Wyniki wyszukiwania - Biblioteka Nauki

1

Ostertagia circumcincta: surface and cuticular proteins and glycoproteins isolated by biotin-streptavidin affinity chromatography

100%

Wedrychowicz H.

Acta Parasitologica

|

1994

|

tom 39

|

nr 1

EN

Surface proteins and glycoproteins of ex- sheathed L3 (XL3), L4 and adults were identified by labelling live worms with NHS-SS-biotin which labels primary amine groups and biotin hydrazide (BH) which introduces biotin into sugar residues. After labelling and extensive washing, worms were homogenised in low-osmotic-strength buffer (TBS) and subjected to sequential extractions with SDS and SDS + 2-Me containing buffers. Labelled proteins released from the worms by these procedures were analysed by SDS-PAGE followed by Western blotting and probing with AP-streptavidin. Western blot analysis of biotinylated cuticular proteins from parasitic stages of O. circumcincta revealed stage specific differences in the labelling patterns of the cuticular proteins and glycoproteins. Developmental differences in cuticular components were apparent in the variety of MW of the components seen in Western blots although some components identified in Western blots appeared to be conserved (78 and 45 kDa). Two to six polypeptides were recognised in XL3 surface extracts by serum from sheep vaccinated with adult nematode somatic proteins. The surface of fourth stage larvae showed less cross-reactivity. Interestingly, the molecular weights of polypeptides recognised by anti-adult serum in streptavidin affinity isolated XL3 cuticular proteins were different from those recognised in adult cuticular proteins, which suggested that the cross-reacting epitopes were located on different proteins.

2

Translational regulation of pollen tube wall-specific glycoprotein

88%

Honys D. J. , Combe J. P.

Acta Biologica Cracoviensia. Series Botanica. Supplement

|

1999

|

tom 41

|

nr 1

3

Development of vaccinia virus recombinants expressing various glycoproteins of varicella-zoster virus

88%

Nemeckova S. , Maresova L. , Ludvikova V. , Hainz P. , Kutinova L.

Bulletin of the Veterinary Institute in Puławy

|

1998

|

tom 42

|

nr 1

4

Distribution of nonhistone proteins and glycoproteins in chromatin from larynx cancer

88%

Stepulak A. , Stryjecka-Zimmer M. , Sanecka-Obacz M.

|

nr 2

5

Diversity of the plasma membrane properties of transplantable hamster melanomas with regard to the expression of P-glycoprotein

88%

Kozlowska K. , Witkowski J. M. , Zarzeczna M. , Cichorek M.

Folia Histochemica et Cytobiologica

|

1999

|

tom 37

|

nr 3

6

Immunoreactive properties of pea protein extract and its trypsin hydrolysates

75%

Fraczek R. J. , Kostyra E. , Kostyra H. , Krawczuk S.

Journal of Animal and Feed Sciences

|

2007

|

tom 16

|

nr 3

472-484

7

Role of sulfation in the processing of gastric mucins

75%

Liau Y. H. , Murty V. L. N. , Slomiany A. , Bielanski W. , Slomiany B. L.

Journal of Physiology and Pharmacology

|

1991

|

tom 42

|

nr 4

EN

The role of sulfation in the processing of mucus glycoprotein in gastric mucosa was investigated. Rat gastric mucosal segments were incubated in MEM at various medium sulfate concentrations in the presence of [³⁵S]Na₂ SO₄ [³H] glucosamine and [³H]proline, with and without chlorate an inhibitor of PAPS formation. The results revealed that the mucin sulfation attained maximum at 300 µM medium sulfate concentration. Introduction of chlorate into the incubation medium, while having no effect on the protein synthesis as evidenced by [³H]proline incorporation, caused at its optimal concentration of 2 mM a 90% decrease in mucin sulfation and a 40% drop in mucin glycosylation. Evaluation of mucin molecular forms distribution indicated the predominance of the high molecular mucin form in the interacellular fraction and the low molecular mucin from in the extracellular fraction. Increase in medium sulfate caused an increase in the high molecular weight mucin form in both fractions, and this effect was inhibited by chlorate. Also, higher medium sulfate concentrations led to a higher degree of sulfation in the high molecular weight mucin form, the effect of which was inhibited by chlorate. The results suggest that the sulfation process is an early event taking place at the stage of mucin subunit assembly and is required for mucin polymer formation. Hence, the disturbances in mucin sulfation process could be determinal to the maintenance of gastric mucus coat integrity.

8

Targeting clusterin in prostate cancer

75%

Rizzi F. , Bettuzzi S.

|

tom 59

|

nr 9

265-274

9

Molecular structure and biological function of von Willebrand factor

75%

Bykowska E.

Acta Biochimica Polonica

|

2007

|

tom 54

|

nr Supplement 4

10

Subcellular localization of UDP-GlcNAc, UDP-Gal and SLC35B4 transporters

75%

Maszczak-Seneczko D. , Olczak T. , Olczak M.

Acta Biochimica Polonica

|

2011

|

tom 58

|

nr 3

EN

The mechanisms of transport and distribution of nucleotide sugars in the cell remain unclear. In an attempt to further characterize nucleotide sugar transporters (NSTs), we determined the subcellular localization of overexpressed epitope-tagged canine UDP-GlcNAc transporter, human UDP-Gal transporter splice variants (UGT1 and UGT2), and human SLC35B4 transporter splice variants (longer and shorter version) by indirect immunofluorescence using an experimental model of MDCK wild-type and MDCK-RCAr mutant cells. Our studies confirmed that the UDP-GlcNAc transporter was localized to the Golgi apparatus only and its localization was independent of the presence of endogenous UDP-Gal transporter. After overexpression of UGT1, the protein colocalized with the Golgi marker only. When UGT2 was overexpressed, the protein colocalized with the endoplasmic reticulum (ER) marker only. When UGT1 and UGT2 were overexpressed in parallel, UGT1 colocalized with the ER and Golgi markers and UGT2 with the ER marker only. This suggests that localization of the UDP-Gal transporter may depend on the presence of the partner splice variant. Our data suggest that proteins involved in nucleotide sugar transport may form heterodimeric complexes in the membrane, exhibiting different localization which depends on interacting protein partners. In contrast to previously published data, both splice variants of the SLC35B4 transporter were localized to the ER, independently of the presence of endogenous UDP-Gal transporter.

11

Cytokines and costimulatory molecules: positive and negative regulation of the immune response to Cryptococcus neoformans

75%

Vecchiarelli A.

Archivum Immunologiae et Therapiae Experimentalis

|

2000

|

tom 48

|

nr 6 Spec.Iss.

12

Serum glycoproteins in diabetic and non-diabetic patients with and without cataract

75%

Gul A. , Rahman A. M. , Ahmed N.

Optica Applicata

|

2008

|

tom Vol. 38, nr 3

531-538

EN

This study describes the changes in serum glycoproteins from type 2 diabetic and non-diabetic patients with and without cataract. A total of 85 subjects were selected for the study and divided into four groups. The first group consisted of 21 healthy subjects, the second group consisted of 21 diabetic patients with no chronic complications, the third group consisted of 20 diabetic patients with cataract, and the fourth group had 23 non-diabetic patients with age related cataract. The patients with and without cataract were selected on clinical grounds from the Ziauddin University and Jinnah Postgraduate Medical Centre in Karachi, Pakistan. As expected diabetic patients with and without cataract had significantly higher levels of fasting plasma glucose, glycated haemoglobin, glycated plasma proteins and serum fructosamine. In addition to these parameters, the levels of hexosamine, sialic acid and serum total protein were higher in diabetic compared to non-diabetic subjects with age related cataract and healthy subjects. Analysis of the protein fractions showed that alpha-1-globulins and alpha-2-globulins were higher in diabetic patients without complications compared to non-diabetic subjects with age related cataract and healthy subjects. Serum alpha-1-globulin, alpha-2-globulin, beta globulins and gamma globulins were all significantly higher in diabetic patients with cataract compared to healthy subjects but not serum albumin. In conclusion, the levels of beta globulins and gamma globulins were significantly higher in diabetic patients with cataract and non-diabetic age related patients with cataract compared to healthy subjects. Thus, mechanisms other than hyperglycaemia are responsible for the development of cataract in these patients.

13

The adjuvant activity of lactoferrin in the generation of DTH to ovalbumin can be inhibited by bovine serum albumin bearing alpha-D-mannopyranosyl residues

75%

Kocieba M. , Zimecki M. , Kruzel M. , Actor J.

Cellular and Molecular Biology Letters

|

2002

|

tom 07

|

nr 4

EN

Lactoferrin (LF) is an iron-binding glycoprotein present in the cytoplasmic granules of neutrophils and in external secretions of mammals. Although the biological role of human and bovine lactoferrin has been extensively studied, there is still uncertainty as to the nature and function of lactoferrin receptors. We recently determined that methyl-α-D-mannopyranoside given intraperitoneally (i.p.) could suppress the adjuvant activity of LF in the generation of delayed-type hypersensitivity (DTH) to ovalbumin (OVA). We concluded that the lactoferrin effects in DTH are mediated by carbohydrate-recognizing receptors like the mannose receptor (MR). This study indicates that subcutaneous (s.c.) administration of very small doses of the Man-bovine serum albumin (Man-BSA) complex, together with a sensitizing dose of the antigen, gives the same effects as i.p. administration of methyl-α-D-mannopyranoside. The latter is also a blocker of MR, although of a much lower affinity to the receptor than Man-BSA. The blocking of the adjuvant effect of LF by the Man-BSA complex (when given together with the sensitising dose of antigen) suggests that the function of antigen-presenting cells in the skin (presumably immature dendritic cells expressing MR) is inhibited. The results of our study indicate that a receptor with an affinity for mannose is essential for the mediation of adjuvant lactoferrin function in the generation of DTH.

14

The effects of glycoprotein modification on beta-adrenoreceptors binding ability in rat cardiac membranes

75%

Szymanski P. T.

Acta Physiologica Polonica

|

1987

|

tom 38

|

nr 6

15

Seminal plasma proteins as markers of biological value of boar semen

75%

Strzezek J. , Saiz-Cidoncha F. , Wysocki P. , Tyszkiewicz A. , Jastrzebski M.

Animal Science Papers and Reports

|

2002

|

tom 20

|

nr 4

16

Current techniques in protein glycosylation analysis. A guide to their application

75%

Merry T.

Acta Biochimica Polonica

|

1999

|

tom 46

|

nr 2

EN

The importance of glycosylation in biological events and the role it plays in glycoprotein function and structure is an area in which there is growing interest. In order to understand how glycosylation affects the shape or function of a protein it is however important to have suitable techniques available to obtain structural information on the oligosaccharides attached to the protein. For many years the complexity of the structures required sophisticated analytical techniques only available to a few specialist laboratories. In many cases these techniques were not available or required a large amount of material and therefore the number of glycoproteins which were fully characterised were relatively few. In recent years there have been substantial developments in the analysis of glycosylation which has significantly changed the capability to fully characterise molecules of biological interest. A number of different techniques are available which differ in terms of their complexity, the amount of information which is available from them, the skill needed to perform them and their cost. It is now possible for many laboratories who do not specialise in glycosylation analysis to obtain some information although this may be incomplete. These developments do, however, also make complete characterisation of a glycoprotein a much less daunting task and in many cases this can be performed more easily and with less starting material than was previously required. In this review a summary will be given of current techniques and their suitability for different types of analysis will be considered.

17

Three-dimensional structures of MHC class I-peptide complexes: implications for peptide recognition

75%

Persson K. , Schneider G.

Archivum Immunologiae et Therapiae Experimentalis

|

2000

|

tom 48

|

nr 3

18

Immunization of sheep with recombinant AG cells

75%

Rulka J. , Buzala E.

Bulletin of the Veterinary Institute in Puławy

|

1998

|

tom 42

|

nr 1

19

Proteomic mapping reveals developmental differences in secondary cell wall-specific glycoproteins in white lupin [Lupinus albus L.]

75%

Luczak M. , Marczak L. , Stobiecki M. , Wojtaszek P.

Cellular and Molecular Biology Letters

|

2002

|

tom 07

|

nr Suppl.

20

Schistosoma haematobium: cytochemistry of the Mehlis' gland and of the ootype wall

75%

Moczon T. , Swiderski Z.

Acta Parasitologica

|

2002

|

tom 47

|

nr 4

EN

Secretory granules produced by the Mehlis' gland and by the wall of the distal ootype in Schistosoma haematobium females, were examined at the ultrastructural level by means of several cytochemical methods. Strong staining, due to a relatively high percentage of carbohydrates in the granules, was observed in polymethacrylate sections treated with a phosphotungstic acidhydrochloric acid mixture at pH ≈ 0.5. Staining with ferric chloride-mixed-diamine mixtures (the LID and the HID reaction) showed no detectable level of oligosaccharide carboxyl and sulphate groups. A periodic acid-thiocarbohydrazide-silver proteinate reaction which was performed on epoxy sections, revealed a relatively high level of glycopyranosidic 1,2-diol groups in the granules. These results as well as the sensitivity of the secretory granules to the proteolytic action of papain indicated that the secretions produced by the Mehlis' gland and by the ootype wall were neutral glycoproteins.