Wynik wyszukiwania w bazie Polska Bibliografia Lekarska GBL

Zapytanie: CHYCZEWSKI
Liczba odnalezionych rekordów: 5



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1/5

Tytuł oryginału: Patomechanizm perlaka
Autorzy: Olszewska Ewa, Chodynicki Stanisław, Chyczewski Lech
Źródło: W: Postępy w otolaryngologii - Wrocław, 2002 s.84-87, bibliogr. 14 poz. - 40 Zjazd Polskiego Towarzystwa Otorynolaryngologów - Chirurgów Głowy i Szyi Mikołajki 2002
Sygnatura GBL: 740,321

Hasła klasyfikacyjne GBL:
  • chirurgia
  • otorynolaryngologia

    Typ dokumentu:
  • praca związana ze zjazdem

    Wskaźnik treści:
  • ludzie

    2/5

    Tytuł oryginału: Immunohistochemical investigations of cathepsin D activity in the structures of cholesteatoma.
    Autorzy: Chodynicki Stanisław, Chyczewski Lech, Olszewska Ewa
    Źródło: Med. Sci. Monitor 2002: 8 (5) s.BR184-BR186, il., bibliogr. 12 poz.
    Sygnatura GBL: 313,278

    Hasła klasyfikacyjne GBL:
  • onkologia
  • otorynolaryngologia

    Typ dokumentu:
  • praca kliniczna
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • ludzie
  • dorośli 19-44 r.ż.
  • dorośli 45-64 r.ż.
  • dorośli = 65 r.ż.
  • płeć męska
  • płeć żeńska

    Streszczenie angielskie: Cathepsin D decomposes cytoplasmic proteins, cell organelles, collagen, elastase and proteoglycans. It takes part in angiogenesis and activates osteoclasts, and is thought to play a major role in the destruction of bone tissue by cholestatoma. The aim of the present study was to evaluate the activity of cathepsin D in the structures of cholesteatoma. Cholesteatomas were collected from 16 patients operated on for chronic inflammation of the middle ear. Specimens were fixed in formalin at pH 7.2, after which parrafin slices were made. Cathepsin D was assayed with a Dako set. Keratin was measured by the Kreyberag method. Normal skin from behind the ear was taken from the patients during the same operation. The samples included a stratified, desquamative epithelium (matrix), a streak containing connective tissue (perimatrix), and a mass of keratin debris. Cathepsin D demonstrates high activity in perimatrix cell adjacent to bone tissue, while it occurs in trace amounts in the matrix. A highly positive reaction was observed within keratin, which was present in the superficial layer of the epithelium. Pseudocathepsin located in desquamative epithelial cells demonstrated a high positive reaction. There were trace amounts of cathepsin D within the dermis. In the control group (the skin samples), there were trace amounts of cathepsin D within the corneous layer of the epithelium. Cathepsin D places a major role in bone tissue destruction due cholesteatoma.

    3/5

    Tytuł oryginału: The effect of pre-eclamptic umbilical cord serum on fibroblast division in culture.
    Autorzy: Pawlicka Elżbieta, Romanowicz Lech, Bańkowski Edward, Chyczewski Lech, Jaworski Stefan
    Źródło: Folia Histochem. Cytobiol. 2002: 40 (4) s.381-384, il., tab., bibliogr. 14 poz.
    Sygnatura GBL: 304,846

    Hasła klasyfikacyjne GBL:
  • ginekologia i położnictwo

    Typ dokumentu:
  • praca kliniczna
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • ludzie
  • noworodki
  • dorośli 19-44 r.ż.
  • płeć żeńska
  • ciąża

    Streszczenie angielskie: Edema, proteinuria, hypertension (EPH-gestosis), most commonly termed as pre-eclampsia, is the most common pregnancy-associated pathological syndrome. It is accompanied by a through remodelling of extracellular matrix in the umbilical cord tissues. It is commonly known that the presence of serum in culture medium storngly stimulates many functions of cells cultured in vitro. It was decided to check how the pre-eclamptic serum affects the fibroblast division in culture. Ki-67 is a protein present in proliferating cells and can be detected during all phases of the cell cycle (G1, S, G2/M) but not in resting (GO) cells. PCNA (proliferating cell nuclear antigen) is an intranuclear polypeptide whose synthesis rate is at its maximum during the S-phase of the cell cycle. The expression of Ki-67 and PCNA was measured by immunocytochemical methods and biosynthesis of DNA was evaluated by [14C]-thymidine incorporation. The activity of pre-eclamptic umbilical cord serum (UC-serum) was found to be distincly lower in comparison to control one. The expression of Ki and PCNA in fibroblast cultures treated wtih pre-eclaptic serum was also distinctly lower. Also the incorporation of [14C]-thymidine to DNA was lower than in the cultures treated with control UC-serum. It may by concluded that pre-eclampsia reduces the mitogenic activity of the umbilical cord serum.

    4/5

    Tytuł oryginału: Suitability of selected markers for indentification of elements of the Intestinal Nervous System (INS).
    Autorzy: Dzienis-Koronkiewicz E[wa], Dębek W[ojciech], Sulkowska M[ariola], Chyczewski L[ech]
    Źródło: Eur. J. Pediatr. Surg. 2002: 12 (6) s.397-401, il., bibliogr. 19 poz., r‚s., res., Zsfg
    Sygnatura GBL: 312,942

    Hasła klasyfikacyjne GBL:
  • pediatria
  • gastroenterologia
  • neurologia

    Typ dokumentu:
  • praca kliniczna
  • praca opublikowana za granicą
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • ludzie
  • noworodki
  • niemowlęta
  • dzieci 2-5 r.ż.
  • dzieci 6-12 r.ż.

    Streszczenie angielskie: The possibility of identifying and characterising elements of the enteric nervous system based on their contents of cathepsin D, chromogranin A, neuronal specific enolase and S-100 protein was studied in colorectal specimens (operative full-thickness, seromuscular and mucosomuscular biopsies) obtained from 15 children, aged 2 days to 10 years. Nine patients suffered from Hirschsprung's disease, and two from chronic constipation. Four neonates with imperforate anus or meconium ileus composed the control group. All markers were identified immunohistochemically by antibodies against human antigens with appropriate detection methods. Chromogranin A staining was not always adequate to identify all neuronal cell bodies and other nervous elements. However, it proved superior to the other methods in the depiction of neuroendocrine cells in the intestinal mucosa. Cathepsin D antibodies stained normal and abnormal neural cells with different intensity; nerve fibres were not stained. This marker did not allow an unequivocal differentiation of ganglion cells from macrophages within the submucosa; the latter exhibited exceptionally strong marking and in some cases represented the predominant elements in this area. Neuronal specific enolase was distinctly expressed in nerve cells and fibres of the intestinal wall. Atrophic and hypoplastic features could be identified, suggesting that this method may give some insight into functional aspects. Continuous connections between ganglions were also observed. S-100 protein antibodies resulted in a negative image of unstained ganglion cells surrounded...

    5/5

    Tytuł oryginału: A novel Gly to Arg substitution at position 388 of the ŕ1 chain of type I collagen in lethal form of osteogenesis imperfecta.
    Autorzy: [Gajko]-Galicka Anna, Wołczyński Sławomir, Leśniewicz Ryszard, Chyczewski Lech, Gindzieński Andrzej
    Źródło: Acta Bioch. Pol. 2002: 49 (2) s.443-450, il., bibliogr. s. 449-450
    Sygnatura GBL: 303,116

    Hasła klasyfikacyjne GBL:
  • traumatologia i ortopedia
  • genetyka

    Typ dokumentu:
  • tytuł obcojęzyczny
  • praca kazuistyczna
  • praca epidemiologiczna

    Wskaźnik treści:
  • płód
  • noworodki
  • dorośli 19-44 r.ż.
  • płeć męska
  • płeć żeńska
  • ludzie

    Streszczenie angielskie: 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 motehr was normal. Peptide mapping experiments localized the structural defect in the proband to ŕ1(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 ŕ1(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 ŕ1(I) chain and results in reduced thermal stability by 3řC and intracellular retention of abnormal molecules.

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