TY  - JOUR
AB  - We analyzed expression of genes associated with metabolism of chemotherapeutic drugs in locally advanced esophageal adenocarcinomas before and after neoadjuvant chemotherapy to study whether there is a change in gene expression induced by chemotherapy and whether such changes are associated with tumor response or nonresponse. We included 21 patients with locally advanced esophageal adenocarcinomas treated by cisplatin- and 5-fluorouracil (5-FU)-based neoadjuvant chemotherapy before surgery. Messenger RNA was extracted from formalin-fixed, paraffin-embedded preoperative endoscopic esophageal tumor biopsy specimens and tumor tissue specimens after surgical resection. Expression levels of chemotherapy metabolism-associated genes thymidylate synthase (TYMS), thymidine phosphorylase (TP), dihydropyrimidine dehydrogenase (DPD), methylenetetrahydrofolate reductase (MTHFR), multidrug resistance-associated protein 1 (MRP1), and multidrug-resistance gene 1 (MDR1) were determined by quantitative real-time reverse transcriptase-polymerase chain reaction. There was a significant posttherapeutic reduction in the expression levels of TP (P = .028) and MRP1 (P = .006). Furthermore, down-regulation of MRP1 (P = .041) and TYMS (P = .028) after chemotherapy was associated with tumor response to chemotherapy, assessed clinically and by histopathologic tumor regression. Down-regulation of chemotherapy metabolism-associated genes occurs after neoadjuvant chemotherapy and may modulate tumor response to chemotherapy.
AU  - Langer, R.*
AU  - Specht, K.*
AU  - Becker, K.*
AU  - Ewald, P.*
AU  - Ott, K.*
AU  - Lordick, F.*
AU  - Siewert, J.R.*
AU  - Höfler, H.
C1  - 743
C2  - 24743
SP  - 191-197
TI  - Comparison of pretherapeutic and posttherapeutic expression levels of chemotherapy-associated genes in adenocarcinomas of the esophagus treated by 5-fluorouracil- and cisplatin-based neoadjuvant chemotherapy.
JO  - Am. J. Clin. Pathol.
VL  - 128
IS  - 2
PB  - American Society for Clinical Pathology
PY  - 2007
SN  - 0002-9173
ER  - 

TY  - JOUR
AB  - The human amyloidoses represent a heterogeneous group of disorders characterized by the deposition of fibrillar protein in vital organs. Given the fact that at least 20 different molecules can form fibrils, the unambiguous identification of the type of amyloid deposited is critical to the correct diagnosis and treatment of patients with these disorders. Heretofore, this information has been inferred from particular clinical features of the disease, ancillary laboratory tests, and results of immunohistochemical analyses. However, to establish unequivocally the kind of protein that is deposited as amyloid, it is necessary to determine its chemical composition through amino acid sequencing or mass spectroscopy of material extracted from fibrillar deposits. We have developed a micromethod whereby such studies can be performed readily using sections of formalin-fixed, paraffin-embedded biopsy specimens. The ability to identify precisely the nature of the tissue deposits has diagnostic, therapeutic, and prognostic implications for patients with amyloid-associated disorders.
AU  - Murphy, C.*
AU  - Eulitz, M.
AU  - Hrncic, R.*
AU  - Sletten, K.*
AU  - Westermark, P.*
AU  - Williams, T.*
AU  - Macy, S.D.*
AU  - Wooliver, C.*
AU  - Wall, J.*
AU  - Weiss, D.T.*
AU  - Solomon, A.*
C1  - 21828
C2  - 20044
SP  - 135-142
TI  - Chemical Typing of Amyloid Protein Contained in Formalin-Fixed Paraffin-Embedded Biopsy Specimens.
JO  - Am. J. Clin. Pathol.
VL  - 116
IS  - 1
PY  - 2001
SN  - 0002-9173
ER  -