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We demonstrated here with the high resolution lectin-gold approach and quantitative analysis, changes of glycoconjugates in the hamster zona pellucida (ZP) during oocyte growth and development in the ovary and the oviduct. Glycoconjugates which contain N-acetyl-D-galactosamine as terminal sugar residues are absent in the ovary but are secreted by secretory cells in the oviduct and are added to the ZP of superovulated oocytes during oviductal transit. Glycoconjugates which carry sialic acid as terminal sugar residues appear to be acquired mainly from the ovary. The oviduct contributes little of this particular component to the ZP during the transit of oocytes in the oviduct. On the contrary D-galactose and N-acetylglucosamine associated glycoconjugates, added to the ZP in ovarian follicles, are also secreted by non-ciliated oviductal epithelial cells and these secretory products are transferred to the ZP in significant amount during passage of the oocyte through the oviduct. Lectin-gold labeling of the ZP of superovulated oocytes reveals homogeneous distribution of gold particles throughout the zona matrix. Thus, we conclude that the ZP of hamster superovulated oocytes consists of glycoconjugates that may derive from different origins. Deposition of ZP glycocomponents begins in the ovary. Similar and new glycoconjugates, secreted by oviductal non-ciliated secretory cells, are added to the ZP of oocytes during oviductal transit. At this stage the ZP is made up of a homogeneous matrix of glycoconjugates.
Anat Rec 1991 Jul
PMID:Changes of glycoconjugate contents of the zona pellucida during oocyte growth and development in the golden hamster: a quantitative cytochemical study. 186 9

Mucous neck cells (MNCs) of the fundic gland are phylogenetically thought to have first appeared in amphibians. We studied the origin and differentiation of MNCs in fundic glands of Xenopus laevis. By means of lectin histochemical methods using Griffonia simplicifolia agglutinin-II (GSA-II), MNCs were detected specifically in fundic glands of adult X. laevis. Mucous granules of MNCs were labeled by GSA-II-colloidal gold (CG) staining. Other cells such as surface mucous cells (SMCs), oxynticopeptic cells (OPCs), and endocrine cells did not react to GSA-II. Ulex europaeus agglutinin-I specifically stained OPCs, but not MNCs and SMCs. During the morphogenetic period of the stomach in metamorphosing larvae, GSA-II reactive cells randomly appeared in various portions of the underdeveloped fundic glands and then rapidly localized in the neck portion. At this time, newly appearing mucous granules of MNC type were labeled by GSA-II-CG. Two types of cells intermediate to MNCs and SMCs and intermediate to MNCs and OPCs were observed in the larval gastric region. Cells intermediate to MNCs and OPCs were also found in adults. In these cells, mucous granules of MNC type were labeled by GSA-II-CG, but mucous granules of SMC type and zymogen-like granules did not react to GSA-II. These observations suggest that GSA-II is a useful marker in studying the differentiation of MNCs and their precursors regardless of species differentiation.
Anat Rec 1991 Aug
PMID:Glycoconjugate histochemistry of Xenopus laevis fundic gland with special reference to mucous neck cells during development. 192 55

Asymmetric thick unit membranes were observed on the luminal surface, fusiform vesicles, and multivesicular bodies of superficial cells of rat transitional epithelium. When HRP-labeled Ricinus communis lectin (RCA-I) was injected into the rat urinary bladder, RCA-I was deposited along the luminal cell membrane and in some multivesicular bodies, but not in the fusiform vesicles either before or after contraction. When the bladder was sliced by Vibratome and stained with HRP-labeled RCA-I after fixation, RCA-I was observed in many cell organelles, including fusiform vesicles and multivesicular bodies as well as the luminal surface. When small pieces of tissue were stained en-bloc with HRP-labeled RCA-I, RCA-I was found along the luminal cell surface but not in the fusiform vesicles nor the multivesicular bodies. When HRP alone was injected into the bladder, HRP was observed in some multivesicular bodies after contraction but not in the fusiform vesicles. Various lysosomes were observed by electron microscopy. Some were wrapping multivesicular bodies in ringlike fashion, and some contained asymmetric unit membranes. These findings suggest that the asymmetric unit membranes are carried to the luminal cell membrane via the fusiform vesicles and that old luminal cell membranes are removed via the multivesicular bodies to be degraded by lysosomes.
Anat Rec 1991 Jan
PMID:Turnover of asymmetric unit membranes in the transitional epithelial superficial cells of the rat urinary bladder. 199 88

Previous cytochemical studies showing that rat primordial germ cells (PGCs) possess a unique surface glycoconjugate containing terminal alpha-N-acetylgalactosamine were extended in this study to determine whether a similar distinctive glycoconjugate coats the surface of PGCs in the mouse. The results showed that mouse PGCs fail to react with peroxidase-conjugated lectins specific for localizing glycoconjugate with terminal N-acetylgalactosamine. All available lectin conjugates with affinity for other terminal sugars or internal sugar linkages also failed to stain mouse PGCs except for the conjugates that bind to alpha-fucose. One fucose-specific lectin conjugate stained only PGCs in the early mouse embryo but stained additional sites in more mature embryos and lost reactivity with PGCs after gestational day 14. Another fucose-specific conjugate stained PGCs until day 15, but with less selectivity, and a third such conjugate bound to several sites, but not to PGCs. The results suggest that the developmental mechanisms mediating cellular interaction, migration, and differentiation may be similar in different genera, but the specific structure of the cell surface glycoconjugate involved in these mechanisms differs.
Anat Rec 1990 Oct
PMID:Glycoconjugate unique to migrating primordial germ cells differs with genera. 224 Jun 10

We have previously localized an antigen of oviductal origin to the zona pellucida of superovulated hamster oocytes (Kan et al.: Journal of Histochemistry and Cytochemistry 36:1441-1447, 1988) and described the intracellular distribution of this antigen in the oviductal epithelium (Kan et al.: Biology of Reproduction 40:585-598, 1989). These results led to our hypothesis that the oviduct is a bona fide site of origin of certain components of the zona pellucida. In this report, using the high resolution lectin-gold approach with Helix pomatia lectin (HPL)-colloidal gold complex, we present cytochemical evidence to show that glycoconjugates containing terminal N-acetyl-D-galactosamine residues are absent from the zona pellucida of ovarian oocytes but are synthesized and secreted by the nonciliated secretory cells of the oviduct and later become associated with well-defined structural elements of the zona matrix of oocytes during passage through the oviduct. The nature of the HPL-binding glycoconjugates was determined by biochemical analyses. Electrophoretic and immunological experiments demonstrated that the glycoconjugates correspond to the high molecular weight polydispersed glycoprotein that we have previously described. We have designated this glycoprotein "hamster oviductin 1" (Hm OV-1). Our results further substantiate the belief that the oviduct is a source of origin of zona pellucida constituents.
Anat Rec 1990 Jan
PMID:Demonstration by lectin-gold cytochemistry of transfer of glycoconjugates of oviductal origin to the zona pellucida of oocytes after ovulation in hamsters. 229 82

Lectin histochemistry was used to examine the expression of cell surface glycoconjugates during secondary neurulation in chick embryos. Fourteen lectins were applied to serial sections of the caudal region of embryos at the various stages of tail bud development. The lectins Bandeiraea simplicifolia, Dolichos biflorus agglutinin, Phaseolus vulgaris leukoagglutinin, soybean agglutinin, Sophora japonica agglutinin, Ulex europaeus agglutinin and succinylated wheat germ agglutinin (sWGA) showed very light or no binding to the developing medullary cord of the tail bud. With the other lectins, staining occurred throughout the early tail bud and solid medullary cord. During cavitation, however, differential expression of cell surface glycoconjugates by different cell populations was observed. The lectins concanavalin A, Lens culinaris agglutinin, Pisum sativum agglutinin, Phaseolus vulgaris erythroagglutinin, Ricinus communis agglutinin and WGA showed basic similarities in the distribution of lectin binding. Of these, the binding pattern of WGA was the most striking. As the medullary cord cells were separating into central mesenchymal and peripheral epithelial populations, WGA bound preferentially to the epithelial cells and the notochord. The lectin PNA, however, became preferentially bound to the mesenchymal cells. Heavy staining by WGA (specific for N-acetylglucosamine and sialic acid) where sWGA staining (specific for N-acetylglucosamine only) was faint suggested that WGA binding was due to the presence of sialic acid containing glycoconjugates.
Anat Rec 1990 Jan
PMID:Distribution of cell surface glycoconjugates during secondary neurulation in the chick embryo. 229 85

Although neural crest (NC) cells can potentially enter a number of intertissue spaces, they select a particular pathway that varies depending on the axial level. In the cranial region, NC cells enter the dorsal-lateral pathway (i.e., immediately subjacent to the ectoderm) and avoid the ventral pathway (i.e., pathway between the mesoderm and neural tube and within the mesodermal cell population), whereas in the trunk region, the majority of the NC cells enter the ventral pathway (i.e., between the somite and neural tube) and not the dorsal-lateral pathway. Our working hypothesis is that one determining factor in directing NC cell migration is the composition and/or intermolecular associations of the extracellular matrix (ECM) in these pathways. Histochemical staining, immunostaining, and lectin-binding studies on cryofixed and conventionally fixed tissue were conducted to initially characterize the ECM found in potential NC cell pathways prior to and during initial NC cell migration at two different axial levels. We found that, regardless of the axial level, the pathways into which NC cells eventually enter possessed a characteristic ECM arrangement. This arrangement included: 1) the presence of multicomponent, glycoprotein-containing spherical particles (0.1-0.5 micron in diameter); and 2) a low-sulfated ECM content. Although all particles contained fibronectin, only those in specific regions were able to bind to a monoclonal antibody directed to the cell-binding domain of fibronectin, suggesting that the conformation of fibronectin may be important in the expression of any in situ function of the molecule.
Anat Rec 1988 Sep
PMID:Specific configurations of fibronectin-containing particles correlate with pathways taken by neural crest cells at two axial levels. 246 Nov 26

The synthesis and secretion of enamel proteins (EPs) in rat incisors was examined using cytochemical and biochemical methods. Radioautography after injection of 3H-methionine showed that ameloblasts in the presecretory, secretory, and maturation stages of amelogenesis actively synthesized and secreted proteins. Immunocytochemistry with an antibody to mouse amelogenins revealed the presence of EPs in the protein synthetic and secretory organelles of these cells at all three stages. Labeling was also found in elements of the endosomal/lysosomal compartment. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and silver staining of proteins extracted from enamel and enamel organ showed several protein bands. However, transfer to nitrocellulose paper and immunoblotting revealed that most of the proteins recognized by the antibody were situated between approximately 14 and 32 kDa. EPs were further characterized by using lectins to examine their carbohydrate content. Lectin-gold cytochemistry on sections showed the binding of wheat germ agglutinin and Helix pomatia lectin to secretory stage enamel. Lectin blotting indicated that the amelogenins were heterogeneously glycosylated and contained the sugars N-acetyl-glucosamine/N-acetyl-neuraminic acid and N-acetyl-D-galactosamine. Fluorography at 6 and 10 min and 1 h after injection of 35S-methionine revealed four labeled bands in the main amelogenin group near 22, 28, 30, and 32 kDa. A short-lived protein of approximately 58 kDa was also observed primarily in cells. The appearance of labeled proteins in enamel was paralleled by their disappearance from cells and the intensity of the radiolabeled protein bands, both, in enamel and in cells, decreased towards the maturation stage. These data are consistent with the concept that ameloblasts produce multiple amelogenins throughout amelogenesis.
Anat Rec 1989 Jun
PMID:Biosynthesis and secretion of enamel proteins in the rat incisor. 277 7

The distribution of motoneurons innervating the primary depressor and elevator muscles of the wing of the domestic pigeon (Columba livia) was studied by using the retrograde axonal tracer lectin-conjugated horseradish peroxidase (WGA-HRP). Injection of WGA-HRP into the pectoralis (pars thoracicus) labeled neurons in the ventromedial corner of the lateral motor column of the spinal cord. These neurons were arranged in a column extending from spinal segment X or XI to spinal segment XII or XIII. The pectoralis, the primary depressor muscle of the wing, consists of two parts which are anatomically and functionally distinct, the sternobrachialis (SB) and thoracobrachialis (TB). Injection into the SB labeled neurons in the rostral and middle regions of the pectoralis motoneuron column. In contrast, injection into the TB labeled neurons in the middle and caudal regions of the pectoralis motoneuron column. Injection into the primary elevator muscle of the wing, the supracoracoideus, labeled neurons in the lateral motor column in spinal segments X and XI. These motoneurons were located dorsolateral to motoneurons labeled following pectoralis injection. These data demonstrate musculotopic segregation of the motoneurons innervating the primary flight muscles in the pigeon and, further, illustrate that the SB and TB subregions of the pectoralis are innervated by discrete aggregations of motoneurons.
Anat Rec 1989 Sep
PMID:Musculotopic innervation of the primary flight muscles, the pectoralis (Pars thoracicus) and supracoracoideus, of the pigeon (Columba livia): a WGA-HRP Study. 277 11

A method for preparative isolation of human monoclonal antibody isoproteins is described in the present paper. A human monoclonal antibody directed against the transmembrane protein gp 41 from the human immunodeficiency virus (HIV-1) was used in this study. The antibody belongs to the IgG1 subtype and exhibits antibody dependent cellular cytotoxicity. The resolving power of conventional preparative protein separation techniques such as ion-exchange chromatography, chromatofocusing and lectin affinity chromatography is too poor for a complete separation of isoproteins. The more sophisticated technique of chromatofocusing on FPLC-based material (Mono P, Pharmacia) did not satisfy our expectation. With semipreparative IEF in immobilized pH gradients we were able to prepare the different isoproteins of a human monoclonal antibody in milligram amounts. No significant difference between the single isoproteins with respect to specificity and avidity to the recombinant antigen (rec gp 160) was detected. Therefore, we assume that the separation conditions did not influence the immunochemical nature of the antibody and significant denaturation and/or precipitation of the IgG did not occur. Furthermore the method affords preparative separation with resolution equivalent to analytical runs. Experiments for scale up and further characterization of isoproteins (carbohydrate composition, amino acid analysis, half life times etc.) are in progress.
 ...
PMID:Isolation of human monoclonal antibody isoproteins by preparative isoelectric focusing in immobilized pH gradients. 277 64


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