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Wyszukujesz frazę "collagen type I" wg kryterium: Temat


Wyświetlanie 1-7 z 7
Tytuł:
Molecular studies in osteogenesis imperfecta [OI] I. Clinical analysis of patients with osteogenesis imperfecta
Autorzy:
Pietrzyk, J J
Kruczek, A.
Kostyk, E.
Sucharski, P.
Piatkowska, E.
Powiązania:
https://bibliotekanauki.pl/articles/2044210.pdf
Data publikacji:
1998
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
disease
collagen protein
clinical classification
collagen type I
collagen synthesis
mutation
diagnostic method
osteogenesis imperfecta
Opis:
The goal of this study is to develop optimal diagnostic methods for osteogenesis imperfecta (OI), which will allow to distinguish familial from spontaneous cases and can be used in prenatal diagnostics as well. The paper summarizes the clinical part of the study, in which 69 families were analyzed. The families with OI were registered, their pedigrees were studied, a clinical classification of the disease was carried out and the dermatoglyphics of the affected patients were analyzed. Based on the above results a diagnostic algorithm was elaborated.
Źródło:
Journal of Applied Genetics; 1998, 39, 4; 331-348
1234-1983
Pojawia się w:
Journal of Applied Genetics
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Studies on type I collagen in skin fibroblasts cultured from twins with lethal osteogenesis imperfecta.
Autorzy:
Galicka, Anna
Wołczyński, Sławomir
Gindzieński, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1043625.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
osteogenesis imperfecta
type I collagen
Opis:
Studies on type I procollagen produced by skin fibroblasts cultured from twins with lethal type II of osteogenesis imperfecta (OI) showed that biosynthesis of collagen (measured by L-[5-3H]proline incorporation into proteins susceptible to the action of bacterial collagenase) was slightly increased as compared to the control healthy infant. SDS/PAGE showed that the fibroblasts synthesized and secreted only normal type I procollagen. Electrophoretic analysis of collagen chains and CNBr peptides showed the same pattern of electrophoretic migration as in the controls. The lack of posttranslational overmodification of the collagen molecule suggested a molecular defect near the amino terminus of the collagen helix. Digestion of OI type I collagen with trypsin at 30°C for 5 min generated a shorter than normal α2 chain which melted at 36°C. Direct sequencing of an asymmetric PCR product revealed a heterozygous single nucleotide change C→G causing a substitution of histidine by aspartic acid in the α2 chain at position 92. Pericellular processing of type I procollagen by the twin's fibroblasts yielded a later appearance of the intermediate pC-α1(I) form as compared with control cells.
Źródło:
Acta Biochimica Polonica; 2003, 50, 2; 481-488
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Mutations in type I collagen genes resulting in osteogenesis imperfecta in humans.
Autorzy:
Gajko-Galicka, Anna
Powiązania:
https://bibliotekanauki.pl/articles/1043782.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
osteogenesis imperfecta
type I collagen
mutation
Opis:
Osteogenesis imperfecta (OI), commonly known as "brittle bone disease", is a dominant autosomal disorder characterized by bone fragility and abnormalities of connective tissue. Biochemical and molecular genetic studies have shown that the vast majority of affected individuals have mutations in either the COL1A1 or COL1A2 genes that encode the chains of type I procollagen. OI is associated with a wide spectrum of phenotypes varying from mild to severe and lethal conditions. The mild forms are usually caused by mutations which inactivate one allele of COL1A1 gene and result in a reduced amount of normal type I collagen, while the severe and lethal forms result from dominant negative mutations in COL1A1 or COL1A2 which produce structural defects in the collagen molecule. The most common mutations are substitutions of glycine residues, which are crucial to formation and function of the collagen triple helix, by larger amino acids. Although type I collagen is the major structural protein of both bone and skin, the mutations in type I collagen genes cause a bone disease. Some reports showed that the mutant collagen can be expressed differently in bone and in skin. Since most mutations identified in OI are dominant negative, the gene therapy requires a fundamentally different approach from that used for genetic-recessive disorders. The antisense therapy, by reducing the expression of mutant genes, is able to change a structural mutation into a null mutation, and thus convert severe forms of the disease into mild OI type I.
Źródło:
Acta Biochimica Polonica; 2002, 49, 2; 433-441
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
mRNA expressions MMP-2 and MMP-9 as potential molecular markers for distinguishing the boundary between tumour and normal tissue in basal cell carcinoma
mRNA dla MMP-2 i MMP-9 jako potencjalne markery molekularne pozwalające na rozróżnienie granicy między guzem a tkanką prawidłową w przypadku raka BCC
Autorzy:
Goździalska, Anna
Pasek, Małgorzata
Jochymek, Małgorzata
Goździalska, Magdalena
Powiązania:
https://bibliotekanauki.pl/articles/2129676.pdf
Data publikacji:
2022
Wydawca:
Krakowska Akademia im. Andrzeja Frycza Modrzewskiego
Tematy:
BCC
MMPs
molecular markers
collagen type I and IV
markery molekularne
kolagen typu I i IV
MMP
Opis:
Introduction: Non-melanoma skin cancers (NMSC) are the most common malignant neoplasms, the number of which continues to increase. BCC is characterized by slow growth, its main clinical feature being that it infiltrates adjacent tissues and destroys adjacent structures. Material and methods: The expression of mRNA transcripts for collagen types I, IV and MMP-2 and MMP-9 were compared in skin biopsies from patients with BCC of the skin and in the biopsies of healthy skin from the tumour margin. The study involved seventy patients diagnosed with BCC. Results: The differences between mRNA expressions for MMP-2 and MMP-9, type I collagen and type IV collagen were investigated in nodular and infiltrative BCC both in tumour tissue samples and normal tissue samples taken from the tumour margins of the same patients. Conclusions: Significantly higher levels of mRNA expressions for type I collagen, MMP-2 and MMP-9, as well as consistently lower levels of mRNA expression for type IV collagen in tumour tissue compared to tumour margin tissue obtained from the same patients, were identified in both types of BCC. These differences indicate a different role for collagen I and collagen IV in the pathomechanism of BCC.
Wprowadzenie: Nieczerniakowe nowotwory skóry (NMSC) są najczęstszymi nowotworami złośliwymi, których liczba stale rośnie. BCC charakteryzuje się powolnym wzrostem, a główną cechą kliniczną tego guza jest naciekanie okolicznych tkanek i niszczenie sąsiadujących struktur. Materiał i metody: Ekspresję transkryptów mRNA dla kolagenu typu I i IV oraz MMP-2 i MMP-9 porównano w biopsjach skóry od pacjentów z BCC skóry oraz w biopsjach zdrowej skóry z marginesu guza. W badaniu wzięło udział 70 pacjentów, u których zdiagnozowano BCC. Wyniki: Stwierdzono różnice między ekspresją mRNA dla MMP-2 i MMP-9, kolagenu typu I i IV w BCC guzkowym i naciekowym w próbkach tkanek nowotworowych i tkanek prawidłowych pobranych z marginesów guza tych samych pacjentów. Wnioski: Istotnie wyższe poziomy ekspresji mRNA dla kolagenu typu I, MMP-2 i MMP-9, a także zawsze niższe poziomy ekspresji mRNA dla kolagenu typu IV w tkance nowotworowej w porównaniu z tkanką marginesu guza uzyskaną od tych samych pacjentów wykazano w obu typach BCC. Postrzegane różnice wskazują na inną rolę kolagenu I i kolagenu IV w patomechanizmie BCC.
Źródło:
Państwo i Społeczeństwo; 2022, 1; 35-53
1643-8299
2451-0858
Pojawia się w:
Państwo i Społeczeństwo
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Coating of poly(l-lactide-co-glycolide) scaffolds with collagen/glycosaminoglycan matrices and their effects on osteoblast behaviour
Autorzy:
Wojak, I.
Pamuła, E.
Dobrzyński, P.
Zimmermann, H.
Worch, H.
Scharnweber, D.
Hintze, V.
Powiązania:
https://bibliotekanauki.pl/articles/284646.pdf
Data publikacji:
2009
Wydawca:
Akademia Górniczo-Hutnicza im. Stanisława Staszica w Krakowie. Polskie Towarzystwo Biominerałów
Tematy:
skaffoldy
kolagen
osteoblasty
poly(L-lactide-co-glycolide)
scaffolds
collagen type I
glycosaminoglycans
hyaluronan
chondroitin sulfate
osteoblasts
Opis:
Collagen type I and glycosaminoglycans (GAGs) were immobilized on the surfaces of two types of porous biodegradable poly(L-lactide-co-glycolide) (PLGA) scaffolds with pore size in the range of 250-320 µm and 400-600 µm. Two methods of coating were evaluated differing in the way of how the fibrillogenesis solution was introduced into the pores. The distribution of the immunostained collagen in the volume of the scaffolds was analysed with a laser confocal microscope (LSM). The total amount of collagen and GAGs was measured by Sirius Red and Toluidine Blue assays, respectively. The potential of the scaffolds for cell colonization and differentiation was tested in a dynamic cell culture system using human osteosarcoma cells (SAOS-2). The proliferation of SAOS-2 cells was measured by determining the DNA content on days 2 and 7, while differentiation was analyzed by Calcium- and Phosphate-Assays on days 7 and 14. Differentiation of cells was improved by increasing the pore diameter of the scaffolds, and artificial extracellular matrix (aECM) coatings had an additional positive effect for the scaffolds of both pore sizes.
Źródło:
Engineering of Biomaterials; 2009, 12, 86; 9-13
1429-7248
Pojawia się w:
Engineering of Biomaterials
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Resorbable scaffolds modified with collagen type I or hydroxyapatite : in vitro studies on human mesenchymal stem cells
Autorzy:
Rumian, Ł.
Wojak, I.
Scharnweber, D.
Pamuła, E.
Powiązania:
https://bibliotekanauki.pl/articles/307304.pdf
Data publikacji:
2013
Wydawca:
Politechnika Wrocławska. Oficyna Wydawnicza Politechniki Wrocławskiej
Tematy:
collagen type I
human mesenchymal stem cells
hydroxyapatite
poly(L-lactide-co-glycolide)
scaffolds
kolagen
hydroksyapatyt
mezenchyma
Opis:
Poly(L-lactide-co-glycolide) (PLGA) scaffolds of pore size within the range of 250–320 μm were produced by solvent casting/ porogen leaching method. Afterwards, they were modified through adsorption of collagen type I and incubation in simulated body fluid (SBF) to allow deposition of hydroxyapatite (HAp). The wettability of the scaffolds was measured by sessile drop test. Scanning electron microscopy (SEM) evaluation and energy dispersive X-ray analysis (EDX) were also performed. SEM evaluation and EDX analysis depicted the presence of HAp deposits and a collagen layer on the pore walls on the surface and in the bulk of the scaffolds. Wettability and water droplets penetration time within the scaffolds decreased considerably after applying modifications. Human mesenchymal stem cells (hMSC) were cultured on the scaffolds for 28 days and cell morphology, proliferation and differentiation as well as calcium deposition were evaluated. Lactate dehydrogenase (LDH) activity results revealed that cells cultured on tissue culture polystyrene (TCPS) exhibited high proliferation capacity. Cell growth on the scaffolds was slower in comparison to TCPS and did not depend on modification applied. On the other hand, osteogenic differentiation of hMSC as confirmed by alkaline phosphatase (ALP) activity and mineralization results was enhanced on the scaffolds modified with hydroxyapatite and collagen.
Źródło:
Acta of Bioengineering and Biomechanics; 2013, 15, 1; 61-67
1509-409X
2450-6303
Pojawia się w:
Acta of Bioengineering and Biomechanics
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Adhesion, growth and osteogenic differentiation of human bone marrow mesenchymal stem cells on positively and negatively charged and uncharged ferroelectric crystal surfaces
Autorzy:
Vandrovcova, M.
Bacakova, L.
Vanek, P.
Petzelt, J.
Powiązania:
https://bibliotekanauki.pl/articles/285786.pdf
Data publikacji:
2016
Wydawca:
Akademia Górniczo-Hutnicza im. Stanisława Staszica w Krakowie. Polskie Towarzystwo Biominerałów
Tematy:
electroactive ceramics
surface charge
cell number
resazurin
type I collagen
alkaline phosphatase
osteocalcin
bone matrix mineralization
Opis:
The cell-material interaction is significantly influenced by the physicochemical properties of the material surface, including its electrical charge. In this study, the effect of the surface polarity of ferroelectric LiNbO3 single crystals on the adhesion, growth and osteogenic differentiation of human bone marrow mesenchymal stem cells was investigated. The cells were cultured on the normal-to-plane poled and in-plane poled plates resulting in positive, negative and zero surface charge. The number of initially adhering cells on day 1 after seeding, their spreading, shape, and their metabolic activity, production of type I collagen, activity of alkaline phosphatase and mineralization in the following days of cultivation (days 6 and 20) were comparable on all three tested surfaces. However, significant differences were found in the expression of mRNA for type I collagen, alkaline phosphatase and osteocalcin, i.e. an early, medium-term and late arkers of osteogenic cell differentiation, respectively. On day 20, the expression of type I collagen was significantly lower in cells on negatively-charged than on non-charged surfaces. Moreover, the expression of alkaline phosphatase and osteocalcin was higher in cells on positively-charged than on negatively-charged surfaces. These differences were generally more pronounced in standard cell culture medium than in osteogenic medium, which could, at least partly, mask the influence of the material surface properties on the cell behaviour. Thus, positively-charged LiNbO3 surfaces seemed to be more suitable for the osteogenic differentiation of bone marrow mesenchymal stem cells than the negatively-charged surfaces.
Źródło:
Engineering of Biomaterials; 2016, 19, 135; 2-7
1429-7248
Pojawia się w:
Engineering of Biomaterials
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-7 z 7

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