Search results

1

Effect of glycosylation inhibitors on binding properties of the Feγ receptors from guinea pig peritoneal macrophages

100%

Gorczyca W., Wieczorek Z., Lisowski J.

|

vol. 38

|

issue 1

135-137

2

Design, synthesis and biological evaluation of a new bridged immunosuppressor.

88%

Szewczuk Z., Wilczyński A., Petry I., Siemion I. Z., Wieczorek Z.

Acta Biochimica Polonica

|

2001

|

vol. 48

|

issue 4

1147-1150

EN

A bridged peptide with the sequence: H-Thr-Pro-Gln-Arg-Gly-Asp-Val-γ-Abu-Asn-Asp-Gln-Glu-Glu-Thr-Thr-Gly-Val-Val-Ser-Thr-Pro-Leu-Ile-Arg-Asn-Gly-OH was designed to mimic the discontinuous epitope of the HLA-DQ molecule that might interact with CD4. The bridged peptide revealed distinct suppressory effect in the humoral immune response. This result supports our suggestion that the 164-172 region of the HLA-DQ molecule may enhance its interactions with coreceptors, possibly with CD4.

3

On the peptide-antipeptide interactions in interleukin-1 receptor system.

76%

Kluczyk A., Cebrat M., Zbozień-Pacamaj R., Lisowski M., Stefanowicz P., Wieczorek Z., Siemion I. Z.

Acta Biochimica Polonica

|

2004

|

vol. 51

|

issue 1

57-66

EN

Interleukin-1 receptor antagonist (IL-1Ra) and vaccinia virus protein C10L share a VTXFYF motif, with X being Lys or Arg residue, respectively. Peptides of such sequence compete successfully with IL-1 for the cellular receptor. A pair of complementary peptides, based on the Siemion's hypothesis on the periodicity of the genetic code (QWLNIN and QWANIN), and another pair, in which, following the Root- Bernstein theory, Lys was used as complementary amino acid to Phe (QWLKIK and QWAKIK), were investigated for the peptide-antipeptide interactions using mass spectrometry (ESI-MS) and circular dichroism (CD) methods. The CD measurements indicated some conformational changes, more pronounced in the Siemion's pairs, however, no heterodimer formation was found by MS. In the region of IL-1 receptor situated close to the position of IL-1Ra in the IL-1Ra-receptor complex, a KQKL motif is present, suggesting a possibility of complementary recognition of the Root-Bernstein type in the IL-1 receptor. The biological activity of the complementary peptides is similar to that of the original ones. They efficiently compete with IL-1 and show moderate immunosuppressory activity in humoral and cellular immune response. The inhibition of the IL-1-IL-1 receptor interaction may result from the complementary peptides acting as mini-receptors with affinity for IL-1.

4

Interaction of three Caenorhabditis elegans isoforms of translation initiation factor eIF4E with mono- and trimethylated mRNA 5' cap analogues.

64%

Stachelska A., Wieczorek Z., Ruszczyńska K., Stolarski R., Pietrzak M., Lamphear B. J., Rhoads R. E., Darżynkiewicz E., Jankowska-Anyszka M.

|

vol. 49

|

issue 3

671-682

EN

Translation initiation factor eIF4E binds the m7G cap of eukaryotic mRNAs and mediates recruitment of mRNA to the ribosome during cap-dependent translation initiation. This event is the rate-limiting step of translation and a major target for translational control. In the nematode Caenorhabditis elegans, about 70% of genes express mRNAs with an unusual cap structure containing m32,2,7G, which is poorly recognized by mammalian eIF4E. C. elegans expresses five isoforms of eIF4E (IFE-1, IFE-2, etc.). Three of these (IFE-3, IFE-4 and IFE-5) were investigated by means of spectroscopy and structural modelling based on mouse eIF4E bound to m7GDP. Intrinsic fluorescence quenching of Trp residues in the IFEs by iodide ions indicated structural differences between the apo and m7G cap bound proteins. Fluorescence quenching by selected cap analogues showed that only IFE-5 forms specific complexes with both m7G- and m32,2,7G-containing caps (Kas 2×106 M-1 to 7×106 M-1) whereas IFE-3 and IFE-4 discriminated strongly in favor of m7G-containing caps. These spectroscopic results quantitatively confirm earlier qualitative data derived from affinity chromatography. The dependence of Kas on pH indicated optimal cap binding of IFE-3, IFE-4 and IFE-5 at pH 7.2, lower by 0.4 pH units than that of eIF4E from human erythrocytes. These results provide insight into the molecular mechanism of recognition of structurally different caps by the highly homologous IFEs.

Refine search results

4 Acta Biochimica Polonica

1 2004

1 2002

1 2001

1 1991

4 Wieczorek Z.

2 Siemion I. Z.

1 Cebrat M.

1 Darżynkiewicz E.

1 Gorczyca W.

1 Jankowska-Anyszka M.

1 Kluczyk A.

1 Lamphear B. J.

1 Lisowski J.

1 Lisowski M.

1 Petry I.

1 Pietrzak M.

1 Rhoads R. E.

1 Ruszczyńska K.

1 Stachelska A.

1 Stefanowicz P.

1 Stolarski R.

1 Szewczuk Z.

1 Wilczyński A.

1 Zbozień-Pacamaj R.

Effect of glycosylation inhibitors on binding properties of the Feγ receptors from guinea pig peritoneal macrophages

Design, synthesis and biological evaluation of a new bridged immunosuppressor.

On the peptide-antipeptide interactions in interleukin-1 receptor system.

Interaction of three Caenorhabditis elegans isoforms of translation initiation factor eIF4E with mono- and trimethylated mRNA 5' cap analogues.