Wyniki wyszukiwania - Biblioteka Nauki

1

Milk-derived angiotensin-I-converting enzymeinhibitory peptides generated by Lactobacillus delbrueckii subsp. lactis CRL 581

100%

Villegas J. M. , Picariello G. , Mamone G. , Espeche Turbay M. B. , Savoy de Giori G. , Hebert E. M.

Peptidomics

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2014

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tom 1

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nr 1

EN

Several strains of Lactobacillus helveticus and Lactobacillus delbrueckii subsp. lactis were evaluated for their ability to release angiotensin-I-converting enzyme (ACE) inhibitory peptides from α-casein (α-CN) and β-casein (β-CN). Casein peptides resulting from L. delbrueckii subsp. lactis CRL 581-mediated hydrolysis exhibited the highest ACE-inhibitory (ACEI) activities, with values of 53 and 40% for α-CN and β-CN, respectively. The casein hydrolysates were fractionated by reversedphase high pressure liquid chromatography and some of the active peptides were identified by mass spectrometry. The fraction with the highest ACEI activity arose from β-CN and contained a mixture of the β-CN f194-206 (QEPVLGPVRGPFP) and f198-206 (LGPVRGPFP) peptides. Furthermore, the ACEI tripeptide IPP was identified in all β-CN hydrolysates; L. delbrueckii subsp. lactis CRL 581 produced the highest amount of this peptide. The bioactive peptides released by CRL 581 strain may be used in the formulation of functional foods and nutraceuticals, representing a healthier and natural alternative for regulating blood pressure.

2

Activity of mi and m-calpain in regenerating fast and slow twitch skeletal muscle

88%

Moraczewski J. , Piekarska E. , Zimowska M. , Sobolewska M.

Acta Biochimica Polonica

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1996

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tom 43

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nr 4

EN

Calpains — non-lysosomal intracellular calcium-activated neutral proteinases, form a family consisting of several distinct members. Two of the isoenzymes: ji (calpain I) and m (calpain II) responded differently to the injury during complete regeneration of Extensor digitorum longus (EDL) muscle and partial regeneration of Soleus muscle. In the crushed EDL the level of m-calpain on the 3rd and 7th day of regeneration was higher than in non-operated muscles, whereas the activity of this calpain in injured Soleus decreased. The level of n-calpain in EDL oscillated irregularly during regeneration whereas in Soleus of both injured and contralateral muscles its level rapidly rose. Our results support the hypothesis that m-calpain is involved in the process of fusion of myogenic cells whereas u-calpain plays a significant but indirect role in muscle regeneration.

3

Elastinolytic activity of horse leukocyte proteinases. Comparison with elastases from human leukocytes and porcine pancreas

75%

Potempa J. , Korzus E. , Dubin A. , Silberring J.

Folia Histochemica et Cytobiologica

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1986

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tom 24

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nr 2

4

Defense against own arms: staphylococcal cysteine proteases and their inhibitors.

75%

Dubin G.

Acta Biochimica Polonica

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2003

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tom 50

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nr 3

715-724

EN

Staphylococcus aureus is a human pathogen causing a wide range of diseases. Most staphylococcal infections, unlike those caused by other bacteria are not toxigenic and very little is known about their pathogenesis. It has been proposed that a core of secreted proteins common to many infectious strains is responsible for colonization and infection. Among those proteins several proteases are present and over the years many different functions in the infection process have been attributed to them. However, little direct, in vivo data has been presented. Two cysteine proteases, staphopain A (ScpA) and staphopain B (SspB) are important members of this group of enzymes. Recently, two cysteine protease inhibitors, staphostatin A and staphostatin B (ScpB and SspC, respectively) were described in S. aureus shedding new light on the complexity of the processes involving the two proteases. The scope of this review is to summarize current knowledge on the network of staphylococcal cysteine proteases and their inhibitors in view of their possible role as virulence factors.

5

Comparison of specificity of human and horse leucocyte proteinases with synthetic peptide substrates

75%

Dubin A. , Potempa J. , Schnebli H. P. , Koj A.

Folia Histochemica et Cytobiologica

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1986

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tom 24

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nr 2

6

Matrix degrading proteinases from human granulocytes: type I, II, III collagenase, gelatinase and type IV, V-collagenase. A survery of recent findings and inhibition by gamma-anticollagenase

75%

Tschesche H. , Fedrowitz J. , Kohnert U. , Michaelis J. , Macartney H. W.

Folia Histochemica et Cytobiologica

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1986

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tom 24

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nr 2

7

Development of leucine aminopeptidase activity during daylily flower growth and senescence

75%

Mahagamasekera M. G. P. , Leung D. W. M.

Acta Physiologiae Plantarum

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2001

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tom 23

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nr 2

8

The mutual influence of proteins from Varroa destructor extracts and from honeybee haemolymph on their proteolytic activity – in vitro study

63%

Fraczek R. J. , Zoltowska K. , Lipinski Z. , Dmitryjuk M.

Acta Parasitologica

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2013

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tom 58

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nr 3

EN

The influence of extracts from Varroa destructor, a parasitic mite of the honeybee Apis mellifera, on the proteinase activity of worker bee haemolymph was analysed in vitro, along with the influence of bee haemolymph on the proteolytic activity of V. destructor extract. The study was conducted in three different environments: pH 7.5 (high activity of bee enzymes and very low activity of parasite enzymes), pH 5 (moderate activity of enzymes from both sources) and pH 3.5 (limited activity of bee proteinases and high activity of mite proteinases). Based on electrophoretic studies, the inhibition of the activity of bee haemolymph proteinases by V. destructor extracts was observed at each pH. The study at pH 7.5 with commercial inhibitors of the 4 main classes of proteinases (pepstatin A, ethylenediaminetetraacetic acid (EDTA), E-64 (trans-epoxysuccinyl-L-leucylamido-(4-guanidino)-butane), soybean trypsin inhibitor and Kunitz inhibitor) suggested that parasite extracts mainly inhibited serine proteinases and, to a lower degree, cysteine and aspartyl proteinases. At pH 3.5 and pH 5, a decrease of approximately 40% in parasite proteinase activity was also observed in the presence of bee haemolymph. The result points to the presence of aspartyl proteinase inhibitors in bee haemolymph, which may be an important defence element for bees during food intake by a mite. It was demonstrated that trypsin and trypsin inhibitors are active in the excretion/secretion products of V. destructor, the proteinases of which may assist the parasite in food suckling by preventing haemolymph coagulation, among other things.

9

Some properties of a proteinase isolated from the hatching liquid of Coregonus albula

63%

Luberda Z. , Strzezek J. , Luczynski M.

Polskie Archiwum Hydrobiologii

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1992

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tom 39

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nr 3-4

10

Affinity purification of chicken pancreas proteinases and their N-terminal amino acid sequences

63%

Tluscik F. , Polanowski A. , Guyonnet V. , Long P. L. , Travis J.

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nr 2

11

Proteinases of Streptomyces fradiae II. Specificity

63%

Galas E. , Kaluzewska M.

Acta Microbiologica Polonica

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1992

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tom 41

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nr 3-4

12

Proteolytic and chitinolytic activity of the Pseudomonas isolated from within sporocarps of Cantharellus cibarius

63%

Dahm H. , Wrotniak W.

Bulletin of the Polish Academy of Sciences. Biological Sciences

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2003

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tom 51

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nr 3

13

Porphyromonas gingivalis proteinases in periodontitis, a review

63%

Potempa J. , Travis J.

Acta Biochimica Polonica

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1996

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tom 43

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nr 3

EN

Porphyromonas gingivalis has been closely associated with the initiation and progression of some forms of periodontal diseases and its proteolytic enzymes have been implicated in invasion, tissue destruction and evasion of host antibacterial defenses. Recently, the primary focus of research has been on cysteine proteinases, referred to as gingipain R and gingipain K which are produced in large quantities and are directly involved in pathological events during development and progression of periodontitis, contributing to clinical hallmarks of the disease including: flow of gingival crevicular fluid, neutrophil accumulation and bleeding on probing. Gingipain R exists as 110-, 95-, 70- to 90- and 50-kDa proteins, the first two being a complex of the 50-kDa catalytic subunit with hemagglutinin/adhesins, with or without an added membrane anchorage peptide. The other forms are single-chain enzymes. The predominant form of gingipain K in P. gingivalis strains is a complex of a 60-kDa catalytic protein with hemagglutinin/adhesins. Molecular cloning and structural characterization of the gingipain R and gingipain K genes has shown that they code for 1704 and 1722 amino-acid residue preproenzymes, respectively. Although both structures show no similarity within the preprofragment and only limited identity within the catalytic domain (27%) they are essentially identical within the putative hemagglutinin/adhesin domain. Furthermore, on the basis of gene structure it is now apparent that various soluble and membrane bound forms of gingipains are derived through proteolytic processing of the preproenzymes, and it can be assumed that the Arg-X-specific enzyme is responsible for this processing.

14

Wykorzystanie niekomercyjnych enzymów proteolitycznych do hydrolizy białek jaja

51%

Pokora M. , Szoltysik M. , Dabrowska A. , Chrzanowska J. , Trziszka T.

Acta Scientiarum Polonorum. Biotechnologia

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2010

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tom 09

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nr 4

PL

Przedmiotem badań był preparat owoalbuminowy stanowiący produkt uboczny uzyskiwany podczas wydzielania lizozymu i cystatyny z białka jaja kurzego, które poddano hydrolizie enzymatycznej. Początkowo oceniono podatność tego białka na działanie handlowych preparatów proteinaz: termolizyny, pronazy i neutrazy oraz enzymów proteolitycznych pozyskanych z dyni figolistnej (Cucurbitaficifolia) oraz z drożdży Y. lipolytica: serynowej i aspartylowej proteinazy. Do dalszej hydrolizy wykorzystano trzy ostatnie enzymy. Rozkład białka śledzono podczas 24-godzinnej inkubacji enzymu z substratem, oznaczając stopień jego hydrolizy i przyrost wolnych grup aminowych, a także prowadząc rozdział chromatograficzny metodą RP-HPLC. Stwierdzono, że najgłębszą degradację preparatu owoalbumi- nowego na poziomie 45% uzyskano pod wpływem proteinazy serynowej z dyni. Wyraźnie niższą aktywność wobec tego białka przejawiały obydwie proteinazy drożdżowe. Profile pep- tydowe RP-HPLC uzyskanych hydrolizatów potwierdziły różnice w podatności preparatu owoalbuminy na działanie testowanych enzymów proteolitycznych.

EN

Ovoalbumine preparation obtained as by-product during isolation of lysozyme and cystatin from egg white was used as substrate for proteolytic enzymes. The protein was degraded by plant serine proteinase isolated from Cucurbita ficifolia and by two yeast proteinases: aspartic and serine isolated from Yarrowia lipolytica. Degradation process was monitored by determination of the hydrolysis degree and the increase of free amino groups concentration. The obtained hydrolysates were also fractioned by RP-HPLC. It was shown that the highest degree of hydrolysis (45%) of ovoalbumin preparation was achieved with plant proteinase. Peptide profiles of the protein hydrolysates confirmed differences in specificity of tested proteinases against ovoalbumin preparation.

15

The effect of doxycycline on atherogenesis in apoE-knockout mice

51%

Pawlowska M. , Gajda M. , Pyka-Fosciak G. , Toton-Zuranska J. , Niepsuj A. , Kus K. , Bujak-Gizycka B. , Suski M. , Olszanecki R. , Jawien J. , Korbut R.

Journal of Physiology and Pharmacology

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2011

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tom 62

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nr 2

EN

Doxycycline at subantimicrobial doses inhibits matrix metalloproteinases (MMPs) activity, and is the only MMP inhibitor which is widely available in clinical practice. The aim of the study was to reveal whether non-specific MMPs inhibition by tetracycline could ameliorate development of atherosclerosis in apolipoprotein E (apoE)-knockout mice. Doxycycline (1.5 mg/ kg b.w./day) administered orally attenuated atherogenesis, measured both by "en face" method (10.25±1.7% vs. 15.7±2.0%, p<0.05) and "cross-section" method (66,254±7,468 µm2 vs. 90,687±8,521 µm2, p<0.05). In-situ zymography showed decrease of the extent of non-specific gelatinase activity in doxycycline-treated mice This is the first report to date describing the effect of doxycycline on atherogenesis in apoE-targeted mice.

16

Human cathepsin D

51%

Minarowska A. , Gacko M. , Karwowska A. , Minarowski L.

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tom 46

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nr 1

23-38

17

Produkcja pozakomórkowych hydrolaz przez szczepy Yarrowia lipolytica pochodzące z sera

51%

Szoltysik M. , Chrzanowska J. , Zelazko M. , Niedbalska J. , Polomska X. , Juszczyk P. , Wojtatowicz M.

Acta Scientiarum Polonorum. Biotechnologia

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2008

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tom 07

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nr 4

18

Changes of activity of some hydrolases during triticale grain development differentiated in pre-harvest sprouting resistance

51%

Andrzejczuk-Hybel J. , Bartoszewicz K. , Bielawski W. , Kaczkowski J.

Acta Physiologiae Plantarum

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1994

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tom 16

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nr 4

19

Molecules released by helminth parasites involved in host colonization

51%

Dzik J. M.

Acta Biochimica Polonica

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2006

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tom 53

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nr 1

EN

Parasites are designed by evolution to invade the host and survive in its organism until they are ready to reproduce. Parasites release a variety of molecules that help them to penetrate the defensive barriers and avoid the immune attack of the host. In this respect, particularly interesting are enzymes and their inhibitors secreted by the parasites. Serine-, aspartic-, cysteine-, and metalloproteinases are involved in tissue invasion and extracellular protein digestion. Helminths secrete inhibitors of these enzymes (serpins, aspins, and cystatins) to inhibit proteinases, both of the host and their own. Proteinases and their inhibitors, as well as helminth homologues of cytokines and molecules containing phosphorylcholine, influence the immune response of the host biasing it towards the anti-inflammatory Th2 type. Nucleotide-metabolizing enzymes and cholinesterase are secreted by worms to reduce inflammation and expel the parasites from the gastrointestinal tract. An intracellular metazoan parasite, Trichinella spiralis, secretes, among others, protein kinases and phosphatases, endonucleases, and DNA-binding proteins, which are all thought to interfere with the host cellular signals for muscle cell differentiation. Secretion of antioxidant enzymes is believed to protect the parasite from reactive oxygen species which arise from the infection-stimulated host phagocytes. Aside from superoxide dismutase, catalase (rarely found in helminths), and glutathione peroxidase (selenium-independent, thus having a poor activity with H2O2), peroxiredoxins are probably the major H2O2-detoxifying enzymes in helminths. Secretion of antioxidant enzymes is stage-specific and there are examples of regulation of their expression by the concentration of reactive oxygen species surrounding the parasite. The majority of parasite-secreted molecules are commonly found in free-living organisms, thus parasites have only adapted them to use in their way of life.

20

Proteinases from pollen and pests

51%

Travis J. , Whitworth T. , Matheson N. , Bagarozzi D.

Acta Biochimica Polonica

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1996

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tom 43

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nr 3

EN

An examination of the proteinases present in two vety different systems is described, in order to illustrate the diversity in function of this class of enzymes. In the first case we have noted the importance of gut proteinases from the fire ant Solenopsis invicta in relation to the nutritional requirements of the entire colony. In the second we have investigated the properties of endoproteases from both ragweed and mesquite pollen, relative to their role in the development of allergies and asthma. If the function of each type of enzyme(s) is correct, then it is clear that addition of exogenous inhibitors might be useful in a) controlling the infestation associated with the fire ant, and b) reducing the deleterious effects associated with the development of asthma.