UMLS:C0162871 - FACTA Search

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Query: UMLS:C0162871 (abdominal aortic aneurysm)
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The oligosaccharide sequences of glycoconjugates and the nature of the saccharide linkage were investigated in normal human testes by means of lectin histochemistry studies, at light and electron microscopy levels. Reaction to WGA was intense in the seminiferous epithelium and interstitium. MAA showed light reactivity in all cell types of the human seminiferous epithelium, the lamina propria and Leydig cells. UEA-I lectin labelled the lamina propria intensely and the seminiferous epithelium and Leydig cells slightly. A slight reaction to AAA was found in the seminiferous epithelium and in Leydig cells. ConA was labelled in Sertoli cells, germ cells and Leydig cells. The reaction to GNA lectin was similar although less intense. PNA labelling was slight in Sertoli cells, spermatogonia, and Leydig cells, and more intense in spermatocytes, spermatids and peritubular cells. Reaction to DSA was intense in the seminiferous epithelium and Leydig cells. HPA labelled all cell types in the seminiferous epithelium and Leydig cells slightly, and labelled peritubular cells intensely. SBA lectin showed a strong reaction in spermatids and a slight reaction in the lamina propria. The reactions to SNA, LTA, and DBA were negative in all testicular cell types. After beta-elimination pre-treatment, MAA, UEA-I, AAA, PNA, DSA, HPA and SBA reactions were all negative. Endo F/PNGase digestion suppressed reactivity to ConA y GNA. Staining for WGA decreased with Endo F/PNGase digestion and also after beta-elimination. Desialization increased reactivity to PNA, SBA and HPA lectins. These results indicate that the terminal sequences of oligosaccharide side-chains in spermatocytes and, principally, in spermatids are: fucose, mannose, Neu5Ac2,3Gal1,3GalNAc, Gal1,3GalNAc, Gal1,4GlcNAc, Neu5AcGalNAc and GalNAc (in O-glycosylated proteins); mannose (in N-glycosylated proteins) and GlcNAc (in both protein types). A sialic acid residue is added to galactose and GalNAc residues. Present findings also indicate that Sertoli cell glycoproteins are similar to those of spermatids, and that the terminal sugar residues in Leydig cells are GlcNAc, fucose, mannose, Neu5Ac2,3Gal1,3GalNAc, Gal1,3GalNAc, and Gal1,4GlcNAc. The lectin pattern of the lamina propria suggests the presence of GlcNAc, galactose, fucose and GalNAc.
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PMID:Lectin histochemistry of the human testis. 997 91

The oligosaccharide sequences of glycoconjugates in the normal human vas deferens and the nature of the saccharide linkage were studied by lectin histochemistry. The cytoplasm of all epithelial cell types (principal cells, basal cells, and mitochondria-rich cells) and luminal contents reacted positively with WGA, MAA, PNA, DSA, LTA, UEA-I, AAA, and ConA. The reaction was more intense in the stereocilia of principal cells. Cytoplasmic staining was diffuse except for PNA and DSA labeling which was limited to the apical cytoplasm and stereocilia of columnar cells. The cytoplasm of all cell types also reacted diffusely with HPA, although staining was weak and was not observed in the stereocilia. Positive reaction with SBA only was encountered in the stereocilia of principal cells. SNA, LTA, and DBA were unreactive. GNA-labeling showed a granular distribution in the supranuclear cytoplasm of columnar epithelial cells. Reactions with MAA, PNA, DSA, AAA, HPA and SBA disappeared after the beta-elimination reaction. Reactions with WGA and UEA-I decreased after beta-elimination or Endo-F digestion. Reactions with ConA and GNA were suppressed by Endo-F digestion. Reactions with PNA, HPA, and SBA increased after desialylation. Of all the lectins that label the luminal contents of the vas deferens, only UEA-I was not found in the luminal contents of seminiferous tubules and epididymis and, thus, this lectin would probably bind to glycoproteins secreted by the vas deferens. The chemical treatments used suggest that this secretion contains fucose residues located in both N- and O-linked oligosaccharides. The other lectins may label secreted proteins, but also structural proteins or proteins reabsorbed from the luminal fluid. The lectin- binding pattern of mitochondria-rich cells in the vas deferens differed from that found in the epididymis.
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PMID:Lectin histochemistry study in the human vas deferens. 1038 93

The partial oligosaccharide sequences of glycoconjugates and the nature of their glycosidic linkages were investigated in normal human prostate, benign prostatic hyperplasia (BPH) and prostatic carcinoma by means of lectin histochemistry, using light microscopy and Western blot analysis. The labeling pattern of BPH differed from that of normal prostate in having more intense staining with DSA, HPA, UEA-I and AAA, and in showing lesser staining with WGA and SBA. Prostatic carcinoma differed from normal prostates in displaying the more intense labeling with PNA, DSA, SBA, DBA, UEA-I and AAA, and in having lesser labeling with WGA. The main differences in labeling pattern between prostatic carcinoma and BPH were that the latter specimens showed more marked staining with PNA, DSA, DBA, SBA, UEA-I and AAA, and lesser staining with WGA and HPA. The staining patterns of SNA, MAA, ConA, LCA and GNA were similar in all three groups of specimens. For most of the lectins studied, including those showing a similar immunohistochemical staining in the three groups of specimens studied, the Western blot analysis showed differences in the banding pattern among normal, hyperplastic, and carcinomatous prostates. Present results suggest that the glycosylation of proteins was modified in both BPH and prostatic carcinoma. In BPH a strong expression of N-acetylgalactosamine residues occurred, while in prostatic carcinoma an increase of sialic acid, galactose and fucose residues was observed. No changes in mannose residues were detected.
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PMID:A lectin histochemistry comparative study in human normal prostate, benign prostatic hyperplasia, and prostatic carcinoma. 1061 10

In the present study, lectin-gold cytochemistry and antibodies against ZP2 and ZP3 glycoproteins were used to investigate the oligosaccharide content of mouse ovarian zona pellucida (ZP) during follicular development. The entire thickness of the ZP and several organelles of the oocyte (cortical granules, Golgi apparatus, and vesicular aggregates) were reactive to RCA-I, DSA, AAA, WGA, MAA, and LFA throughout follicular development. HPA labeling was not detected at the earliest stages of follicular folliculogenesis. HPA reactivity was first observed in the ZP, Golgi apparatus, and the vesicles of oocytes at the trilaminar primary follicle stage. HPA labeling in the ZP was always restricted to the inner region of the zona matrix. After neuraminidase treatment, HPA reacted with the entire ZP in ovarian follicles at different stages of development. Immunolabeling with specific antibodies showed that, although ZP2 and ZP3 glycoproteins were uniformly distributed in the zona matrix of ovarian oocytes, there was a progressive increase in thickness of the ZP in parallel with the proliferation of follicular cells. ZP3 glycoprotein was also localized to the Golgi apparatus and vesicular aggregate. The present results suggest: (1) a difference in composition of carbohydrate content between the inner and outer region of the fully developed ZP generated probably by a modification in the biosynthetic pathway of oligosaccharides in the oocyte during folliculogenesis, (2) that newly synthesized ZP glycoproteins displace previously synthesized ZP components in a direction toward the follicular cells and, therefore, no redistribution of the ZP matrix occurs during folliculogenesis, and (3) that the vesicular aggregates in the ooplasm constitute an intermediate step in the secretory pathway of ZP glycoproteins.
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PMID:Cytochemical demonstration of modification of carbohydrates in the mouse zona pellucida during folliculogenesis. 1081 75

The aim of this work is the characterization of the glycoconjugates of the spermatids during the spermiogenesis of the testis of an urodele amphibian, Pleurodeles waltl, by means of lectins in combination with several chemical and enzymatic procedures, in order to establish the distribution of N- and O-linked oligosaccharides in these cells. The acrosome was the most relevant lectin-labeled structure. The O-linked oligosaccharides contained DBA- and SBA-positive GalNAc, AAA-positive Fuc and PNA-positive Gal beta1,3GalNAc. Sialic acid was scarcely observed, the Neu5Ac alpha2,3Gal beta1,4GlcNAc sequence was found in N-linked oligosaccharides. Additionally, N-linked oligosaccharides containing HPA-positive GalNAc and AAA-positive Fuc were found. Moreover, with some lectins the acrosome showed a variable composition of the oligosaccharides in the different steps of the sperm maturation. Some residues were found only in the early steps in maturating acrosome, while others were in the later steps, showing that acrosomal glycoconjugates are modified during acrosome development in spermiogenesis. The changes observed during acrosome maturation suggest the existence of a predetermined pattern of storage of the acrosome components and a progressive compression of them.
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PMID:Lectin histochemical localization of N- and O-linked oligosaccharides during the spermiogenesis of the urodele amphibian Pleurodeles waltl. 1097 42

The present study describes the sugar content of the seminiferous epithelium, using lectin histochemistry, in healthy boars and in boars with unilateral and bilateral abdominal cryptorchidism. In healthy boars the apical cytoplasm of Sertoli cells exhibited abundant glucosyl (Con A and WGA lectins), galactosyl (HPA, DBA, SBA and PNA lectins), and fucosyl (AAA lectin) residues. Spermatogonia and spermatocytes contained abundant glucosyl (Con A and WGA lectins) and fucosyl (AAA lectin) residues. In spermatids, galactosyl (SBA and PNA lectins) and glucosyl (Con A and WGA lectins) residues increased progressively throughout spermiogenesis, and fucosyl (AAA lectin) residues decreased. As compared with healthy boars, the scrotal testis of unilateral cryptorchid boars showed decreased amounts of fucosyl (AAA lectin) and galactosyl (HPA and DBA lectins) residues on the Sertoli cell apical cytoplasm; spermatocytes exhibited higher content of glucosyl (Con A lectin) residues and spermatids showed altered nature of glucosyl (Con A and WGA lectins) and galactosyl (SBA and PNA lectins) complexes. In abdominal testes of unilateral and bilateral cryptorchid boars, immature Sertoli cells and spermatogonia showed decreased fucosyl (AAA lectin), and increased glucosyl (Con A and WGA lectins) and galactosyl (SBA and PNA lectins) contents. These results suggest that the seminiferous epithelium of healthy boars has polarized activity with the apical compartment implicated in germ cell-Sertoli cell adhesion and interaction, in transport of ions, substrates and fluids, and in acrosomal differentiation. In scrotal testes, unilateral abdominal cryptorchidism could lead to defective germ cell-Sertoli cell adhesion, impaired acrosomal differentiation and increased ionic transport in the apical compartment of the seminiferous epithelium. Unilateral and bilateral cryptorchidism could induce increased ionic transport and membrane permeability in the seminiferous epithelium of abdominal testes.
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PMID:Lectin affinity of the seminiferous epithelium in healthy and cryptorchid post-pubertal boars. 1138 Jul 4

In the present study, we have employed a battery of colloidal gold-tagged lectins as probes in conjunction with quantitative analysis to demonstrate the distribution and changes of carbohydrate residues in the hamster zona pellucida (ZP) during ovarian follicular development and during transit of the oocyte through the oviduct after ovulation. High-resolution lectin-gold cytochemistry performed on thin sections of LR White-embedded ovaries revealed a moderate to strong reactivity to WGA, PNA, DSA, AAA, and MAA over the entire thickness of the ZP of ovarian oocytes at different stages of follicular development. Labeling intensity over the ZP progressively increased as follicles matured in the ovary. In parallel, there was an association of labeling by gold particles with cortical granules, stacks of Golgi saccules, and complex structures called vesicular aggregates in the oocyte proper especially during the late stages of follicular growth. In contrary, labeling with each of HPA, DBA, and BSAIB(4) was absent in the ovary but was found to be localized over Golgi complexes and secretory granules in the non-ciliated secretory cells of the oviduct. When ovulated oocytes were labeled with each of HPA, WGA, RCA-I, PNA, DSA, BSAIB(4), AAA, MAA, and DBA, the ZP and several organelles in the oocyte proper presented a differential distribution of lectin-binding sites. Quantitative analysis was also performed on labeling by lectin-gold complexes that bind specifically to the ZP of mature follicular and ovulated oocytes. Quantitative evaluation revealed heterogeneous labeling between the inner and the outer zone of the ZP. A significant increase in the labeling densities in both inner and outer ZP was noted when tissue sections of ovulated oocytes were labeled with RCA-I or AAA. Tissue sections of ovaries labeled with WGA demonstrated a significant increase in the density of labeling in the outer layer of the ZP. Labeling by PNA, DSA, and MAA, however, showed a significant decrease in both the inner and outer portions of the ZP. Together, these results suggest that in the hamster, glycoproteins carrying specific sugar residues are added to the ZP of ovarian follicles during the early stages of folliculogenesis and are processed through a common secretory machinery, and that there is a significant change in both the sugar moieties and distribution of glycoproteins in the ZP following ovulation. Our results also showed that the hamster oviduct plays an important role in contributing certain glycoproteins to the ZP suggesting that the sugar moieties of these oviductal glycoproteins may have functional significance in fertilization.
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PMID:Distribution of lectin-binding glycosidic residues in the hamster follicular oocytes and their modifications in the zona pellucida after ovulation. 1174 63

Lectins were used as probes in conjunction with quantitative analysis to investigate the distribution of different carbohydrate residues in hamster zona pellucida and their possible modification patterns after in vivo fertilization and in vitro egg activation. Several lectins including HPA, WGA, RCA-I, PNA, DSA, BSAIB(4), DBA, AAA and MAA were used to label the zona pellucida of both unfertilized and fertilized eggs. With the exception of PNA and BSAIB(4), the same lectins were also used to label the zona pellucida of oocytes activated in vitro. A multicomparison quantitative analysis of the density of labelling in the inner and outer regions of the zona pellucida before and after fertilization in vivo, as well as after in vitro egg activation, was performed. Of all the lectins studied, preferential localization of labelling by RCA-I and DSA to the inner zona pellucida of unfertilized eggs was observed. After in vivo fertilization, there was an increase in labelling in the inner region of the zona pellucida when thin sections of fertilized oocytes were incubated with HPA, BSAIB(4) and AAA. Although increased labelling by RCA-I was observed, a significant decrease in labelling intensity was obtained with WGA and the sequence Neu-WGA in both the inner and outer zona pellucida of fertilized oocytes. A significant increase in the density of labelling with WGA was also observed after digestion with neuraminidase. In parallel, when hamster oocytes activated in vitro were compared with those fertilized in vivo, a difference in lectin-gold labelling was observed in both the inner and outer region of the zona pellucida. Labelling with HPA, WGA, DSA and MAA increased significantly in both the inner and outer regions of the zona pellucida, whereas labelling by DBA significantly decreased in the inner portion of the zona pellucida. After neuraminidase treatment, a significant increase in labelling density was observed when thin sections of in vitro-activated oocytes were incubated with WGA. These results demonstrate: (i) the post-fertilization modifications of major saccharidic determinants that may play a role in the sperm-egg interaction process of fertilization in vivo; and (ii) that the modified properties of zonae pellucidae of fertilized and in vitro-activated eggs resulting from the action of hydrolytic enzymes, as well as glycoproteins released through exocytosis of cortical granules, are not identical.
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PMID:Variations in modifications of sugar residues in hamster zona pellucida after in vivo fertilization and in vitro egg activation. 1200 95

Carbohydrate-binding polypeptides, including carbohydrate-binding modules (CBMs) from polysaccharidases, and lectins, are widespread in nature. Whilst CBMs are classically considered distinct from lectins, in that they are found appended to polysaccharide-degrading enzymes, this distinction is blurring. The crystal structure of CsCBM6-3, a "sequence-family 6" CBM in a xylanase from Clostridium stercorarium, at 2.3 A reveals a similar, all beta-sheet fold to that from MvX56, a module found in a family 33 glycoside hydrolase sialidase from Micromonospora viridifaciens, and the lectin AAA from Anguilla anguilla. Sequence analysis leads to the classification of MvX56 and AAA into a family distinct from that containing CsCBM6-3. Whilst these polypeptides are similar in structure they have quite different carbohydrate-binding specificities. AAA is known to bind fucose; CsCBM6-3 binds cellulose, xylan and other beta-glucans. Here we demonstrate that MvX56 binds galactose, lactose and sialic acid. Crystal structures of CsCBM6-3 in complex with xylotriose, cellobiose, and laminaribiose, 2.0 A, 1.35 A, and 1.0 A resolution, respectively, reveal that the binding site of CsCBM6-3 resides on the same polypeptide face as for MvX56 and AAA. Subtle differences in the ligand-binding surface give rise to the different specificities and biological activities, further blurring the distinction between classical lectins and CBMs.
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PMID:Structure and ligand binding of carbohydrate-binding module CsCBM6-3 reveals similarities with fucose-specific lectins and "galactose-binding" domains. 1263 60

The objective of the present study was to characterize glycoconjugates of hamster testis in gonadally-active and -inactive states by lectin histochemical methods. Thirteen HRP- or digoxigenin-labeled lectins were used in samples obtained from fertile and photoinhibited hamsters. In gonadally-active hamsters, spermatozoa tails were stained with Con-A, HPA, PNA, UEA-I, LTA, AAA, WGA and LFA and weakly with GNA and RCA-I. Spermatozoa acrosomes were labeled with HPA, SBA, WGA and PNA. Spermatid acrosomes were labeled with SBA, RCA-I, PNA, and WGA. Staining with GNA and Con-A was found in the Golgi phase and HPA staining was found in the Golgi phase and maturated spermatids. Cytoplasm of spermatocytes was labeled with Con-A, GNA, LTA, AAA, RCA-I, HPA, WGA and LFA, whereas spermatocyte membranes were stained with Con-A, LTA and AAA. Spermatogonia were strongly labeled with Con-A and moderately labeled with AAA, WGA and LFA. Sertoli cells were positive after staining with Con-A, AAA, WGA, and LFA. The lamina propria was positive after staining with UEA-I, LTA, AAA and LFA. Leydig cells showed strong labeling with SBA, Con-A, GNA, SNA and MAA, moderate labeling with WGA, weak labeling with RCA-I, AAA and LFA. In gonadally-inactive hamsters, spermatocytes showed increased staining with HPA, PNA and AAA, whereas staining with Con-A, GNA and LTA had disappeared. Spermatogonia showed an increased labeling with AAA and WGA, but labeling with Con-A and LFA had disappeared. Sertoli cells were strongly labeled with GNA. Con-A and GNA staining was decreased in Leydig cells of gonadally-inactive hamsters but PNA and HPA staining was increased. The lamina propria in regressed testes showed intense labeling with PNA. These results suggest that histological, morphological and hormonal changes occurring in hamster testis during exposure to a short photoperiod are reflected in altered patterns of expression and distribution of N- and O-linked glycans.
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PMID:Histochemical study of glycoconjugates in active and photoperiodically-regressed testis of hamster (Mesocricetus auratus). 1283 Nov 68

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