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  1. 26 Acta Biochimica Polonica
  2. 26 Engineering of Biomaterials
  3. 13 Folia Histochemica et Cytobiologica
  4. 13 Journal of Physiology and Pharmacology
  5. 5 Acta of Bioengineering and Biomechanics
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  1. 1 2023
  2. 3 2022
  3. 6 2021
  4. 3 2020
  5. 15 2019
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  1. 18 Sionkowska A.
  2. 8 Bankowski E.
  3. 7 Kwiatkowska A.
  4. 6 Bajek A.
  5. 6 Galicka A.
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1
Content available remote A novel Gly to Arg substitution at position 388 of the α1 chain of type I collagen in lethal form of osteogenesis imperfecta.
100%
Galicka A. , Wolczynski S. , Lesniewicz R. , Chyczewski L. , Gindzienski A.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 2
443-450
EN
Cultured skin fibroblasts from a proband with a lethal form of osteogenesis imperfecta produce two forms of type I collagen chains, with normal and delayed electrophoretic migration; collagen of the proband's mother was normal. Peptide mapping experiments localized the structural defect in the proband to α1(I) CB8 peptide in which residues 123 to 402 are spaned. Direct sequencing of amplified cDNA covering this region revealed a G to A single base change in one allele of the α1(I) chain, that converted glycine 388 to arginine. Restriction enzyme digestion of the RT-PCR product was consistent with a heterozygous COL1A1 mutation. The novel mutation conforms to the linear gradient of clinical severity for the α1(I) chain and results in reduced thermal stability by 3°C and intracellular retention of abnormal molecules.
2
Content available remote Accumulation of collagen in ovarian benign tumours
80%
Wolańska M. , Sobolewski K. , Bańkowski E. , Drożdżewicz M.
Acta Biochimica Polonica
|
1999
|
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.
3
Content available remote Effect of cadmium on collagen content and solubility in rat bone.
80%
Galicka A. , Brzóska M. M. , Średzińska K. , Gindzienski A.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 3
825-829
EN
The toxic action of cadmium in the bone tissue is known, but its mechanisms are still unexplained. We examined whether Cd influences collagen content and its solubility in the femoral bone of three-week-old female rats exposed to 5 or 50 mg Cd/l in drinking water. Non-cross linked collagen was extracted with 0.5 M acetic acid, and two acid-insoluble collagen fractions were extracted with pepsin and 4.0 M guanidine hydrochloride, respectively. SDS/PAGE showed the presence of two collagen types, I and V, in all three extracted fractions. Exposure of rats to Cd for 6 months increased the amount of acid-soluble collagens type I and V and decreased the level of acid-insoluble collagens. The amount of total collagen extracted from the bones of rats exposed to 50 mg Cd/l was reduced by about 14% as compared to control and those intoxicated with 5 mg Cd/l. The solubility of type I bone collagen (determined as the percentage of acetic-soluble fraction of total collagen) was increased 2.9- and 3.0-fold in rats intoxicated with 5 and 50 mg Cd/l, respectively. Similarly, the solubility of type V collagen was increased 2.3- and 2.7-fold, respectively. Our results indicate that Cd treatment affects bone collagen by decreasing its content and increasing its solubility.
4
Content available The properties of collagen/chitosan porous matrices in the presence of small amount of poly(ethylene)glycol
80%
Kozłowska J. , Sionkowska A.
Engineering of Biomaterials
|
2016
|
tom Vol. 19, no. 138 spec. iss.
46
5
Content available Collagen, silk fibroin and chitosan based materials for biomedical and cosmetic applications
80%
Sionkowska A. , Grabska S.
Engineering of Biomaterials
|
2018
|
tom Vol. 21, no. 148
23
6
Content available The in vitro analysis of scaffolds with glycosaminoglycans addition
80%
Kaczmarek B. , Sionkowska A. , Łukowicz K. , Osyczka A. M. , Unrod V.
Engineering of Biomaterials
|
2018
|
tom Vol. 21, no. 148
28
7
Content available remote Collagen of umbilical cord vein and its alterations in pre-eclampsia.
80%
Romanowicz L. , Jaworski S.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 2
451-458
EN
The state of the vascular system of the mother and of placenta is known to exert a great influence on intrauterinal development of the fetus. Pre-eclampsia is the most common pathological syndrome connected with pregnancy. Since collagen is one of the main constituents of the vessel wall a comparison was made with collagen content and its molecular polymorphism in umbilical cord veins of newborns from healthy and pre-eclamptic mothers. It was found that umbilical cord veins of newborns from mothers with pre-eclampsia contained 18% less collagen than those of the newborns from normal pregnancies. This decrease was accompanied by a slight decrease of collagen solubility, but all its types (I, III, IV, V and VI) were present. However, the umbilical vein wall of newborns from mothers with pre-eclampsia contained relatively less of type I and more of type III collagen than the normal umbilical cord. These differences may be connected with a disturbance of blood flow in fetus of a woman with pre-eclampsia.
8
Content available remote The Variants Within the COL5A1 Gene are Associated with Reduced Risk of Anterior Cruciate Ligament Injury in Skiers
80%
Stępień-Słodkowska M. , Ficek K. , Kaczmarczyk M. , Maciejewska-Karłowska A. , Sawczuk M. , Leońska-Duniec A. , Stępiński M. , Ziętek P. , Król P. , Chudecka M. , Cięszczyk P.
Journal of Human Kinetics
|
2015
|
tom 45
|
nr 1
103-111
EN
The purpose of this study was to examine the association of the BstUI RFLP C/T (rs 12722) and DpnII RFLP C/T (rs 13946) COL5A1 polymorphisms, individually and as haplotypes, with anterior cruciate ligament ruptures in recreational skiers. Subjects were 138 male recreational skiers with surgically diagnosed primary anterior cruciate ligament ruptures. The control group consisted of 183 apparently healthy male recreational skiers, who were without any self-reported history of ligament or tendon injury. DNA was extracted from buccal cells donated by the subjects and genotyping was carried out using real-time PCR. The genotype distributions for both polymorphisms met Hardy- Weinberg expectations in both groups. There were no significant differences in genotype distribution of allele frequencies of COL5A1 BstUI RFLP C/T and COL5A1 DpnII RFLP C/T polymorphisms between the ACL rupture and control groups. The T-T (BstUI RFLP T, DpnII RFLP T) haplotype was the most common (55.6%). The haplotype T-C was not present in any of the subjects. There was an underrepresentation tendency of the C-T haplotype in the study group compared to controls under recessive mode of inheritance. Higher frequency of the COL5A1 BstUI RFLP C/T and COL5A1DpnII RFLP C/T polymorphisms haplotype is associated with reduced risk of anterior cruciate ligament injury in a group of apparently healthy male recreational skiers.
9
Content available Resorbable scaffolds modified with collagen type I or hydroxyapatite: in vivo studies on rabbits
80%
Pamuła E. , Orzelski M. , Malisz P. , Rumian Ł. , Menaszek E. , Nowak B. , Dobrzyński P. , Silmanowicz P.
Engineering of Biomaterials
|
2012
|
tom Vol. 15, no. 116-117 spec. iss.
115--117
10
Content available remote Utylizacja kolagenu z odpadów skór garbowanych
80%
Przepiórkowska A. , Stańczak M.
Przemysł Chemiczny
|
2003
|
tom T. 82, nr 8-9
1146-1148
PL
Dokonano przeglądu metod utylizacji odpadów skór nie garbowanych i garbowanych. Zagospodarowanie odpadów nie garbowanych jest względnie proste. Natomiast utylizacja odpadów garbowanych, które ze względu na 3–5-proc. zawartości soli chromu(III) należą do grupy odpadów szczególnie niebezpiecznych dla środowiska naturalnego, jest rozwiązana tylko w niewielkim stopniu.
XX
A review with 34 refs. covering utilization of untanned and tanned leather waste materials, recovery of collagen from chrome-tanned wastes and its use as a filler for isoprene rubber mixes.
11
Content available remote Novel antibacterial bioactive glass nanocomposite functionalized with tetracycline hydrochloride
80%
Rivadeneira J. , Luz G. M. , Audisio M. C. , Mano J. F. , Gorustovich A. A.
Biomedical glasses
|
2015
|
tom 1
|
nr 1
EN
To prevent the high frequency of wound infections, anti-bacterial agents can be loaded onto composites. In the present study, the antibiotic tetracycline hydrochloride (TC)was incorporated, for the first time, in collagen type I membranes coated with nano-sized SiO2-CaOP2O5 bioactive glass (n-BG) obtained by a sol-gel chemical route. Collagen membranes coated with n-BG were immersed in simulated body fluid (SBF) containing 0.25, 0.75 or 1.25 mg mL−1 of TC for 48 h at 37∘C following a coprecipitation method. The antibiotic was released in distilledwater at 37∘C for up to 72 h. The antibacterial activity of the composites was evaluated in vitro by the inhibition zone test and plate count method. Two different Staphylococcus aureus strains, S. aureus ATCC29213 and S. aureus ATCC25923, were exposed to the biomaterials. The results showed that the incorporation but not the release of TC was dependent on the initial concentration of TC in SBF. The biomaterials inhibited S. aureus growth, although the efficacy was similar for all the concentrations. The results allow us to conclude that the new composite could have potential in the prevention of wound infections.
12
Content available Zawartość kolagenu w mięśniach tylnej ćwierćtuszy wołowej
80%
Dąbrowska E. , Jankowska B. , Kwiatkowska A. , Cierach M.
Inżynieria i Aparatura Chemiczna
|
2011
|
tom Nr 3
18-19
PL
Określono zawartość kolagenu w głównych mięśniach ćwierćtuszy wołowej otrzymanej w wyniku towarowego krzyżowania bydła mlecznego i mięsnego. Wykazano, że mięśnie, z których pozyskuje się mięso kulinarne charakteryzują się niską zawartością kolagenu. Zawartość badanego białka w mięśniu prostowniku palców pozyskanym z bydła uzyskanego na drodze krzyżowania towarowego była z kolei dwukrotnie wyższa niż w mięśniach pochodzących z tusz typowego bydła mięsnego.
EN
The collagen content in main muscles of beef quarter-carcass of an anim; received in cross-breeding of dairy and beef cattle was determined. It wi shown, that the collagen content in muscles from which culinary meat wi gained over was low. The collagen content in a finger extensor muscle froi the cross-breeding carcass was two times higher compared with typical bei carcasses.
13
Content available STRUCTURAL RESEARCH OF THERMOSENSITIVE CHITOSAN-COLLAGEN GELS CONTAINING ALP
80%
Skwarczyńska A. , Biniaś D. , Modrzejewska Z.
Progress on Chemistry and Application of Chitin and its Derivatives
|
2016
|
tom 21
176-186
EN
Introducing collagen, which is basic ingredient of bone tissue, into the structure of chitosan gels which are formed at the physiological body temperature, is aimed at creating the so-called biomimetic structures, i.e. close in their composition to the natural composition of bone tissue. Within the research the influence of collagen on structural properties of thermosensitive chitosan gels and the influence of ALP on structural properties of chitosan and chitosan-collagen gels was determined.
14
Content available Cyclodextrines as an modifying agent for protein matrices
80%
Skopińska-Wiśniewska J. , Kozlowska J. , Bajek A. , Sionkowska A.
Engineering of Biomaterials
|
2018
|
tom Vol. 21, no. 148
85
15
Content available Composite collagen-calcium phosphate hydrogels for bone substitution
80%
Douglas T. E. L. , Gkioni C. , Jansen J. A. , Leeuwenburgh S. C. G.
Engineering of Biomaterials
|
2009
|
tom Vol. 12, no. 89-91
28--29
16
Content available remote Glutathione reductase activity correlates with concentration of extracellular matrix degradation products in synovial fluid from patients with joint diseases
80%
Średzińska K. , Galicka A. , Porowska H. , Średziński Ł. , Porowski T. , Popko J.
Acta Biochimica Polonica
|
2009
|
tom 56
|
nr 4
635-640
EN
The mechanisms underlying cartilage matrix degradation in joint diseases is not fully understood but reactive oxygen species are implicated as main causative factors. Comparative studies of glutathione reductase (GR) activity in synovial fluid from patients with rheumatoid arthritis (RA), reactive arthritis (ReA) and osteoarthritis (OA) as well as correlations between GR activity and concentration of the major cartilage components in synovial fluid are presented in this study. We found significantly higher activity of GR in RA (about three-fold) and ReA (about two-fold) than in OA. In RA and ReA patients, GR activity in synovial fluid correlates negatively with the concentrations of collagen and degradation products of sulfated glycosaminoglycans. In OA patients the activity of GR was significantly lower than in RA and ReA, which positively correlated with the concentration of collagen and showed a tendency for positive correlation with the degradation products of sulfated glycosaminoglycans. Our results suggest that in RA and ReA patients increased activity of GR does not prevent the increased degradation of collagen and proteoglycans by ROS.
17
Content available In vitro study of a novel collagen – calcium phosphate composites
80%
Kozłowska J. , Sionkowska A. , Bajek A. , Rynkiewicz A.
Engineering of Biomaterials
|
2014
|
tom Vol. 17, no. 128-129
85
18
Content available remote Percolation thresholds in temperature dependence of electric conductivity of collagen films
80%
Gauza M. , Kubisz L.
Polish Journal of Medical Physics And Engineering
|
2009
|
tom 15
|
nr 4
183-191
EN
Temperature measurement of electrical conductivity s were carried out from 395 to 543 K. The obtained dependence indicates an increase in s. The temperature dependence of the electrical conductivity allowed to observe the release of the free water, bound water and structural water. Studies on electric conductivity of collagen indicate the occurrence of percolation threshold, which comprises free release of water and change its properties from semiconducting to dielectric one.
19
Content available The influence of collagen from various sources on skin parameters
80%
Prus W. , Kozłowska J.
Engineering of Biomaterials
|
2018
|
tom Vol. 21, no. 148
49
20
Content available Selection of active fragments of collagen
80%
Kolesińska B. , Frączyk J. , Kamński Z. J. , Rosiak P. , Becht A. , Czerchawy A. , Chaberska A. , Waśko J. , Czerczak K. , Walczak M. E.
Engineering of Biomaterials
|
2018
|
tom Vol. 21, no. 148
41
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