Novel Markers of Pancreatic Adenocarcinoma in Fine-Needle Aspiration: Mesothelin and Prostate Stem Cell Antigen Labeling Increases Accuracy in Cytologically Borderline Cases

McCarthy, Denis M.; Maitra, Anirban; Argani, Pedram; Rader, Anne E.; Faigel, Douglas O.; Heek, N. Tjarda van; Hruban, Ralph H.; Wilentz, Robb E.

doi:10.1097/00129039-200309000-00006

Cited by 99 publications

(61 citation statements)

References 25 publications

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“…Not surprisingly, all top candidates have been identified in previous studies and well described in the literature. [23][24][25][26][27][28][29][30][31] A special approach was used to identify pancreasspecific markers. Pancreatic ductal adenocarcinoma develops from ductal epithelial cells that compose only a small percentage of all pancreatic cells (with acinar and islet cells composing the majority) in the normal pancreas.…”

Section: Marker Candidate Selectionmentioning

confidence: 99%

A Quantitative Reverse Transcriptase-Polymerase Chain Reaction Assay to Identify Metastatic Carcinoma Tissue of Origin

Talantov

Baden

Jatkoe

et al. 2006

The Journal of Molecular Diagnostics

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Identifying the primary site in patients with metastatic carcinoma of unknown primary origin can enable more specific therapeutic regimens and may prolong survival. Twenty-three putative tissue-specific markers for lung, colon, pancreatic, breast, prostate, and ovarian carcinomas were nominated by querying a gene expression profile database and by performing a literature search. Ten of these marker candidates were then selected based on validation by reverse transcriptase-polymerase chain reaction (RT-PCR) on 205 formalin-fixed, paraffin-embedded metastatic carcinoma specimens originating from these six and from other cancer types. Next, we optimized the RNA isolation and quantitative RT-PCR methods for these 10 markers and applied the quantitative RT-PCR assay to a set of 260 metastatic tumors. We then built a gene-based algorithm that predicted the tissue of origin of metastatic carcinomas with an overall leaveone-out cross-validation accuracy of 78%. Lastly, our assay demonstrated an accuracy of 76% when tested on an independent set of 48 metastatic samples, 37 of which were either a known primary or initially presented as carcinoma of unknown primary but were subsequently resolved.

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Section: Marker Candidate Selectionmentioning

confidence: 99%

A Quantitative Reverse Transcriptase-Polymerase Chain Reaction Assay to Identify Metastatic Carcinoma Tissue of Origin

Talantov

Baden

Jatkoe

et al. 2006

The Journal of Molecular Diagnostics

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“…42,43). Although interesting progresses have been done with mesothelin and the prostate stem cell antigen (44), physicians are still awaiting for a specific marker of the pancreatic malignancy with interest both in diagnostic and eventually in targeting the pancreatic neoplastic cell.…”

Section: Discussionmentioning

confidence: 99%

Monoclonal antibody 16D10 to the COOH-terminal domain of the feto-acinar pancreatic protein targets pancreatic neoplastic tissues

Benkoël

Bernard²,

Payan-Defais³

et al. 2009

Molecular Cancer Therapeutics

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We have shown that the 16D10 antigen located on the mucin-like COOH-terminal domain of the feto-acinar pancreatic protein (FAPP) is expressed at the surface of human pancreatic tumor cell lines such as SOJ-6 cell line. Furthermore, an in vivo study indicates that targeting this cell-membrane glycopeptide by the use of the monoclonal antibody (mAb) 16D10 inhibits the growth of SOJ-6 xenografts in nude mice. To validate the potential use of the mAb16D10 in immune therapy, this study examined the expression of 16D10 antigens at the surface of human pancreatic adenocarcinomas versus control tissues. We examined the reactivity of mAb16D10 and mAb8H8 with pancreatic ductal adenocarcinomas (PDAC) compared with controls by using immunohistochemistry and confocal laser scanning microscopy. mAb8H8 does react with control or nontumoral human pancreatic tissues. mAb16D10 has a strong and specific reactivity with PDAC and does not react with other cancers of epithelia or normal tissues tested. Notable, mAb16D10 mostly recognizes membrane of tumoral cells. Furthermore, mAb8H8 and mAb16D10 recognized a protein of 110 to 120 kDa in homogenates of nontumoral and tumoral human pancreatic tissues, respectively. This size correlates with that of FAPP or with that of the normal counterpart of FAPP, the so-called bile salt-dependent lipase. The results suggest that mAb16D10 presents a unique specificity against PDAC; consequently, it could be effective in immune therapy of this cancer. Furthermore, mAb16D10 and mAb8H8 pair might be useful for diagnosis purpose in discriminating tumoral from nontumoral human pancreatic tissues. [Mol Cancer Ther 2009;8(2):282 -91]

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“…26,27 Although these molecular techniques definitely have a potential role in the improvement of the sensitivity and specificity of the pancreatic FNAs, they are not available to many laboratories as routine tests. Search for immunohistochemical markers that might be helpful in the cytologic differentiation of the pancreatic lesions in FNA specimens prompted us to choose as a potentially useful tool a panel of mucin markers comprising 4 apomucins-MUC1, 2, 5AC, and 6.…”

Section: Discussionmentioning

confidence: 99%

Diagnostic utility of mucin profile in fine-needle aspiration specimens of the pancreas

Giorgadze

Peterman

Baloch

et al. 2006

Cancer

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Novel Markers of Pancreatic Adenocarcinoma in Fine-Needle Aspiration: Mesothelin and Prostate Stem Cell Antigen Labeling Increases Accuracy in Cytologically Borderline Cases

Cited by 99 publications

References 25 publications

A Quantitative Reverse Transcriptase-Polymerase Chain Reaction Assay to Identify Metastatic Carcinoma Tissue of Origin

A Quantitative Reverse Transcriptase-Polymerase Chain Reaction Assay to Identify Metastatic Carcinoma Tissue of Origin

Monoclonal antibody 16D10 to the COOH-terminal domain of the feto-acinar pancreatic protein targets pancreatic neoplastic tissues

Diagnostic utility of mucin profile in fine-needle aspiration specimens of the pancreas

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