Peanut Agglutinin Binding Sites Research Articles

Specific lectin binding sites during in vitro capacitation and acrosome reaction in boar spermatozoa

Sperm glycocalyx and plasma membrane undergo outstanding modifications during fertilization. However, it is unclear how in vitro capacitation time and acrosome reaction affect the specific location of boar sperm glycoconjugates. This study aimed to identify lectin binding patterns and to describe the sequential changes during different in vitro capacitation times (1 and 4 h) and acrosome reaction in boar spermatozoa. With Aleuria aurantia agglutinin (AAA), most uncapacitated cells were labelled in the postacrosomal region. Nevertheless, after 1 h of in vitro capacitation and the acrosome reaction, most AAA binding sites were in the acrosomal region. With Concanavalin A (ConA), most sperm were labeled in the postacrosomal region before and after capacitation. After the acrosome reaction induction, this pattern changed to a highly stained acrosomal and postacrosomal regions. Peanut agglutinin (PNA) binding sites were in the acrosomal region in uncapacitated and capacitated sperm. In acrosome reacted sperm after 4h capacitation, the most frequent pattern showed remaining positive labeling in the central area of the head. With Pisum sativum agglutinin (PSA), most uncapacitated cells showed a postacrosomal region staining. Nevertheless, faint stained all over the head and highly acrosomal region labelling was observed in the major part of capacitated and acrosome reacted sperm respectively. With Wheat germ agglutinin (WGA), the most representative pattern in uncapacitated, capacitated and acrosome reacted sperm was labelled in the acrosomal region. Regarding capacitation time, the most significant changes in the most representative pattern were observed in acrosome reacted spermatozoa after 4 h of in vitro capacitation. Highlights Lectins allow detailed descriptions of eight different populations in boar sperm. Changes in lectin binding patterns during capacitation are time dependent. Lectin binding patterns significantly change after 4 h of in vitro capacitation.

The effects of estrogen deficiency on glycosylation of odontoblasts in rats

To investigate the effects of estrogen deficiency on odontoblast metabolism, we induced osteoporosis in rats by ovariectomy and examined the glycosylation of the matrix component in odontoblasts. Peanut agglutinin (PNA) lectin histochemistry, which detects D-galactose and N-acetylgalactosamine sugars, was conducted in incisor odontoblasts of ovariectomized (OVX) and sham-operated (sham) rats. At 5 wk after the operation, bone mineral density and serum level of estrogen in OVX rats were lower than those in sham rats. PNA binding sites were found in the odontoblasts in incisors, and the binding sites in OVX rats were much stronger than those in sham rats. Furthermore, PNA binding sites were localized at the predentin matrix in OVX rats, but the reaction in sham rats was not detected. Because D-galactose and N-acetylgalactosamine sugars bound to PNA are important constituents of proteoglycans in dentin matrix and the PNA binding sites reflect the proteoglycan production of odontoblasts, these results indicated that galactosyl glycosylation of proteoglycans in odontoblasts is influenced by estrogen deficiency in rat incisors.

Regulated expression of keratan sulphate and peanut agglutinin binding sites during organogenesis in the developing chick.

Keratan sulphate proteoglycans are potentially important during development and are possible binding molecules for the lectin, peanut agglutinin, a marker for areas that are inhibitory for axonal growth in early embryos. The present study describes the spatiotemporal distributions of keratan sulphate epitopes and peanut agglutinin binding sites during organogenesis in the developing chick from E5 to hatching. The widespread distributions of these molecules did not often overlap but clearly delimited different carbohydrate compartments demonstrating that peanut agglutinin does not necessarily bind to keratan sulphate proteoglycans. These markers were mostly extracellular but keratan sulphate, in particular, was found within certain specific cells in cartilage, gonad, heart and pancreas, at certain ages. The presence of keratan sulphate in putative germ cells during their migrations and in the gonads may be of particular importance. Their distributions generally evoke modulation of adhesion allowing cell migrations or morphogenetic movements related to epitheliomesenchymal interactions, but may also suggest an involvement in axonal guidance in skin, cartilage, gut and possibly heart. Furthermore, in the kidney, peanut agglutinin binding sites seem to be related to the functional differentiation of the nephrons.

Keratan sulphate is present in developing chick skin in vivo where it could constitute a barrier to advancing neurites as observed in vitro

Proteoglycans play an important role in axonal guidance. The glycosaminoglycan chondroitin sulphate is known to be inhibitory. Keratan sulphate is structurally similar and may play a similar role. The lectin peanut agglutinin potentially labels chondroitin or keratan sulphate rich areas. In order to elucidate the mechanisms by which the regular nerve pattern develops in chick skin, keratan sulphate epitopes and peanut agglutinin binding sites were localized in chick embryos and compared to previous studies of chondroitin sulphate. The markers all display specific, developmentally regulated staining patterns, thus reflecting their individuality. Their maximal expression coincides with the formation of feathers and their nerve pattern in both time and space. Furthermore, culture experiments using dorsal root ganglia demonstrate the avoidance of keratan sulphate by the growing sensory neurites, although outgrowth and elongation occur if they grow directly on the keratan sulphate substrate. Thus, keratan sulphate proteoglycans in developing chick skin are potentially involved in guidance of sensory neurites or maintenance of the new nerve pattern, but are clearly different to the chondroitin sulphate proteoglycans which have a complementary distribution. Furthermore, peanut agglutinin binding sites are independent of both proteoglycans.

Keratan sulphate is present in developing chick skin in vivo where it could constitute a barrier to advancing neurites as observed in vitro

Proteoglycans play an important role in axonal guidance. The glycosaminoglycan chondroitin sulphate is known to be inhibitory. Keratan sulphate is structurally similar and may play a similar role. The lectin peanut agglutinin potentially labels chondroitin or keratan sulphate rich areas. In order to elucidate the mechanisms by which the regular nerve pattern develops in chick skin, keratan sulphate epitopes and peanut agglutinin binding sites were localized in chick embryos and compared to previous studies of chondroitin sulphate. The markers all display specific, develop-mentally regulated staining patterns, thus reflecting their individuality. Their maximal expression coincides with the formation of feathers and their nerve pattern in both time and space. Furthermore, culture experiments using dorsal root ganglia demonstrate the avoidance of keratan sulphate by the growing sensory neurites, although outgrowth and elongation occur if they grow directly on the keratan sulphate substrate. Thus, keratan sulphate proteoglycans in developing chick skin are potentially involved in guidance of sensory neurites or maintenance of the new nerve pattern, but are clearly different to the chondroitin sulphate proteoglycans which have a complementary distribution. Furthermore, peanut agglutinin binding sites are independent of both proteoglycans. J. Neurosci. Res. 48:133–145, 1997. © 1997 Wiley-Liss, Inc.

Developmentally regulated expression of peanut agglutinin (PNA)-specific glycans on murine thymocytes.

Intrathymic maturation of T lymphocytes is characterized by variable expression of O-linked Gal beta 1,3GalNAc glycans reactive with peanut agglutinin (PNA) lectin. Recent studies on human thymocytes show that conversion from PNA+ to PNA- phenotype is correlated with increased expression of alpha 2,3 O-linked sialyltransferase (ST), which sialylates Gal beta 1,3GalNAc glycans, masking their binding sites for PNA. Interestingly, alpha 2,3 O-linked ST expression is highest within the regions of the thymus containing the most immature and most mature thymocyte subsets, suggesting that PNA-specific glycans are intermittently masked by sialylation during thymic selection processes. Here, we studied expression of PNA receptors on developing thymocytes in the murine system using thymocytes from both normal mice and transgenic mice that are genetically arrested at the early phases of T cell development. Our results confirm and extend recent findings in the human system by showing that murine T cells sequentially progress from PNAlo-->PNAhi-->PNAlo stages during their differentiation within the thymus. In addition, our data demonstrate that a similar set of polypeptides is variably masked by sialylation throughout T cell development.

Expression of extracellular matrix molecules and cell surface molecules in the olfactory nerve pathway during early development.

The spatial and temporal expression patterns of several extracellular matrix molecules--laminin and fibronectin and cell surface molecules, neural cell adhesion molecule (NCAM), L1, tenascin, chondroitin sulfate proteoglycan, and peanut agglutinin (PNA) binding sites--were investigated during early olfactory nerve development. NCAM and L1 have similar patterns: They are expressed in the olfactory nerve and on the olfactory receptor neurons (ORNs) commencing with the earliest olfactory axon outgrowth (E12-E15). Their expression patterns suggest that both NCAM and L1 are associated with extension and fasciculation of olfactory axons. A comparison of L1 and olfactory marker protein suggests that L1 is expressed predominantly on immature ORNs. Laminin has an unique punctate staining pattern in the developing olfactory pathway as early as E12. These laminin puncta might play a role in olfactory neurite outgrowth and guidance. At E14, when pioneer olfactory axons enter the brain, the laminin-positive meninges on the surface of the olfactory bulb primordium break down but remain intact in the rest of the telencephalon. This suggests a functional interaction between the olfactory axons and the glial-pial barrier. Fibronectin staining is diffuse throughout the cranial mesenchyme but is absent from the olfactory nerve pathway. No specific patterns of tenascin or chondroitin sulfate, were observed during early olfactory development. PNA binding sites were associated with olfactory axon fasciculation. The expression of several extracellular matrix molecules and cell surface molecules is spatially and temporally regulated in the developing olfactory system. These molecules, thus, may play functional roles in olfactory axon outgrowth, fasciculation, and/or guidance.

Expression of extracellular matrix molecules and cell surface molecules in the olfactory nerve pathway during early development

The spatial and temporal expression patterns of several extracellular matrix molecules—laminin and fibronectin and cell surface molecules, neural cell adhesion molecule (NCAM), L1, tenascin, chondroitin sulfate proteoglycan, and peanut agglutinin (PNA) binding sites—were investigated during early olfactory nerve development. NCAM and L1 have similar patterns: They are expressed in the olfactory nerve and on the olfactory receptor neurons (ORNs) commencing with the earliest olfactory axon outgrowth (E12-E15). Their expression patterns suggest that both NCAM and L1 are associated with extension and fasciculation of olfactory axons. A comparison of L1 and olfactory marker protein suggests that L1 is expressed predominantly on immature ORNs. Laminin has an unique punctate staining pattern in the developing olfactory pathway as early as E12. These laminin puncta might play a role in olfactory neurite outgrowth and guidance. At E14, when pioneer olfactory axons enter the brain, the laminin-positive meninges on the surface of the olfactory bulb primordium break down but remain intact in the rest of the telencephalon. This suggests a functional interaction between the olfactory axons and the glial-pial barrier. Fibronectin staining is diffuse throughout the cranial mesenchyme but is absent from the olfactory nerve pathway. No specific patterns of tenascin or chondroitin sulfate, were observed during early olfactory development. PNA binding sites were associated with olfactory axon fasciculation. The expression of several extracellular matrix molecules and cell surface molecules is spatially and temporally regulated in the developing olfactory system. These molecules, thus, may play functional roles in olfactory axon outgrowth, fasciculation, and/or guidance. ©1996 Wiley-Liss, Inc.

Lectin binding distinguishes between neuroendocrine and neuronal derivatives of the sympathoadrenal neural crest.

Lectin cytochemistry was used to identify surface epitopes selectively expressed by chromaffin cell chemoreceptors (glomus cells) in the rat carotid body. Unexpectedly, these studies revealed that binding sites for peanut agglutinin (PNA; Arachis hypogea) were highly expressed by all neuroendocrine-derivatives of the sympathoadrenal neural crest, including glomus cells, small, intensely fluorescent cells, and adrenal chromaffin cells in situ. In contrast, principal sympathetic neurons did not express PNA receptors. PNA binding was inhibited by 2% galactose. To determine whether expression of PNA receptors was selectively induced by neuroendocrine differentiation of sympathoadrenal precursors, we compared PNA labeling of embryonic sympathoblasts in the presence of either nerve growth factor (NGF) or the synthetic glucocorticoid dexamethasone (DEX). DEX-treated cells, which expressed several neuroendocrine traits, bound PNA, whereas NGF-treated neuronal derivatives did not. In addition, to examine whether expression of existing PNA receptors was down-regulated by neuronal differentiation of chromaffin cells, we compared labeling of PC12 cells, which normally bind PNA, in the presence and absence of NGF. Although PC12 cells acquired characteristic neuronal morphologies in the presence of NGF, they did not lose PNA labeling, even after 8 days of NGF treatment. These findings indicate that neuronal and neuroendocrine derivatives of the sympathoadrenal lineage can be distinguished by differential expression of carbohydrate epitopes and suggest that PNA receptors are induced by neuroendocrine differentiation.

Cell differentiation of alveolar epithelium in the developing rat lung: ultrahistochemical studies of glycoconjugates on the epithelial cell surface.

Glycoconjugates on the surface of pulmonary epithelial cells were ultrahistochemically examined in the fetal, neonatal and adult rat lung. Lectin and colloidal iron staining procedures were performed in combination with digestion using carbohydrate-degrading enzymes or methylation. The glycoconjugate composition of columnar cells at 16 days gestation was similar to that of cuboidal cells at 19 days gestation. Glycoconjugate differentiation on the cell surface occurred at 20 days gestation, and especially the loss of soybean agglutinin (SBA) binding sites could be detected on type II cells. The contents of Ricinus communis agglutinin-I (RCA-I) and Concanavalin A (Con A) binding sites on type II cells also began to decrease. On the contrary, the content of sulfated saccharides decreased on the surface of type I cells during development. Glycoconjugate differentiation on both type I and II cells was completed with the disappearance of hyaluronic acid and peanut agglutinin (PNA) binding sites; type I and II cells acquired a similar histochemical composition to that on adult type I and II cells at 5 days after birth. Both type I and II cells share a common early precursor cell, that is, the cuboidal epithelial cell at the canalicular stage.

Peanut Agglutinin Lectin Immunohistochemical Staining of Normal and Neoplastic Canine Tissues

Peanut lectin binding sites were demonstrated in normal canine tissues and in 114 canine tumors by avidin biotin complex immunohistochemical staining on unfixed cryostat tissue sections. Peanut agglutinin (PNA) receptors occurred in a variety of normal cells and tissues, including lymphoid follicle center cells; cortical thymocytes; basal cells and the stratum spinosum of stratified squamous epithelium; columnar epithelium of the gastrointestinal tract; parietal cells and chief cells of the stomach; some endothelial cells; myelin; chondrocytes; spermatogenic cells; cells of the adrenal medulla; Bowman's capsule and the distal convoluted tubules of the kidney; prostatic, perianal and endometrial epithelium; and the extracellular matrix of connective tissues. Neoplastic cell staining was sporadic and was most often observed in benign or well-differentiated neoplastic tissues in which the corresponding normal cells also expressed PNA binding sites. However, PNA also bound to some tumor cells in which the analogous normal tissues were unstained, including cells of some fibrosarcomas, rhabdomyosarcomas, hemangiopericytomas and proliferating myoepithelial cells in mixed mammary tumors. Although PNA binding is complex and heterogeneous in canine tissues and does not appear to immunohistochemically detect a moiety associated with neoplastic transformation per se in the majority of canine tumors, the expression of PNA receptors may be associated with neoplastic changes in some mesenchymal cell populations.

Regulation of alpha 2,3-sialyltransferase expression correlates with conversion of peanut agglutinin (PNA)+ to PNA- phenotype in developing thymocytes.

Staining of thymus tissue with the plant lectin peanut agglutinin (PNA) is a classic technique for defining the cortical (PNA+) and medullary (PNA-) regions of this tissue. These two regions are primarily composed of immature and mature thymocytes, respectively. Conversion of the PNA+ to the PNA- phenotype has been attributed to masking of the cell surface carbohydrate receptors of PNA by sialic acid during the intrathymic maturation of these cells. We present evidence that the regulated expression of a single glycosyltransferase, a Gal beta 1,3GalNAc alpha 2,3-sialyltransferase, can account for this glycosylation change. This enzyme sialylates the preferred ligand of PNA, Gal beta 1,3GalNAc, forming the sequence NeuAc alpha 2,3Gal beta 1,3GalNAc, thus masking PNA binding sites. Expression of the enzyme is inversely proportional to expression of the PNA receptor, as evidenced by analysis of T-lymphoblastoid cell lines and by in situ hybridization experiments in human thymic tissue.

A novel core protein as well as polymorphic epithelial mucin carry peanut agglutinin binding sites in human gastric carcinoma cells: sequence analysis and examination of gene expression.

The peanut agglutinin (PNA)-binding site is protein-bound Gal beta 1-->3GalNAc, and is a tumor-associated carbohydrate marker expressed in many human carcinomas. PNA-binding glycoproteins isolated from KATO-III human gastric carcinoma cells were deglycosylated by trifluoromethanesulfonic acid, and rabbit antibodies against the core proteins were used to screen a lambda gt11 expression library constructed from these cells. Two different core proteins were identified by this approach. One was polymorphic epithelial mucin (PEM), initially found in breast carcinomas. PEM mRNA was expressed in normal tissues of the stomach, colon, and lung, but not in the small intestine, thyroid, and spleen. High levels of PEM mRNA were detected in some nude mouse-transplanted carcinomas, i.e. colorectal, pancreatic, stomach, and lung carcinomas. The other core protein was a novel one called MGC-24, which has a molecular mass of 24 kDa, is rich in hydroxyl amino acids and cysteine, and lacks repeating motifs. The mature MGC-24 glycoprotein behaved as a high-molecular-mass one upon SDS-polyacrylamide gel electrophoresis even after neuraminidase treatment. Treatment with endo-alpha-N-acetylgalactosaminidase in the absence of neuraminidase significantly changed the staining pattern by anti-MGC-24, confirming that MGC-24 carried PNA-binding sites. MGC-24 mRNA was intensely expressed in normal tissues of the colon, small intestine and thyroid, and in some nude mouse-transplanted colorectal and pancreatic adenocarcinomas.

Mechanical release and lectin labeling of maize root protoplasts

An improved method for the mechanical release of protoplasts from plant tissues is described. The historically-low yield of mechanically-released protoplasts is greatly increased by use of a simple electrically-driven tissue sheer and by optimization of various other steps in the procedure. As counted by light microscopy of a purified preparation, the number of mechanically-released protoplasts obtained is about 6×104 per gram fresh weight of cortical tissue from the primary root of maize (Zea mays L. WF9×Mo 17) seedlings. Nuclear staining of the preparation, however, shows that about half of these protoplasts lack a nucleus and thus are actually subprotoplasts. Comparison of lectin binding to the plasma membranes of mechanically-and enzymatically-released protoplasts shows that both types contain binding sites forRicinus communis agglutinin. Binding sites for peanut (Arachis hypogaea) agglutinin are not naturally present on mechanically-released protoplasts but are generated by exposure to a mixture of Cellulysin and Pectolyase Y-23, the cell wall-degrading enzymes used to prepare enzymatically-released protoplasts.

胃原発Ｂ細胞性悪性リンパ腫に関する免疫組織化学的検討 特にリンパ腫とリンパろ胞との関連性

Immunohistochemical studies were performed on formalin-fixed and paraffin-embedded specimens of 28 cases of primary B-cell type gastric malignant lymphomas. Avidin-biotin complex method was employed to detect peanut agglutinin (PNA) binding sites, lysozyme, and S-100 protein. PNA-binding characteristics similar to those in the nodal lymphomas were also observed in the gastric lymphomas. Lymphoid follicles or lymphoid follicle-like cell aggregation coexistent with gastric lymphomas can be classified into 4 categories according to the morphology and staining patterns. They showed morphological transition from typical secondary follicle to lymphoma cell aggregation according to the distance from lymphoma lesion. It is suggested that lymphoma lesions expand by invading neibouring lymphoid follicles and that some gastric lymphomas grow and spread in the germinal centers of the associated lymphoid follicles. And from these points of view, it is suggested that lymphoid follicles associated with gastric lymphoma play an improtant role as supportive structure for the growth or expansion of lymphomas rather as a defense mechanism of the hosts.

Peanut agglutinin and chondroitin-6-sulfate are molecular markers for tissues that act as barriers to axon advance in the avian embryo

Axon outgrowth between the spinal cord and the hindlimb of the chick embryo is constrained by three tissues that border axon pathways. Growth cones turn to avoid the posterior sclerotome, perinotochordal mesenchyme, and pelvic girdle precursor during normal development and after experimental manipulation. We wanted to know if these functionally similar barriers to axon advance also share a common molecular composition. Since the posterior sclerotome differentially binds peanut agglutinin (PNA) and since PNA binding is also typical of prechondrogenic differentiation, we examined the pattern of expression of PNA binding sites and cartilage proteoglycan epitopes in relation to axon outgrowth. We found that all three barrier tissues preferentially express both PNA binding sites and chondroitin-6-sulfate (C-6-S) immunoreactivity at the time when growth cones avoid these tissues. Moreover, both epitopes are expressed in the roof plate of the spinal cord and in the early limb bud, two additional putative barriers to axon advance. In contrast, neither epitope is detected in peripheral axon pathways. In the somites, this dichotomous pattern of expression clearly preceded the invasion of the anterior sclerotome by either motor growth cones or neural crest cells. However, in the limb, barrier markers disappeared from presumptive axon pathways in concert with the invasion of axons. Since this coordinate pattern suggested that the absence of barrier markers in these axon pathways requires an interaction with growth cones, we analyzed the pattern of barrier marker expression following unilateral neural tube deletions. We found that PNA-negative axon pathways developed normally even in the virtual absence of axon outgrowth. We conclude that the absence of staining with carbohydrate-specific barrier markers is an independent characteristic of the cells that comprise axon pathways. These results identify two molecular markers that characterize known functional barriers to axon advance and suggest that barrier tissues may impose patterns on peripheral nerve outgrowth by virtue of their distinct molecular composition.

Germinal center T cells are distinct helper-inducer T cells

Germinal centers (GCs) contain a significant number of CD4 + T cells, but what role these T cells may play in the development of GC B cells has not been determined. To gain insight into their role, we studied the phenotype of GC T cells and the lymphokines secreted by GC T cells isolated from human tonsils obtained after tonsillectomies. In addition to confirming that a large fraction of GC T cells are Leu-7(CD57) + and Leu-8 −, we found that they have no binding sites for peanut agglutinin. Furthermore, we found that they are CD45RA − and CD45RO +, the phenotype of helper-inducer T cells. We also found that Leu-7(CD57) + cells display CD69, a phenotypic marker of very early cell activation, but do not display three other markers of cell activation: CD25 [interleukin-2 (IL-2) receptor], CD71 (transferrin receptor), and DR. When isolated, Leu-7(CD57) + cells were stimulated in vitro with a mitogen that can induce peripheral blood T cells with the helper-inducer phenotype to produce various cytokines, Leu-7(CD57) + cells did not produce IL-2, interleukin-4 (IL-4), interferon-γ (IFN-γ) or tumor necrosis factor-α (TNF-α) in significant amounts. Taken together, GC T cells form a distinct subpopulation of T cells with helper-inducer phenotype by their histologic location, by their surface phenotype, and by their ability to produce lymphokines. This finding is consistent with the possibility that GC T cells have been selectively recruited to actively help B cells develop in GCs.

A comparative study of histopathology, hormone receptors, peanut lectin binding, ki-67 immunostaining, and nucleolar organizer region-associated proteins in human breast cancer

The current study was performed on 71 cases of human female breast cancer and compares the results of five morphologic methods developed for the detection of estrogen receptors (ER), progesterone receptors (PgR), lectin Peanut agglutinin (PNA) binding sites, monoclonal antibody Ki-67 immunoreactivity, and the mean number of argyrophilic nucleolar organizer regions (Ag-NOR). All the parameters were evaluated on serial cryostat sections representative of a closely related, if not identical, neoplastic population. A significant positive correlation was found between the occurrence of estrogen, progesterone, and peanut receptors and between Ki-67 immunoreactivity, mean number of NOR, and mitotic index. Furthermore, ER, PgR, and PNA receptors showed a significant, inverse correlation with Ki-67 immunoreactivity, mitotic index, and mean number of Ag-NOR. These results provide further data that support the hypothesis that (1) progesterone and PNA receptors are estrogen-induced and indicate a metabolic response of the target cells to functioning estrogen receptors; (2) the mean number of NOR reflects the cell kinetics of the tumor; and (3) metabolic differentiation of neoplastic cells is inversely correlated to the proliferation index.

Squamous cell carcinoma of the prostate

Eleven case of squamous cell carcinoma of the prostate have been divided into four groups according to their histological features and natural history: a pure squamous cell carcinoma of the prostate (one case); b common prostatic adenocarcinoma with malignant squamous component after oestrogen treatment (two); c urothelial carcinoma of the prostate with malignant squamous cell metaplasia (four); and d urothelial carcinoma of the urinary bladder with squamous cell metaplasia growing into the prostate (four). The squamous portions may spread to invade the fibromuscular stroma and grow in prostatic ducts. Necrosis of comedo type and inflammatory infiltrates appeared in a number of cases. The survival times of nine patients ranged from 1 to 17 months. Squamous components were shown by immunohistochemistry to contain various keratin types, carcino-embryonic antigen and peanut agglutinin binding sites. Whenever a squamous cell carcinoma in the prostate is diagnosed histologically various possibilities as to its origin should be considered.

Differences in lectin binding patterns of normal endometrium and endometrial adenocarcinoma, with special reference to staining with Ulex europeus agglutinin 1 and peanut agglutinin

Differences in glycoconjugate composition between proliferative endometrium and endometrial adenocarcinoma were investigated by histochemical techniques using seven different lectins as probes. For light microscopy, the avidin-biotin-peroxidase complex (ABC) method was used. Concanavalin A (Con A), wheat germ agglutinin (WGA), and Ricinus communis agglutinin (RCA) stained almost all glandular cells in both proliferative (normal) and malignant endometria. Ulex europeus agglutinin 1 (UEA-1) strongly stained cancer cells, especially well-differentiated adenocarcinoma, but it scarcely stained normal endometrium. Peanut agglutinin (PNA) binding sites were observed only along the apical surface of normal endometrial glands, while the cytoplasm of endometrial adenocarcinoma cells was often positive for PNA. Soybean agglutinin (SBA) faintly reacted with proliferative endometrium and occasionally with malignant cells. Dolichos biflorus agglutinin (DBA) slightly stained proliferative and malignant endometria. By electron microscopic examinations using horseradish peroxidase (HRP)-labeled lectins, we observed that UEA-1, PNA, and Con A stained the Golgi membranes and plasma membrane of carcinoma cells. In addition, the Con A reaction was positive in the endoplasmic reticulum and nuclear envelope. These results revealed the differences in oligosaccharide chains between normal and malignant endometria, suggesting that UEA-1 and PNA, in particular, may be useful indicators of malignancy of the endometrium.