The aetiology of oral premalignant lesions is generally accepted to be multifactorial. Tobacco and alcohol are established as important cofactors in malignant development in the oral cavity, but in addition microorganisms, such as human papillomavirus (HPV), have gained much interest over the past decade. For many years, HPV has been accepted as an important cofactor in the development of cervical cancer, originating from a mucous membrane with similarities to the oral mucosa. 49 patients with oral premalignant lesions and 20 control patients with normal oral mucosa and no history of HPV infection were examined for the presence of HPV by immune histochemical staining using the peroxidase anti-peroxidase technique (PAP), DNA-DNA in situ hybridisation (ISH), and polymerase chain reaction (PCR) analysed by Southern blot hybridisation with an HPV 16 specific probe. The investigations revealed that HPV was found in 62.5% of the verrucous leucoplakias, 50.0% of the erythroplakias, 45.5% of the homogeneous leucoplakias, 33.3% of erythroleucoplakias and in 12.5% of the nodular leucoplakias. An overall HPV detection rate in the examined premalignant lesions was 40.8% and no patients in the control sample were positive. Concerning oral cancer development, it seems likely that HPV may be a cofactor, as 100% of patients who developed oral cancers within 4–12 years were all positive for HPV, one being positive for HPV 16.

FEBS LettersVolume 367, Issue 1 p. 100-100 Book reviewFree Access Human papillomaviruses and cervical cancer. Biology and immunology Edited by P.L. Stern and M.A. Stanley, Oxford University Press, 1994. xiii + 226 pages. £ 60.00. ISBN 0-19854-796-X Bodil Norrild, Bodil NorrildSearch for more papers by this author Bodil Norrild, Bodil NorrildSearch for more papers by this author First published: June 19, 1995 https://doi.org/10.1016/0014-5793(95)90063-2AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat No abstract is available for this article. Volume367, Issue1June 19, 1995Pages 100-100 RelatedInformation

Herpes simplex virus type 1 (HSV-1) infection of human fibroblast cells grown in culture induces reorganization of the cytoskeleton fibrillar structures. Normal transport and insertion of HSV glycoproteins into the plasma membrane of the cells depend on the integrity of the microtubules. The natural host cells for HSV are epithelial cells, and an epithelial cell line established from rat palate was used in the present study. The effect of virus on the structure of the intermediate filaments and especially on the keratin proteins was studied. Two-dimensional gel electrophoresis of total cell extracts identified in uninfected cells two major acidic keratin proteins with apparent molecular weights of 44,000 (44K) and 48K (pI 5.45 to 5.30, 5.50 to 5.35). A new keratin protein of 46K (pI 5.40 to 5.25) appeared in infected cells between 8 h and 12 h post-infection. Pulse-chase experiments identified the 46K protein as a processed form of the 48K keratin component, which was also cleaved in uninfected cells grown in the presence of cycloheximide. Partial proteolysis of the 46K and 48K keratins with Staphylococcus aureus V8 protease showed that the 48K and the 46K proteins differed in only one oligopeptide. The significance of the changed keratin composition of HSV-infected cells is discussed.

In this preliminary study the distribution of blood group A- and H-antigens and their structural precursor N-acetyllactosamine in normal, pre-malignant and malignant squamous epithelium were investigated using the immunofluorescence technique. In normal cervical epithelium the basal cells and few parabasal cells expressed N-acetyllactosamine. The parabasal and lower spinous cells expressed the H-antigen and the upper spinous layer expressed the A-antigen. All pre-malignant and malignant lesions showed irregular decrease in contents of A- and H-antigens. N-acetyllactosamine was either completely lost or found to accumulate in these lesions, and it is suggested that this antigen could be a valuable tool in the diagnosis of cervical cancer.

Keratin proteins in human cervical squamous epithelium were investigated by the immunofluorescence technique, using the monoclonal keratin antibodies AE1 and AE2. Although the exocervic is covered by a non-keratinizing, histologically homogenous, squamous epithelium, different staining patterns were found within a single histological section. This indicates a regional variation in the maturation pattern of stratified exocervical epithelium. Detection of morphological versus biochemical keratinization in the diagnosis of pathological cervical conditions is discussed.

Scandinavian Journal of ImmunologyVolume 17, Issue s10 p. 279-282 Radioimmunoelectrophoresis for Determination of Molecular Size of Polypeptides B. NORRILD, B. NORRILD Institute of Medical Microbiology, University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this author B. NORRILD, B. NORRILD Institute of Medical Microbiology, University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this author First published: December 1983 https://doi.org/10.1111/j.1365-3083.1983.tb04030.xCitations: 2AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume17, Issues10December 1983Pages 279-282 RelatedInformation

Scandinavian Journal of ImmunologyVolume 15, Issue s9 p. 223-240 Synaptic Membrane Proteins in Mammalian Brain E. BOCK, E. BOCK The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this authorI. DIVAC, I. DIVAC The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this authorB. NORRILD, B. NORRILD The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this authorN. A. THORN, N. A. THORN The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this authorC. TORP-PEDERSEN, C. TORP-PEDERSEN The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this authorM. TREIMAN, M. TREIMAN The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this author E. BOCK, E. BOCK The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this authorI. DIVAC, I. DIVAC The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this authorB. NORRILD, B. NORRILD The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this authorN. A. THORN, N. A. THORN The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this authorC. TORP-PEDERSEN, C. TORP-PEDERSEN The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this authorM. TREIMAN, M. TREIMAN The Protein Laboratory; Institute of Neurophysiology, Panum Institute; Institute of Medical Microbiology; and Department of Physiology C, Panum Institute; University of Copenhagen, Copenhagen, DenmarkSearch for more papers by this author First published: November 1982 https://doi.org/10.1111/j.1365-3083.1982.tb03766.xCitations: 5AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Citing Literature Volume15, Issues9November 1982Pages 223-240 RelatedInformation

Tissue culture cells infected with herpes simplex type 1 virus express virus-specified glycoprotein antigens on the plasma membrane. Three of these have been previously identified and have been designated as Ag-11, Ag-8, and Ag-6. In the present study, immunoglobulins to each of the antigens were shown to be capable of mediating immunocytolysis in the presence of either complement (antibody-dependent complement-mediated cytotoxicity) or peripheral blood mononuclear cells (antibody-dependent cell-mediated cytotoxicity [ADCC]). Two herpes simplex virus type 1 strains, VR-3 and F, reacted similarly in the ADCC test in the presence of immunoglobulins to Ag-11, Ag-8, and Ag-6 in both infected Chang liver cells and HEp-2 cells. Anti-Ag-6, however, produced a lower ADCC reaction in HEp-2 cells than in Chang liver cells, suggesting differences in the Ag-6 surface expression in, or release from, these cells. Chang liver and HEp-2 cells infected with the MP mutant strain of herpes simplex virus type 1 showed reduced ADCC in the presence of anti-Ag-11 and anti-Ag-8, but no reactivity at all with anti-Ag-6. Crossed immunoelectrophoretic analysis showed that MP-infected cell extracts contain Ag-11 and Ag-8, but lack Ag-6. Polypeptide analysis of herpes simplex virus type 1 strains F, VR-3, and MP showed that Ag-11 consists of the glycoproteins gA and gB, that Ag-8 consists of gD, and that Ag-6 consists of gC. In conclusion, the present study demonstrates that either one of the glycoproteins (gC, gD, and a mixture of gA and gB) can function as a target for immunocytolysis and that the antibody preparation to gC (Ag-6) does not cross-react with any of the other glycoproteins.