2 edition of pattern and specificity of lectin binding to normal and abnormal human sperm found in the catalog.
pattern and specificity of lectin binding to normal and abnormal human sperm
Yi Ni Chen
Thesis (M.Med.Sc.) - University of Birmingham, Dept. of Obstetrics and Gynaecology, 1992.
|Statement||by Yi Ni Chen.|
RESULTS. LSECtin Is a Novel Member of the C-type Lectin Family—To identify novel adhesion molecules of the C-type lectin family, the expressed sequence-tagged data base (dbEST) of the cDNA library of human fetal liver in our laboratory was searched with the CRD domains of CD23, DC-SIGN, and novel EST (D), which is bp and . Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation .
This is probably the best-known functional sperm defect (Afzelius et al., ; Escalier and David, ), which typically presents at semen analysis as normal numbers of spermatozoa with apparently normal morphology in stained smears combined with normal levels of sperm vitality – but essentially zero by: 8. Lectin histochemical findings of the kidney of diabetic animal Lectin reactivities in the kidney of diabetic animals at 3 MAI are shown in Table 2. Apart from an increase in the intensity of lectin reactivity at 3 MAI, the lectin binding characteristics were Cited by: 7.
the staining pattern is presented, allowing the inves- tigator to distinguish between intracellular and sur- face labeling; and (c) stained glands ready for view- ing can be obtained within 2 h of fixation. Second, the observed distribution of lectin-binding sites in. Genetic Polymorphisms of Mannan-binding Lectin (MBL)and Serum Levels of MBL in Patients With Endometriosis The safety and scientific validity of this study is the responsibility of the study sponsor and investigators.
The daddy factor
Position papers for the Symposium on the Parish and the Educational Mission of the Church.
Rain: A Great Day for Ducks
Appletons medical dictionary
Taku Glacier evaluation study.
Problems of petroleum geology
Constitution and by-laws
The trade gap in food and drink.
Memoir of the life and episcopate of George Augustus Selwyn, D.D., Bishop of New Zealand, 1841-1869, Bishop of Lichfield, 1867-1878
Further guide for the retrieval of dropsize distributions in water clouds with a ground-based clear-air-sensing doppler radar
Atlas of Mercury
Cincinnatis historic Findlay Market
Estimate of Known Recoverable Reserves of Coking Coal in Grundy County, Tenn.
Discipline at work
bookseller of the last century
Characterization of the lectin binding pattern in human spermatozoa after swim-up selection María José Gómez-Torres 1, Manuel Avilés 2, Jose Luis Girela 1, Verónica Murcia 1 *.
The lectin binding profiling of human sperm. The human sperm surface is decorated with a thick layer of glycans, i.e., the glycocalyx. Though it is known that some lectins have positive bindings to human sp29,30,31, the overall picture of the glycan composition of human sperm glycocalyx is still took advantage of the established lectin microarray based Cited by: The inheritance pattern of mannose-binding lectin deficiency is unclear.
Some reports show that having a disease-associated mutation in one copy of the MBL2 gene in each cell can lead to the condition, while other reports state that a mutation in both copies of the gene is necessary. It is important to note that people inherit an increased risk of developing mannose-binding lectin.
The pattern of lectin binding in normal human labial mucosa was examined by light and electron microscopy using eight different lectins (ConA, LCA, WGA, UEA-1, RCA-1, SBA, DBA and PNA) and compared with the patterns in normal human skin and oesophageal mucosa.
As seen by light microscopy, ConA, LCA, and WGA stained cell membranes in all Cited by: 7. Lectins and Specificity: Lectin Characteristics and Properties Lectins are proteins that form reversible complexes with mono- or oligosaccharide strength of the binding event increases with the number of molecular interactions and thus from monovalent interactions to multivalent complexes.
Characterization in the lectin staining patterns in selected human sperm The distribution of lectin binding pattern was observed in human sperm after the swim-up selection (Table 2).
With AAA lectin the most frequent pattern after selection was P4 (%), this pattern was also the most representative in fresh sperm. However, patterns P2. However, previous studies have shown that some sperm showing good motility have membrane damage.
The aim of our study was to characterize the lectin staining pattern on the sperm plasma membrane of unselected and selected human sperm of normozoospermic donors. Sperm selection was performed by the swim-up by: Lectin binding patterns in normal human endometrium were examined by light and electron microscopy using seven different lectins (ConA, WGA, RCA, PNA, UEA-1, DBA, and SBA).
For light microscopic observations, criteria based on the incidence and intensity of cells positive for the lectin staining were adopted to evaluate the different staining patterns of the Cited by: A sequential study was performed with electronic microscopy and flow cytometry techniques, where the binding of 4 lectins was assessed on normal human sperm samples during in.
Differences in lectin binding patterns of normal human endometrium between proliferative and secretory phases D. Aoki, H. Kawakami, S. Nozawa, Y. Udagawa, R. Iizuka, H. Hirano Department of Obstetrics and Gynecology (Gynecology)Cited by: GYNECOLOGIC ONCOL () Differences in Lectin Binding Patterns of Normal Endometrium and Endometrial Adenocarcinoma, with Special Reference to Staining with Ulex europeus Agglutinin 1 and Peanut Agglutinin DAISUKE AOKI, M.D.,*'' SHIRO NOZAWA, M.D.,* RIHACHI IIZUKA, M.D.,* HAYATO KAWAKAMI, PH.D.,+ AND HIROSHI HIRANO, Cited by: Mannose-binding lectin (MBL), also called mannan-binding lectin or mannan-binding protein (MBP), is a lectin that is instrumental in innate immunity Human MBL2 gene is located on chromosome 10qq whose function appears to be pattern recognition in the first line of defense in the pre-immune s: MBL2, COLEC1, HSMBPC, MBL.
Soluble pattern recognition proteins were purified from human serum and identified as human mannose-binding lectin (MBL) and l-ficolin. The use of specific microbial cell component-coupled columns demonstrated that MBL and l -ficolin bind to PGN and 1,3-β- d -glucan, respectively.
Bovine genital tritrichomonosis is caused by the protozoon Tritrichomonas foetus and leads to embryonic death and abortion. The complexity of handling Cited by: 8.
Whereas ConA binding was proved to be positive in the plasma membrane, endoplasmic reticulum, Golgi apparatus and nuclear envelope of normal and malignant cells. These results indicate that sugar components of endometrial glycoconjugates change during the menstrual cycle and differ between normal endometrium and endometrial : Daisuke Aoki.
the effect of infection with Brucella abortus on the pattern of lectin binding in bovine fetal lungs (n=6) and bovine placentas (n=5). Fetal lungs and placenta from heifers experimentally inoculated with B.
abortus, strain were examined by histological, lectin-histochemical, immunohistochemical and cultural techniques. abortus antigens. Differences in Lectin Binding Patterns of Normal Endometrium and To confirm the specificity of lectin staining, some sec- differences in staining pattern were recognized between normal and malignant endometria.
AOKI ET AL. TY - JOUR. T1 - An immunofluorescent analysis of lectin binding to normal and regenerating skeletal muscle of rat. AU - Gulati, Adarsh K.
AU - Zalewski, Andrew by: Cellular localization of lectin-affinity in tissue sections of normal human duodenum K. WURSTER 1, P. PESCHKE2, and W. KUHLMANN2 1 Institut für Pathologie, Städtisches Krankenhaus München-Schwabing, D München, Germany, and 2 Labor für Experimentelle Medizin, Institut für Nuklearmedizin DKFZ, D Heidelberg, Germany Virchows Arch [Pathol Anat].
PAPERS&ARTICLES Concentration Lectin Acronym (pg/mi) Specificity* Arachishypogoea PNA 10 fD-Gal(>3) D-GaINAc Ricinuscommunis-!RCA-I 30 13,Gal Glycinemaximus SBA 30 a-D-GaINAc;f-D-GaINAc Dolichosbiflorus QBA 30 a-D-GaNAc tcm vdgoris WGA 30 f-DGICN;NeuNAc Concinl enshifris ConA 30 fJ-D-Man; a-D-Glc heterophyllus Jacalin) JAC 30 a-Gal'Ga1f3 Cited by: 1.
Differential Binding of Lectins to M Cells and Enterocytes in the Rabbit Cecum 5-nm gold, or lo-nm gold. For lectins, lectin abbreviations, and normal sugar specificities, see Table 1.
The lectins were purchased from Medac (Hamburg, Ger- many) or from Sigma (Deisenhofen, Germany). Specificity Lectin Selective binding to M cells Binding.in human and rodent oral mucosa [) and this work has been Lectin specificity was examined (Table I) as described by Brabec et al [11).
Lectins and control reagents were bought from in a ll other aspects lectin binding did not differ with age or site of tissue.T-antigen expressions were measured by the enzyme-linked lectin assay (ELLA) with peanut agglutinin (PNA) in the sera of patients with squamous cell carcinoma (SCC) of the uterine cervix from patients.
This study has a sensitivity of 80%, specificity of Cited by: