Cancer Research PRL Inhibitor Induces the Cleavage of p130Cas  Protein Translation and Cancer
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[Cancer Research 50, 438-443, January 15, 1990]
© 1990 American Association for Cancer Research

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Presence of Villin, a Tissue-specific Cytoskeletal Protein, in Sera of Patients and an Initial Clinical Evaluation of Its Value for the Diagnosis and Follow-up of Colorectal Cancers1

B. Dudouet, L. Jacob, P. Beuzeboc, H. Magdelenat, S. Robine, Y. Chapuis, B. Christoforov, G. A. Cremer, P. Pouillard, P. Bonnichon, F. Pinon, R. J. Salmon, A. Pointereau-Bellanger, J. Bellanger, M. T. Maunoury and D. Louvard2

Département de Médecine interne [L. J., B. C., G. A. C.], Clinique Chirurgicale [Y. C., P. Bo.], and Poste de Transfusion sanguine [F. P.], Hôpital Cochin, 27, rue du Faubourg Saint Jacques, 75674 Paris Cedex 14 Département de Médecine oncologique [P. Be., P. P.], Laboratoire de radiopathologie [H. M.], and Service de Chirurgie [R. J. S.], Institut Curie, 26 rue d'Ulm, 75005 Paris Service de Gastroentérologie, Pr. Y. Le Quintrec, Hôpital Rothschild, 75012 Paris [J. B.] Pharmacie Hôpital Salpétrière, 83 bd de l'Hôpital, 75013 Paris [A. P. B.] Institut Gustave Roussy, 39 rue Camille Desmoulins, 94805 Villejuif Cedex [M. T. M.]; and Unité de Biologie des Membranes, Département de Biologie Moléculaire, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15 [B. D., S. R., D. L.], France

Villin is an actin-binding protein found in a few normal adult epithelia, namely epithelial cells in the digestive and urogenital tracts. Moreover, villin production is maintained in malignant cells. We assumed that cell lysis and necrosis of solid tumors producing villin might result in villin release into blood. We analyzed the villin content of sera from 788 patients and controls using an enzyme-linked immunosorbent assay. Patients and controls were classified into healthy donors, patients with benign diseases of the gastrointestinal tract, patients with colorectal cancers, and patients with malignant nondigestive diseases. In the panel of sera analyzed, the sensitivity of the assay for colorectal cancers was 50.5%, and its overall specificity for malignant digestive tumors was 94.5%. Results were statistically analyzed comparing each group of sera with each other. We conclude that the presence of villin is indicative of a pathological state in the gastrointestinal tract (P < 0.001). Finally, we followed villin levels after tumor resections (60 patients). We found that the villin level in sera remains low in remissions but is raised in recurrences.

We suggest that the villin assay may have clinical utility as a diagnostic adjunct for adenocarcinoma of the gastrointestinal tract. It may also have some value in monitoring patients with advancing colorectal carcinomas after resection of these tumors.

1 This work was supported by grants from the Institut National de la Santé et de la Recherche Médicale (No. 86-7008), by the Fondation pour la Recherche Médicale Française, by the Association pour la Recherche sur le Cancer (No. 6379), the CNRS (UA-1149), and the Ligue Nationale Française contre le Cancer.

2 To whom requests for reprints should be addressed.

Received 2/27/89. Revised 7/13/89. Accepted 9/25/89.




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HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cancer Prevention Research
Cancer Prevention Journals Portal Cancer Reviews Online
Annual Meeting Education Book Meeting Abstracts Online
Copyright © 1990 by the American Association for Cancer Research.