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    Tytuł:
    Orthopedic upper limb appliances in post-stroke patients used in prevention of shoulder pain syndrome
    Zaopatrzenie ortopedyczne kończyny górnej u chorych po udarze mózgu stosowane w profilaktyce zespołu bolesnego barku
    Autorzy:
    Gieremek, Krzysztof
    Cieśla, Wojciech
    Kubacki, Janusz
    Rojczyk-Chmarek, Jolanta
    Powiązania:
    https://bibliotekanauki.pl/articles/1939042.pdf
    Data publikacji:
    2008
    Wydawca:
    Akademia Wychowania Fizycznego im. Bronisława Czecha w Krakowie
    Tematy:
    Stroke
    hemiplegic shoulder
    orthopedic upper limb appliances
    Rehabilitation
    udar mózgu
    zespół bolesnego barku hemiplegika
    ortezy konczyny górnej
    rehabilitacja
    Opis:
    Shoulder pain constitutes one of the more serious problems that occur after cerebral stroke. Such ailments concern evan 65% of patients. The so-called Painful Shoulder Syndrome of Hemiplegic (p.s.s.h) is often a result of negligence and delayed initiation of physiotherapy. Application of appropriate orthopaedic supply is an important element of the therapy. Possibilities of orthopedic appliances of paretic upper limb in post-stroke patients are commonly limited to forearm and arm orthesis or sling. Such equipment is, however, not sufficient, especially for patient’s shoulder joint. Post-stroke processes within the shoulder area occur in 81% of patients resulting in physical therapy difficulties and causing pain and limb dysfunction. The article presents aetiopathogenesis of hemiplegic shoulder; special attention is directed to the most common therapy and nursing mistakes. The article describes market analysis with regard to availability of modern orthopedic equipment for both prevention and treatment of the syndrome of hemiplegic shoulder. Advantages and disadvantages of the following devices were discussed: traditional sling, Itman’s sling, abduction pillow and Aperent Activ apparatus. The new, original type of orthopaedic supply: Hemi-Flex apparatus was described in a wider range. Significant advantages of this type of supply were stressed out, while a conclusion was also drawn that this supply should be an element of standard treatment of patients with paresis or plegia following cerebral stroke.
    Źródło:
    Medical Rehabilitation; 2008, 12(1); 25-31
    1427-9622
    1896-3250
    Pojawia się w:
    Medical Rehabilitation
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Phosphorylation of basic amino acid residues in proteins: important but easily missed
    Autorzy:
    Cieśla, Joanna
    Frączyk, Tomasz
    Rode, Wojciech
    Powiązania:
    https://bibliotekanauki.pl/articles/1039902.pdf
    Data publikacji:
    2011
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    basic amino acids
    posttranslational modification
    phosphorylation
    acid-labile
    base-stable
    phosphoramidate
    Opis:
    Reversible phosphorylation is the most widespread posttranslational protein modification, playing regulatory role in almost every aspect of cell life. The majority of protein phosphorylation research has been focused on serine, threonine and tyrosine that form acid-stable phosphomonoesters. However, protein histidine, arginine and lysine residues also may undergo phosphorylation to yield acid-labile phosphoramidates, most often remaining undetected in conventional studies of protein phosphorylation. It has become increasingly evident that acid-labile protein phosphorylations play important roles in signal transduction and other regulatory processes. Beside acting as high-energy intermediates in the transfer of the phosphoryl group from donor to acceptor molecules, phosphohistidines have been found so far in histone H4, heterotrimeric G proteins, ion channel KCa3.1, annexin 1, P-selectin and myelin basic protein, as well as in recombinant thymidylate synthase expressed in bacterial cells. Phosphoarginines occur in histone H3, myelin basic protein and capsidic protein VP12 of granulosis virus, whereas phospholysine in histone H1. This overview of the current knowledge on phosphorylation of protein basic amino-acid residues takes into consideration its proved or possible roles in cell functioning. Specific requirements of studies on acid-labile protein phosphorylation are also indicated.
    Źródło:
    Acta Biochimica Polonica; 2011, 58, 2; 137-148
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Altered mouse leukemia L1210 thymidylate synthase, associated with cell resistance to 5-fluoro-dUrd, is not mutated but rather reflects posttranslational modification
    Autorzy:
    Cieśla, Joanna
    Frączyk, Tomasz
    Zieliński, Zbigniew
    Sikora, Jacek
    Rode, Wojciech
    Powiązania:
    https://bibliotekanauki.pl/articles/1041288.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    protein phosphorylation
    L1210
    thymidylate synthase
    posttranslational modification
    FdUrd resistance
    Opis:
    Thymidylate synthase purified from 5-fluoro-dUrd-resistant mouse leukemia L1210 cells (TSr) was less sensitive to slow-binding inhibition by 5-fluoro-dUMP than the enzyme from the parental cells (TSp), both enzyme forms differing also in sensitivity to several other dump analogues, apparent molecular weights of monomer and dimer, and temperature dependence of the catalyzed reaction. Direct sequencing of products obtained from RT-PCR, performed on total RNA isolated from the parental and 5-fluoro-dUrd-resistant cells, proved both nucleotide sequences to be identical to the mouse thymidylate synthase coding sequence published earlier (NCBI protein database access no. NP_067263). This suggests that the altered properties of TSr are caused by a factor different than protein mutation, presumably posttranslational modification. As a possibility of rat thymidylate synthase phosphorylation has been recently demonstrated (Samsonoff et al. (1997) J Biol Chem 272: 13281), the mouse enzyme amino-acid sequence was analysed, revealing several potential phosphorylation sites. In order to test possible influence of the protein phosphorylation state on enzymatic properties, endogenous TSp and TSr were purified in the presence of inhibitors of phosphatases. Although both enzyme forms were phosphorylated, as shown by electrophoretical separation followed by phosphoprotein detection, the extent of phosphorylation was apparently similar. However, the same two purified enzyme preparations, compared to the corresponding preparations purified in the absence of phosphatase inhibitors, showed certain properties, including sensitivity to the slow-binding inhibition by FdUMP, altered. Thus properties dependence on phosphorylation was indicated.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 1; 189-198
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The effect of Arg209 to Lys mutation in mouse thymidylate synthase.
    Autorzy:
    Cieśla, Joanna
    Gołos, Barbara
    Wałajtys-Rode, Elżbieta
    Jagielska, Elżbieta
    Płucienniczak, Andrzej
    Rode, Wojciech
    Powiązania:
    https://bibliotekanauki.pl/articles/1043728.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    nucleotide's phosphate binding
    thymidylate synthase
    mutation
    Opis:
    Mouse thymidylate synthase R209K (a mutation corresponding to R218K in Lactobacillus casei), overexpressed in thymidylate synthase-deficient Escherichia coli strain, was poorly soluble and with only feeble enzyme activity. The mutated protein, incubated with FdUMP and N5,10-methylenetetrahydrofolate, did not form a complex stable under conditions of SDS/polyacrylamide gel electrophoresis. The reaction catalyzed by the R209K enzyme (studied in a crude extract), compared to that catalyzed by purified wild-type recombinant mouse thymidylate synthase, showed the Km value for dUMP 571-fold higher and Vmax value over 50-fold (assuming that the mutated enzyme constituted 20% of total crude extract protein) lower. Thus the ratios kcat, R209K/kcat, 'wild' and (kcat, R209K/Km, R209KdUMP)/( kcat, 'wild'/Km, 'wild'dUMP) were 0.019 and 0.000032, respectively, documenting that mouse thymidylate synthase R209, similar to the corresponding L. casei R218, is essential for both dUMP binding and enzyme reaction.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 3; 651-658
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-5 z 5

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