Wyniki wyszukiwania - Biblioteka Nauki

1

Accumulation of collagen in ovarian benign tumours

100%

Wolańska M. , Sobolewski K. , Bańkowski E. , Drożdżewicz M.

Acta Biochimica Polonica

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1999

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tom 46

|

nr 4

941-947

EN

Extracellular matrix components of benign ovarian tumours (cystadenoma, adenofibroma, cystadenofibroma) were analysed. The investigated tumours contained twice as much collagen than control ovarian tissues. Significant alterations in mutual quantitative relationships between collagens of various types were observed. The proportion of type I collagen decreased and that of type III collagen increased. The accumulation of collagen was accompanied by a reduction in sulphated glycosaminoglycan content whereas the amount of hyaluronic acid was not changed. Dermatan sulphate was the most abundant glycosaminoglycan component. It is suggested that the accumulation of collagen (natural barrier to the migration of tumour cells) and underexpression of glycosaminoglycans/proteoglycans (binding some growth factors and interleukins) may exert an inhibitory effect on tumour growth.

2

Pre-eclampsia-associated alterations in Wharton's jelly proteoglycans

88%

Gogiel T. , Galewska Z. , Jaworski S.

Acta Biochimica Polonica

|

2005

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tom 52

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nr 2

EN

Proteoglycans of Wharton’s jelly contain mainly chondroitin/dermatan sulphate chains. The predominant proteoglycan is decorin (core proteins of 45 and 47 kDa), although the core proteins of biglycan (45 kDa), versican (260 kDa) and of other proteoglycans (90, 110, 220 kDa) were also detected (Gogiel et al., 2003). The aim of the present study was to compare the proteoglycan composition of Wharton’s jelly of newborns delivered by healthy mothers and those with pre-eclampsia. Proteoglycans from pre-eclamptic Wharton’s jelly had a higher sulphated glycosaminoglycan/protein ratio than those of normal tissue. Pre-eclampsia is associated with a lower level of all proteoglycan core proteins, especially those of higher molecular mass (such as versican), although the same set of core proteins were found in normal and pre-eclamptic Wharton’s jelly. The alterations in the proteoglycan composition of Wharton’s jelly may affect the mechanical properties of the umbilical cord and, in the case of pre-eclampsia, disturb foetal blood circulation.

3

Electrophoretic and chromatographic patterns of glycosaminoglycans of the umbilical cord vessels and their alteration in EPH-gestosis

88%

Romanowicz L. , Bankowski E. , Jaworski S.

Acta Biochimica Polonica

|

1998

|

tom 45

|

nr 3

EN

It was found that hyaluronic acid is the most abundant glycosaminoglycan (GAG) both in the umbilical cord arteries and in the umbilical cord veins. Chromatographic and as well as electrophoretic studies demonstrated that EPH-gestosis (Edema-Proteinuria-Hypertension), the most common pathological syndrome occurring in pregnancy, is accompanied by premature replacement of hyaluronic acid by sulphated GAGs in the investigated arteries but not in the veins. Such a replacement is a characteristic feature of the ageing process. One may conclude that EPH-gestosis is associated with a "premature ageing" of the umbilical cord arterial walls. The mechanism and possible role of this phenomenon in pathology are discussed.

4

Clinical significance of urinary glycosaminoglycan excretion in inflammatory bowel disease patients

75%

Derkacz A. , Olczyk P. , Jura-Poltorak A. , Waluga-Kozlowska E. , Olczyk K. , Komosinska-Vassev K.

Journal of Physiology and Pharmacology

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2020

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tom 71

|

nr 6

5

Protein-bound glycosaminoglycans in serum of patients with lung cancer and patients with diabetes mellitus

75%

Olczyk K. , Kucharz E. J. , Glowacki A. , Sonecki P. , Koscielniak-Kocurek E.

Acta Biochimica Polonica

|

1992

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tom 39

|

nr 1

6

Glycosaminoglycans of normal and scarred fascia

75%

Glowacki A. , Olczyk K. , Sonecki P. , Kozma E. , Najmiec T.

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nr 2

7

Insulin influence on glycosaminoglycan synthesis in diabetic [IDDM] fibroblasts

75%

Yevdokimova N.

Folia Histochemica et Cytobiologica. Supplement

|

1997

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tom 35

|

nr 2

8

Accumulation of collagen in ovarian benign tumours

75%

Wolanska M. , Sobolewski K. , Bankowski E. , Drozdzewicz M.

|

nr 4

EN

Extracellular matrix components of benign ovarian tumours (cystadenoma, adenofibroma, cystadenofibroma) were analysed. The investigated tumours contained twice as much collagen than control ovarian tissues. Significant alterations in mutual quantitative relationships between collagens of various types were observed. The proportion of type I collagen decreased and that of type III collagen increased. The accumulation of collagen was accompanied by a reduction in sulphated glycosaminoglycan content whereas the amount of hyaluronic acid was not changed. Dermatan sulphate was the most abundant glycosaminoglycan component. It is suggested that the accumulation of collagen (natural barrier to the migration of tumour cells) and underexpression of glycosaminoglycans/proteoglycans (binding some growth factors and interleukins) may exert an inhibitory effect on tumour growth.

9

Proteoglycans of human umbilical cord arteries

75%

Gogiel T. , Jaworski S.

Acta Biochimica Polonica

|

2000

|

tom 47

|

nr 4

EN

Proteoglycans (PGs) were dissociatively extracted from human umbilical cord arteries (UCAs) with 4 M guanidine hydrochloride containing Triton X-100 and protease inhibitors, purified by Q-Sepharose anion exchange chromatography and lyophilized. They were analysed by gel filtration, SDS/PAGE and agarose gel electrophoresis before and after treatment with chondroitinase ABC. It was found that the PG preparation was especially enriched in chondroitin/dermatan sulphate PGs. The predominant PG fraction included small PGs that emerged from Sepharose CL-2B with Kav = 0.74. Their molecular mass, estimated by SDS/PAGE, was 160-200 kDa and 90-150 kDa, i.e. it was typical for biglycan and decorin, respectively. Treatment with chondroitinase ABC yielded the core proteins of 45 and 47 kDa, characteristic for both small PGs. Remarkable amounts of the 45 kDa protein were detected in non-treated PG samples, suggesting the presence of free core proteins of biglycan and decorin. Large PGs were present in lower amounts. In intact form they were eluted from Sepharose CL-2B with Kav = 0.17 and 0.43. Digestion with chondroitinase ABC yielded the core proteins with a molecular mass within the range of 180-360 kDa but predominant were the bands of 200, 250 and 360 kDa. The large PGs probably represent various forms of versican or perlecan bearing chondroitin sulphate chains.

10

Glycosaminoglycans of human serum and their alterations in diabetes mellitus

75%

Kozma E. M. , Olczyk K. , Glowacki A. , Komosinska K. , Sonecki P. , Najmiec T. , Jazwiec M.

Acta Biochimica Polonica

|

1996

|

tom 43

|

nr 3

EN

Human serum contains several glycosaminoglycans (GAGs), mainly chondroitin sulphates and significantly less of heparan sulphate + heparin and dermatan sulphate. The non-insulin-dependent diabetes mellitus (with vascular complications) was associated with a significant increase in total serum GAG concentration, mainly of chondroitin sulphates and dermatan sulphate, with a simultaneous decrease in heparan sulphate + heparin level. These alterations were much more evident in patients with poor metabolic control. Hyaluronic acid (undetectable in healthy subjects and in patients with good metabolic control) appeared only in trace amounts in poorly controlled diabetic individuals. The obtained data allow to conclude that the diabetes mellitus-associated disturbances in tissue GAG metabolism lead to significant alterations in serum GAG composition.

11

Surface modified liposomes by coating with charged hydrophilic molecules

75%

Sagrista M. L. , Mora M. , De Madariaga M. A.

Cellular and Molecular Biology Letters

|

2000

|

tom 05

|

nr 1

EN

The design of liposomes with a hydrophilic/steric barrier at their bilayer surface allows the modification of their pharmacokinetics and reduces the uptake by the RES. Liposomes can be coated by hydrophilic molecules such as polysaccharides, which disguise the vesicle surface by creating a three-dimensional matrix near them and prevent the binding of plasma proteins and their recognition by some cellular receptors. All these considerations, and previous results obtained in our laboratory showing the formation of stable GAG-liposome complexes, have lead us to think about the use of the negatively charged glycosaminoglycans (GAGs), alternately to other molecules such as the monosialoganglioside GM1, more expensive, or polyethylene glycol (PEG-PE) that can disturb the structural organization of the bilayer. The present paper describes the effect of the incorporation of GAGs to phospholipid vesicles, in relation to their electrical and permeability properties. The results obtained show that there is an effective coating of the bilayer surface when glycosaminoglycans are added to liposome suspensions. The shielding of the negative surface charge by the neutral hyaluronic acid, in the absence of calcium, and the increase in the negative charge when the negative polyelectrolytes chondroitin sulfate, heparin or dextran sulfate are added to calcium-containing liposome suspensions account for the formation of stable liposome-GAG complexes. Moreover, the reduced permeability of the GAG-coated liposomes points out on their ability to hold encapsulated drugs and, so, their potential usefulness as drug-sustained release carriers. The hydrophilic coating will give to these liposomal carriers long-circulating properties.

12

Role of cathepsin A and cathepsin C in the regulation of glycosidase activity

63%

Minarowska A. , Minarowski L. , Karwowska A. , Milewska A. J. , Gacko M.

Folia Histochemica et Cytobiologica

|

2012

|

tom 50

|

nr 1

13

Melatonin-induced glycosaminoglycans augmentation in myocardium remote to infarction

63%

Drobnik J. , Tosik D. , Piera L. , Szczepanowska A. , Olczak S. , Zielinska A. , Liberski P. P. , Ciosek J.

Journal of Physiology and Pharmacology

|

2013

|

tom 64

|

nr 6

14

Are chondroclasts and osteoclasts identical?

63%

Wlodarski K. H. , Brodzikowska A. , Kuzaka B.

Folia Biologica

|

2014

|

tom 62

|

nr 2

15

Cytochemical characterization of mucosubstances in the chick glandular stomach during embryonary and postnatal development

63%

Altamirano F. , Avila R. , Samar M. E. , De Fabro S. P.

Folia Histochemica et Cytobiologica

|

1984

|

tom 22

|

nr 2

16

Isoenzymes of N-acetyl-beta-hexosaminidase

63%

Zwierz K. , Zalewska A. , Zoch-Zwierz W.

Acta Biochimica Polonica

|

1999

|

tom 46

|

nr 3

EN

Biological significance, structure and posttranslational processing of N-acetyl-β-hexosaminidase isoenzymes are described. Clinical application of N-acetyl-β-hexosaminidase is also reviewed.

17

Alterations in glycosaminoglycans in wounded skin of diabetic rats. A possible role of IGF-I, IGF-binding proteins and proteolitic activity

63%

Cechowska-Pasko M. , Palka J. , Bankowski E.

Acta Biochimica Polonica

|

1996

|

tom 43

|

nr 3

EN

In the skin of diabetic animal tissues the amount of extracellular matrix (ECM) components is drastically decreased as a result of a reduced rate of their biosynthesis or increased degradation. In the present study we have investigated the mechanism of poor wound healing in diabetic rats. We have found that wounded skin of diabetic rats shows a significant decrease in glycosaminoglycan (GAG) content compared to that of control animals. This decrease was accompanied by significant depletion of insulin-like growth factor-I (IGF-I), known as a stimulator of GAG biosynthesis, and a distinct decrease in the content of high molecular weight IGF-binding proteins (HMW-BPs) with a simultaneous increase in low molecular weight IGF-binding proteins (LMW-BPs) in the sera of diabetic animals. Basing on determination of proteolytic activities we suggest that insulin shortage in diabetes results in increased proteolytic activity in various tissues. Proteolytic enzymes may cleave the HMW-BPs and convert them to LMW-BPs. The LMW-BPs may inactivate IGF-I and eliminate its stimulatory effects on GAG biosynthesis. The proteolytic enzymes may also digest the protein cores of proteoglycans releasing the GAGs and making them more susceptible to the action of glycosidases. These phenomena may be responsible for the observed marked decrease in GAG content in the skin of diabetic rats and disturb the wound-healing process.

18

Effects of wheat germ agglutinin and concanavalin A on the accumulation of glycosaminoglycans in pericellular matrix of human dermal fibroblasts. A comparison with insulin

63%

Yevdokimova N. Y. , Yefimov A. S.

Acta Biochimica Polonica

|

2001

|

tom 48

|

nr 2

EN

The ef fect of in su lin, wheat aerm ag glu ti nin (WGA), pea nut ag glu ti nin (PNA) and concanavalin A (ConA) on [ 3H]glucosamine incorporation into pericellular glycosaminoglycans (GAGs) was investigated in two lines of cultured human dermal fibroblasts. Insulin and WGA stimulated [3H]glucosamine incorporation into hyaluronic acid (HA) and heparan sul phate (HS) with out any al ter ation of chondroitin sulphate (CS) and dermatan sul phate (DS) con tents. ConA in creased [ 3H]glucosamine in- cor po ra tion into HS, CS and DS, but had no ef fect on [ 3H]glucosamine in cor po ra tion into HA. PNA af fected nei ther the con tent, nor the com po si tion of GAGs. In con trast to PNA, ConA and WGA stimulated glycolysis and demonstrated an evident antiproliferative ef fect on der mal fibroblasts. Thus, both the in su lin-like ac tion of WGA and ConA on cul tured der mal fibroblasts and the dif fer ences be tween the ef fects of lectins on mod u la tion of GAGs syn the sis ap pear to be de ter mined by their chem i cal structure.

19

Heparin- and Zn2plus -binding proteins from boar seminal plasma

63%

Holody D. , Strzezek J.

|

nr 4

EN

Low molecular mass, heparin-binding proteins from seminal plasma play an important role in gametes interaction whereas plasmatic Zn2+-binding proteins stabilize chromatin and plasmalemma structures and protect spermatozoa in the female reproductive tract. By means of affinity chromatography the heparin- and Zn2+-binding proteins were isolated from boar seminal plasma and both preparations were analyzed by reverse HPLC. Most of the proteins bound to heparine and Zn2+-ions were classified as spermadhesins. Three fractions binding exclusively Zn2+ were isolated. They differ in amino-acid composition, content of glucosamine and content of protein components revealed by SDS/PAGE.

20

Differential binding of hyaluronan on the surface of tissue-specific endothelial cell lines

63%

Szczepanek K. , Kieda C. , Cichy J.

Acta Biochimica Polonica

|

2008

|

tom 55

|

nr 1

EN

Tissue-specific heterogeneity of endothelial cells, both structural and functional, plays a crucial role in physiologic as well as pathologic processes, including inflammation, autoimmune diseases and tumor metastasis. This heterogeneity primarily results from the differential expression of adhesion molecules that are involved in the interactions between endothelium and circulating immune cells or disseminating tumor cells. Among these molecules present on endothelial cells is hyaluronan (HA), a glycosaminoglycan that contributes to primary (rolling) interactions through binding to its main receptor CD44 expressed on leukocytes and tumor cells. While the regulation of CD44 expression and function on either leukocytes or tumor cells has been well characterized, much less is known about the ability of endothelial cells to express HA on their surface. Therefore, in these studies we analyzed HA levels on tissue-specific endothelium. We used endothelial cell lines of different origin, including lung, skin, gut and lymph nodes that had been established previously as model lines to study interactions between the endothelium and leukocytes/tumor cells. Our results indicate that HA is accumulated on the surface of all endothelial cells examined. Moreover, retention of endogenous HA differs between the lines and may depend on their tissue origin. Analysis of binding of exogenous HA reveals the presence of specific HA binding sites on all endothelial cell lines tested. However, the retention of endogenous HA and the binding of exogenous HA is mediated through a CD44-independent mechanism.