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1

Fibrillar collagens: how it is possible that seemingly monotonous structures have so numerous and various biological functions?

100%
Sieron A. L.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr Supplement 1
2

Tolloids, function-structure relations and related disorders resulting from extra-cellular matrix pathology

100%
Sieron A. L.
Acta Biochimica Polonica
|
2018
|
tom 65
|
nr S2
3

Izoprostany jako bio-wskaźniki stresu oksydacyjnego in vivo

51%
Klarzynska K., Scieglinska D., Sieron A. L.
Postępy Biologii Komórki
|
2017
|
tom 44
|
nr 4
4

Specific inhibition of procollagen C-endopeptidase activity by synthetic peptide with conservative sequence found in chordin

45%
Lesiak M., Augusciak-Duma A., Szydlo A., Pruszczynska K., Sieron A. L.
Acta Biochimica Polonica
|
2008
|
tom 55
|
nr 2
297-305
Procollagen C-endopeptidase (BMP-1) and N-endopeptidase (ADAMTS-2) are key enzymes for correct and efficient conversion of fibrillar procollagens to their self assembling monomers. Thus, they have an essential role in building and controlling the quality of extracellular matrices (ECMs). Here, we tested inhibition of activity of the largest variant of BMP-1, a recombinant mammalian tolloid (mTld), in vitro by three synthetic peptides with conservative amino-acid sequences found in chordin using procollagen type I as a substrate. We also verified the specific action of best inhibitory 16 amino-acid peptide in the procollagen type I cleavage assay with the use of ADAMTS-2 (procollagen N-endopeptidase). Subsequently, we determined the critical residues and minimal sequence of six amino acids in the original 16 amino-acid peptide required to maintain the inhibitory potential. Studies on the interactions of 6 and 16 amino acid long peptides with the enzyme revealed their binding to non-catalytic, regulatory domains of mTld; the inhibitory activity was not due to the competition of peptides with the substrate for the enzyme active center, because mTld did not cleave the peptides. However, in the presence of mTld both peptides underwent cyclization by disulfide bond formation. Concluding, we have shown that procollagen C-endopeptidase may be specifically blocked via its non-catalytic domains by synthetic peptide consisting of 6 amino acids in the sequence found in highly conservative region of chordin. Thus, we hypothesize that the 6 amino-acid peptide could be a goodcandidate for anti-fibrotic drug development.
5
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Sensitization to the storage mite Tyrophagus putrescentiae in urban population of Upper Silesia [Poland]

45%
Szilman E., Szilman P., Solarz K., Brewczynski P., Sieron A. L.
Wiadomości Parazytologiczne
|
2004
|
tom 50
|
nr 3
6

Cytochrome P450 mRNA expressions along with in vitro differentiation of hepatocyte precursor cells from fetal, young and old rats

39%
Czekaj P., Bryzek A., Czekaj T. M., Koryciak-Komarska H., Wiaderkiewicz A., Plewka D., Sieron A. L.
Folia Histochemica et Cytobiologica
|
2010
|
tom 48
|
nr 1
46-57
7

Occupational exposure to allergenic mites among workers of the Silesian Zoo

39%
Szilman P., Szilman E., Szilman M., Meszynska E., Maniurka H., Solarz K., Sieron A. L.
Biological Letters
|
2006
|
tom 43
|
nr 2
8

Mutations in the COL1A1 and COL1A2 genes associated with osteogenesis imperfecta (OI) types I or III

33%
Augusciak-Duma A., Witecka J., Sieron A. L., Janeczko M., Pietrzyk J. J., Ochman K., Galicka A., Boeszewska-Kornacka M. K., Pilch J., Jakubowska-Pietkiewicz E.
Acta Biochimica Polonica
|
2018
|
tom 65
|
nr 1
9

Possible association of the TERT promoter polymorphisms rs2735940, rs7712562 and rs2853669 with diabetes mellitus in obese elderly Polish population: results from the national PolSenior study

33%
Gutmajster E., Chudek J., Augusciak-Duma A., Szwed M., Szybalska A., Mossakowska M., Puzianowska-Kuznicka M., Wiecek A., Sieron A. L.
Journal of Applied Genetics
|
2018
|
tom 59
|
nr 3
10

Two novel COL1A1 mutations in patients with osteogenesis imperfecta [OI] affect the stability of the collagen type I triple-helix

33%
Witecka J., Augusciak-Duma A. M., Kruczek A., Szydlo A., Lesiak M., Krzak M., Pietrzyk J. J., Mannikko M., Sieron A. L.
Journal of Applied Genetics
|
2008
|
tom 49
|
nr 3
283-295
Osteogenesis imperfecta (OI) is a bone dysplasia caused by mutations in the COLIA1 and COL1A2 genes. Although the condition has been intensely studied for over 25 years and recently over 800 novel mutations have been published, the relation between the location of mutations and clinical manifestation is poorly understood. Here we report missense mutations in COLIA1 of several OI patients. Two novel mutations were found in the D1 period. One caused a substitution of glycine 200 by valine at the N-terminus of D1 in OI type I/IV, lowering collagen stability by 50% at 34°C. The other one was a substitution of valine 349 by phenylalanine at the C-terminus of D1 in OI type I, lowering collagen stability at 37.5°C. Two other mutations, reported before, changed amino residues in D4. One was a lethal substitution changing glycine 866 to serine in genetically identical twins with OI type II. That mutated amino acid was near the border of D3 and D4. The second mutation changed glycine 1040 to serine located at the border of D4 and DO.4, in a proband manifesting OI type III, and lowered collagen stability at 39°C (2°C lower than normal). Our results confirm the hypothesis on a critical role of the D1 and D4 regions in stabilization of the collagen triple-helix. The defect in D1 seemed to produce a milder clinical type of OI, whereas the defect in the C-terminal end of collagen type caused the more severe or lethal types of OI.
11

Heterogeneous mixture of amniotic cells is likely a better source of stem cells than adipose tissue

27%
Kitala D., Klama-Baryla A., Misiuga M., Labus W., Kraut M., Szapski M., Lesiak M., Krakowian D., Sieron A. L., Los M. J., Kucharzewski M.
Archivum Immunologiae et Therapiae Experimentalis
|
2019
|
tom 67
|
nr 3
12

The comparison of multipotential for differentiation of progenitor mesenchymal-like stem cells obtained from livers of young and old rats

27%
Tarnowski M., Koryciak-Komarska H., Czekaj P., Sebesta R., Czekaj T. M., Urbanek K., Likus W., Malinowska-Kolodziej I., Plewka D., Nowaczyk-Dura G., Wiaderkiewicz R., Sieron A. L.
Folia Histochemica et Cytobiologica
|
2007
|
tom 45
|
nr 3
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