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Biomedical subjects

P J Klein

Publications and source records attributed to P J Klein.

At least 37 records · Page 2Linked to original sources
PubMed1986

Epithelioid hemangioendothelioma. Report of a case with immuno-lectinhistochemical and ultrastructural demonstration of its vascular nature.

The epithelioid hemangioendothelioma (EHE) is a rare vascular tumour of borderline malignancy, first described as a separate entity in 1982 by Weiss and Enzinger. The abundant cytoplasm of endothelial cells mimiking epithelioid appearances, prominent cytoplasmic vacuolization and barely perceptible lumina even in reticulin stains may result in EHE being mistaken for a signet ring cell carcinoma. In our case, difficulties in differential diagnosis were enhanced by the location of the tumour within an inguinal lymph node. The usefulness of FVIIIR: Ag- and UEA I- histochemistry in ascertaining the endothelial nature of this tumour is demonstrated, in correlation with electron microscopic data. The different reaction sites of these markers are striking and typical: FVIIIR: Ag displays a granular or diffuse cytoplasmic reaction, whereas UEA I provides a linear staining of vacuoles and luminal surfaces.

Adenocarcinoma, Mucinous↗
PubMed1986

Comparative histological, histochemical, immunohistochemical and biochemical studies on oestrogen receptors, lectin receptors, and Barr bodies in human breast cancer.

The present study performed on a total of 567 cases of human female breast cancer compares the results of the biochemical assay (dextran-coated charcoal assay = DCC) for oestrogen receptor (ER) with those of several morphological methods developed for the detection of the ER or for the prediction of prognosis by use of other systems (FSA = fluorescent ligand binding assay, ER-ICA = monoclonal antibody assay for ER, LRA = lectin receptor assay using peanut agglutinin, and Barr body estimation). Whereas no correlation at all was observed among the results of the DCC and those of the FSA and Barr body estimation, the ER-ICA and the LRA showed an unanimous tendency towards higher values of ER with increasing intensity of the staining product. The results of the ER-ICA may be expressed by an immuno-reactive score (IRS) calculated from the staining intensity (SI) and the percentage of positive cells (PP). The morphological methods are evaluated with special regard to their correlation with the DCC, their theoretical basis, and their practical application. In summary, the ER-ICA appears to be the sole method directly visualizing the ER protein and--in contrast to the DCC--is therefore completely independent of the content of endogenous or exogenous oestrogens in the tumor tissue. The LRA provides valuable additional information concerning tumour differentiation and possible response to endocrine therapy, whereas the FSA and Barr body estimation should be considered as obsolete and should therefore be abandoned.

Antibodies, Monoclonal↗
PubMed1984

Isolation and chemical and immunochemical characterization of the peanut-lectin-binding glycoprotein from human milk-fat-globule membranes.

Membrane glycoprotein with high Mr (HMr-MGP) was purified from neuraminidase-treated Triton X-100-solubilized human milk-fat-globule membranes by peanut-agglutinin (PNA) affinity chromatography. The high carbohydrate content (75%), blood-group-A activity and typical monosaccharide composition (L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosamine in the proportions 0.26:1.00:1.85:1.30) indicate that the isolated HMr-MGP is a mucinous substance. Fractionation of the oligosaccharides from alkaline-borohydride-treated HMr-MGP on Bio-Gel P-2 suggest that the PNA-binding sites are located mainly on longer (tetra- to deca-saccharide) alkali-labile bound oligosaccharide chains. Polyclonal antibodies raised against the HMr-MGP showed an antigenic distribution in histological sections that was comparable with the distribution of peroxidase-labelled-PNA-binding sites in both normal and malignant breast tissues. The positive immunohistological staining of some other tissue components with this antibody indicates that HMr-MGP is not strictly breast-associated. The functional role of HMr-MGP is unknown, but, since its expression is dependent on the differentiation state of secretory epithelial cells, it serves as a differentiation antigen that can be used for better functional characterization of breast cancers.

Adenocarcinoma↗
PubMed1984

Energy metabolism and histomorphological findings in replanted rat hind limbs using various conservation methods.

Using various storage and conservation methods, we examined amputated and subsequently replanted limbs for their ischaemia tolerance level by investigating the changes in the adenylphosphocreatine system and glycolysis cycle. After replantation, amputated limbs that had been stored at room temperature (21.0 +/- 1.5 degrees C) for 2 hours were examined 14 days after operation. The adenosine triphosphate level of the skeletal muscle was reduced to 51% and the creatine phosphate to 77% of that of the control group. The glycogen was 13% of the normal value. The biochemical findings correlate with the histomorphological findings. After 2 hours ischaemia, the cross striations of the skeletal muscle and nuclear staining remained intact. There is a breakdown of the biochemical systems after 4 hours of ischaemia. They are no longer intact and the ischaemic limb does not recover. Histologically, muscle necrosis can be observed.

Adenosine Triphosphate↗
PubMed1984

Characterization of glycoconjugates of human gastrointestinal mucosa by lectins. I. Histochemical distribution of lectin binding sites in normal alimentary tract as well as in benign and malignant gastric neoplasms.

Labeled lectins with binding specificity to the hexose components of mucus glycoproteins (HPA, RCA I, PNA, Con A, WGA, and UEA I) were used to demonstrate structural differences in the glycoprotein composition of various cell types of the normal, benign and malignant gastrointestinal mucosa. While in the RCA I, UEA I, and WGA binding of normal mucus secreting cell types only quantitative differences were observed, the mucus in the surface epithelial cells of gastric mucosa and in the colonic goblet cells was characterized by the absence of PNA, Con A, and PNA, HPA binding sites, respectively. These lectins, however, showed a strong binding to the supranuclear, Golgi-region in the undifferentiated or activated forms of these cells. Even the staining intensity of the luminal membrane surfaces of the non mucinous parietal and chief cells was often stronger by PNA, HPA, and RCA I lectins than that of the mucus secretions in the highly differentiated mucus cells. These results indicate the existence of either heterogeneous glycoprotein components or mucus molecules with variations in the degree of glycosylation of their oligosaccharide chains in the different cells. The latter seems more likely since in benign and malignant alterations lectin binding sites appear in great density, which were found to be characteristic of the undifferentiated mucus cells or for the non mucinous cells of the normal gastric mucosa. Similarly in some gastric cancers which do not stain with the periodic acid-Schiff reaction at all, large amount of free or neuraminic acid substituted PNA binding sites can be detected.

Adenocarcinoma↗
PubMed1984

Characterization of glycoconjugates of human gastrointestinal mucosa by lectins. II. Lectin binding to the isolated glycoproteins of normal and malignant gastric mucosa.

Using affinity chromatography on HPA-, PNA-, Con A, and WGA-agarose columns only a part (10-30%) of the high molecular weight mucous glycoproteins could be isolated from the Triton X-100 solubilized components of normal as well as carcinomatous gastric mucosa. The main part of the mucus was not bound by the lectins, which corresponds to our earlier lectin histochemical observations on paraffin-embedded tissue sections. The lectin-bound mucous glycoproteins had a relatively lower molecular weight, ranging from about 250-1,000 kilodaltons, as indicated by polyacrylamide gradient gel electrophoresis and by gel filtration on Biogel A 1.5 m column. In gas chromatographic analysis the molar ratio of aminohexoses to galactose was found to be much higher (3:1) in the lectin-bound mucous substances than in the whole high molecular weight mucus (1:1). This finding indicates that lectins have a higher affinity to the hexosamine rich components of mucus, which may be special forms of mucous glycoprotein molecules or the incompletely glycosylated core and backbone regions of the oligosaccharide chains of mucus. Extremely high hexosamine values (10:1) were found in the PNA isolated mucus of gastric adenocarcinoma. Since it is known that PNA binds to the terminal disaccharide, beta-galactose-(1-3)-N-acetylgalactosamine, which is localized at the reducing end of the oligosaccharide chains of mucus, it is highly probable that the elongation of the oligosaccharide side chains is disturbed in gastric cancer cells.

Binding Sites↗
PubMed1983

The significance of lectin receptors for the evaluation of hormone dependence in breast cancer.

Benign and malignant breast diseases were histochemically investigated with regard to their secretory function. Thereby, the labelled lectin from peanut (peanut agglutinin = PNA) which possesses a high affinity for D-galactosyl-(1-3)-N-acetyl-D-galactosamine, showed a binding pattern partly indicating disturbed secretory cell mechanisms. Further studies with a labelled antibody directed against a milk fat globule membrane glycoprotein, which was isolated by PNA affinity chromatography from human milk, confirmed the PNA receptor as a marker of a milk protein in breast carcinomas. Additionally, two other monoclonal antibodies which were raised against other components of the milk fat globule membrane were used for a more detailed characterization of the functional situation of mammary carcinomas. These immuno- and lectin-histochemical investigations revealed that tumors with a high secretory activity responded in about 80% to endocrine treatment, whereas breast carcinomas that exhibited no secretory function failed to respond to endocrine therapy. Thereby, the hormone dependence of tumor tissue showed an inverse correlation with the proliferative activity, as determined by the mitosis index.

Arachis↗
PubMed1983

Histochemical tumor markers for evaluation of hormone dependence in breast cancer.

Lectin from the peanut (peanut agglutinin = PNA) possesses a high affinity for D-galactosyl-(1-3)-N-acetyl-D-galactosamine, used for histochemical investigations on formalin-fixed tissue sections of normal mammary gland as well as of benign and malignant breast diseases. Thereby, a lectin-binding pattern was found that partly exhibited secretory malfunction. Additional studies with a labeled antibody directed against a milk fat globule membrane glycoprotein, which was isolated by PNA affinity chromatography from human milk, confirmed the PNA receptor as a marker of a milk protein in breast carcinomas. The most important clinicopathological finding, however, was that in accordance with the secretory activity about 77% of PNA-positive tumors responded to endocrine treatment, whereas PNA-negative mammary carcinomas usually failed to show any response to hormonal therapy. These results also correlated with the hormone receptor content of tumor tissue.

Breast Neoplasms↗
PubMed1983

Peanut agglutinin (PNA) binding sites: a useful marker for hormonal dependence in experimental breast cancer.

Histochemical studies were performed with the labeled lectin from Arachis hypogaea (peanut agglutinin, PNA) to detect the occurrence, distribution, and amount of this lectin receptor in N-nitrosomethylurea-induced rat mammary carcinomas. Since in normal rat mammary tissue, the formation and secretion of PNA binding sites are controlled by the combined action of estrogen and prolactin, the amount of secretion-associated PNA binding sites was correlated with tumor response to either ovariectomy or antiestrogenic treatment with tamoxifen. Free as well as sialic acid-substituted PNA binding sites which were represented by the disaccharide beta-D-Gal(1-3)NAcGal occurred in the apical cytoplasm of tumor cells and within the secretions of acinar and tubular structures. In contrast the whole tumor cell membrane contained predominantly sialic acid-substituted PNA binding sites. All of the tumors investigated contained some secretion-associated PNA binding sites. The values showed a continuum from very low to very high amounts. The number of PNA binding sites associated with secretory activity was lower in hormone-independent than in hormone-dependent tumors. Furthermore, there was an inverse relationship between mitotic and secretory activities with positive PNA staining. In conclusion, these studies revealed that the secretory PNA index, mitotic index, and especially the ratio of secretory PNA index to mitotic index represent useful parameters to select tumors for endocrine therapy in this experimental model.

Animals↗
PubMed1983

Histochemical demonstration of neuraminidase effects in pneumococcal meningitis.

In three cases of pneumococcal meningitis the in vivo action of pneumococcal neuraminidase could be demonstrated. The removal of sialic acid was demonstrated in necrospy material by the use of labeled peanut agglutinin, which has a high specific affinity for the subterminal disaccharide beta-D-galactopyranosyl-(1-3)N-acetyl-D-galactosamine, thereby exposed. Furthermore, this lectin was used for a rapid in vitro histochemical assay of neuraminidase activity in cerebrospinal fluid and culture medium taken from these cases. From the clinical point of view the exposure of the disaccharide which represents the immunodominant group of the Thomsen-Friedenreich antigen may induce immunologic reactions, because all human sera contain antibodies to this cryptic antigen. Thereby, neuraminidase can contribute to the poor prognosis of pneumococcal meningitis.

Choroid Plexus↗
PubMed1983

Lectin binding properties of glycoproteins in cells of normal gastric mucosa and gastric cancers: a comparative histochemical and biochemical study.

The different binding of labeled lectins to the individual cell types of the normal mucosa indicates differences in glycoprotein composition of the: a) surface epithelial cells showing various degrees of differentiation; b) cell types lying above and below the generative cell zone; c) specific membrane systems of the parietal and chief cells. The enhanced peanut agglutinin (PNA) binding of activated, hyperplastic isthmus cells, of goblet cells in intestinal metaplasia, and even of the majority of gastric cancer cells may be indicative for their common origin and for their similar functional states in glycoprotein synthesis. Lectins demonstrate differences also in the mucus structure of the main types of gastric cancers. Adenocarcinomas show similar lectin binding patterns to activated isthmus cells, but the subtypes of signet ring cells resemble mucus neck cells or intestinal and colonic goblet cells, respectively. Glycoproteins which can be isolated by the lectins in a pure form allow further detailed studies in these fields.

Binding Sites↗
PubMed1982

Histochemical distribution of certain biochemical constituents in the albumin glands of snails.

The presence in situ of the biochemical constituents galactans, proteinase-inhibitors, and erythro-agglutinin anti-A in snail's albumin gland tissues has been demonstrated by histochemical techniques using fluorescein isothiocyanate (FITC)-conjugated counterparts; namely, anti-galactan-specific lectins, different proteinases, and blood group A substance. Invariably, these constituents are localized as globular structures, predominantly within the lobules of the gland tissue. There is a good correlation between the histochemical findings and the previously reported biochemical and serological findings for these substances.

Albumins↗