BACKGROUND:Heat shock protein 27 (hsp27) is a molecular chaperone which supports cells to keep their homeostasis under stressful conditions. It is associated with resistance to chemotherapeutics, radiation and hyperthermia. The aim of this retrospective study was to investigate the prognostic value of hsp27 for patients with node-negative breast cancer.MATERIALS AND METHODS:Paraffin sections of 191 patients were stained immunohistochemically with a monoclonal antibody against hsp27. Median follow-up was 177 months. The results were correlated with clinical and histopathological parameters using the Chi-square test.RESULTS:There was no significant correlation between hsp27 expression and standard histopathological features or the proliferation marker ki-67. Disease-free survival (DFS) was not altered for patients expressing hsp27-positive tumors, whereas overall survival (OS) [p=0. 02] and survival after first recurrence (SR) [p=0.01] were significantly decreased.CONCLUSION:The expression of hsp27 in primary breast cancers is associated with a short survival for node-negative patients.

Background: Breast and ovarian tumor cell lines with defined tumor-associated antigens could serve as allogeneic antigen-sources for the biological therapy of cancer. Materials and Methods: Eight breast and 3 ovarian cancer cell lines were stained for the antigens in question by immunohistochemistry. Antigen-expression was graded in 5 steps by light microscopic examination. Results: All cell lines with the exception of PA-1 expressed EMA. Only MCF-7 was CEA-positive. MUC-1 was found in all cell lines apart from MDA-MB and SK-OV3. The highest expression of Her-2/neu was found in ZR-75/1 and SK-OV3. A491D and PA1 cells were CD19-negative, all other lines were positive. Only A491D and BT-20 had p53 accumulation. PR was found in 5 cell lines and ER in 6 cell lines. Conclusion: The cell lines investigated express a different pattern of tumor markers. In consequence, a careful examination should be performed in order to find the "best fitting" cell line to a patient's tumor for a tumor-vaccine.

Background: Heat-shock proteins (hsp) are involved in processes which are associated with tumour neogenesis and the biological behaviour of tumours. The object of our study was to investigate the significance of the 70 kDa lisp for the outcome of women with node-negative breast cancer. Patients and Methods: Paraffin sections of 191 patients with operated breast cancer and a median follow-up of 177 months were stained immunohistochemically with a commercially available antibody against hsp70. Results: We found a statistically significant correlation of the nuclear staining pattern with tumour size (> or less than or equal to 2 cm; p = 0.046) and with a low tumour grading (G1 and G2 versus G3; p = 0.029). Patients showing a cytoplasmatic staining for hsp70 had a statistical significantly decreased overall survival [OS] (p = 0.04) and a shorter survival after recurrence [SR] (p = 0. 026). Conclusion: The nuclear share of hsp70 is associated with various biological characteristics of malignant breast tumours, while the occurrence of cytoplasmatic hsp70 influences OS and SR.

Two sisters whose mother had pseudo-pseudohypoparathyroidism, simultaneously developed in infancy pseudohypoparathyroidism with severe liver damage leading to cirrhosis and characterised by "ectoplasmic vacuoles", as well as severe anaemia and thrombocytopenia. As any known metabolic or inflammatory liver disease could largely be excluded, a common genetic defect is assumed as the cause of the combined disorder in calcium and hepatic metabolism.

The course of illness of a male infant who lived for seven months with a diffuse, nesidioblastic hyperplasia of pancreatic islets is described. Before surgical intervention the diagnosis should be ascertained by 1. observation of acetonuria which is always absent after hypoglycemic episodes, 2, the typical constellation of insulin concentration, free fatty acid concentration and beta-hydroxybutyrat during a hypoglycemia (as found by Baker et al. 1976) and/or by simultaneous measuring of glucose-insulin levels under the conditions of fasting as well as of oral leucine, oral glucose and intravenous tolbutamide loading. Therapy with diazoxide should be tried in any case. If all conservative measure fail and relative or absolute hyperinsulinemia is proved, experience shows that an immediate operation is indicated.

Studies of the carbohydrate utilization in bacteria have indicated that the phosphorolysis of polymeric α-1,4-linked glucose to glucose-1-P by pyridoxal-5’-P-dependent phosphorylases is a universally occurring process (Palmer et al., 1973). While phosphorylases of higher organisms respond to energy needs by means of allosteric or covalent activation, in bacteria activation in response to a changing nutritional environment is mediated via phosphorylase induction. Nonregulatable phosphorylases might be interesting tools to study the role of pyridoxal-5’-P for the structure and function of these enzymes.

FEBS LettersVolume 55, Issue 1-2 p. 178-182 Full-length articleFree Access Hydrophobic and biospecific chromatography in the purification of maltodextrin phosphorylase from E. Coli F. Thanner, F. Thanner Physiologisch-Chemisches Institut der Universität Würzburg, D 8700 Würzburg, Germany Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, Israel Universitätskinderklinik D8700 Würzburg, Germany. Search for more papers by this authorD. Palm, D. Palm Physiologisch-Chemisches Institut der Universität Würzburg, D 8700 Würzburg, Germany Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, IsraelSearch for more papers by this authorS. Shaltiel, S. Shaltiel Physiologisch-Chemisches Institut der Universität Würzburg, D 8700 Würzburg, GermanySearch for more papers by this author F. Thanner, F. Thanner Physiologisch-Chemisches Institut der Universität Würzburg, D 8700 Würzburg, Germany Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, Israel Universitätskinderklinik D8700 Würzburg, Germany. Search for more papers by this authorD. Palm, D. Palm Physiologisch-Chemisches Institut der Universität Würzburg, D 8700 Würzburg, Germany Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, IsraelSearch for more papers by this authorS. Shaltiel, S. Shaltiel Physiologisch-Chemisches Institut der Universität Würzburg, D 8700 Würzburg, GermanySearch for more papers by this author First published: July 15, 1975 https://doi.org/10.1016/0014-5793(75)80987-2Citations: 17 AboutPDF 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 Volume55, Issue1-2July 15, 1975Pages 178-182 ReferencesRelatedInformation