threshold often used for invasive carcinoma. AR expression was seen in all grades of DCIS. Of the 72 positive AR cases, 21 (29%) were ER negative, corresponding to 10% (21/221) of all patients. The majority of the AR-positive cases were high grade, and the most common histologic subtype in this subset was a solid growth pattern with apocrine features. Early data from clinical trials evaluating AR antagonists in invasive/metastatic triple-negative breast cancer suggest that some patients may benefit from androgen blockade. IHC testing and potential clinical trials of AR antagonists for chemoprevention in patients with AR-positive and ER-negative DCIS could be considered.</p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"373-377"},"PeriodicalIF":1.6,"publicationDate":"2019-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000625","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35870226","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":"Liver Metastases From Renal Oncocytoma With Vascular Extension.","authors":"Giovanni Cacciamani,&nbsp;Luca Cima,&nbsp;Miriam Ficial,&nbsp;Giovanni Novella,&nbsp;Salvatore Siracusano,&nbsp;Umberto Tedeschi,&nbsp;Matteo Balzarro,&nbsp;Umberto Montin,&nbsp;Maria A Cerruto,&nbsp;Vincenzo De Marco,&nbsp;Antonio B Porcaro,&nbsp;Ondrej Hes,&nbsp;Antonia DʼErrico,&nbsp;Guido Martignoni,&nbsp;Claudio Ghimenton,&nbsp;Gianluigi Zaza,&nbsp;Walter Artibani,&nbsp;Matteo Brunelli,&nbsp;Albino Eccher","doi":"10.1097/PAI.0000000000000490","DOIUrl":"https://doi.org/10.1097/PAI.0000000000000490","url":null,"abstract":"<p><p>The 2016 World Health Organization Renal Tumor Classification defines renal oncocytoma (RO) as a benign epithelial tumor; however, malignant histopathologic features have been documented. Rare cases with metastases have been reported. We describe the case of a 62-year-old woman who was referred to the Urology Clinic for a routine work-up. Magnetic resonance imaging and computerized tomography showed a 7-cm mass in the middle and lower portions of the left kidney and 2 suspected liver metastases. The patient underwent surgery. Microscopically both renal and liver lesions presented solid, solid-nested, and microcystic architecture, composed predominantly of large eosinophilic cells without any worrisome pattern except the vascular extension. The cells were positive for S100A1, CD117, and PAX-8 and negative for CAIX, CK7, and AMACR. Fluorescence in situ hybridization showed a disomic profile for the chromosomes 1, 2, 6, 7, 10, 17. No mutation of coding sequence of the SDHB, SDHC, SDHD, VHL, and BHD genes and no loss of heterozygosity at 3p were found. The final diagnosis was \"RO\" according to the 2016 World Health Organization Renal Tumor Classification with \"liver metastases.\" This report provides a wide clinical-pathologic, immunophenotypical and molecular documentation of a RO with liver metastases.</p>","PeriodicalId":520562,"journal":{"name":"Applied immunohistochemistry & molecular morphology : AIMM","volume":" ","pages":"e48-e53"},"PeriodicalIF":1.6,"publicationDate":"2019-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/PAI.0000000000000490","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35146937","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}