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Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju

Implications of posttranslational changes of fibrinogen on its reactivity and function

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2018
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Authors
Gligorijević, Nikola
Contributors
Vujčić, Zoran
Nedić, Olgica
Popović, Milica M.
Doctoral thesis (Published version)
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Abstract
Fibrinogen je vaţan protein primarne i glavni protein sekundarne hemostaze. Nakon povrede, on se dejstvom trombina pretvara u nerastvorni fibrin koji se dalje umreţava, pri čemu nastaje fibrinska mreţa koja ojačava krvni ugrušak na mestu povrede. Da bi fibrinogen obavljao svoju biohemijsku ulogu, bitni su odreĎeni faktori, u koje spadaju njegove posttranslacione modifikacije i interakcije sa drugim proteinima. Posttranslacione modifikacije fibrinogena utiču na njegovu strukturu, strukturu fibrina i interakcije sa drugim proteinima. Fibrin nije pasivna mreţa koja samo daje potporu krvnom ugrušku, već je aktivna struktura koja reguliše svoju sintezu i razgradnju interakcijom sa brojnim proteinima. Zato je vaţno otkriti nove proteine koji sa njim interaguju, a koji imaju uticaj na proces zarastanja povreda.U okviru ove diseretacije, optimizovana je procedura za izolovanje i analizu fibrinogena. Upotrebom dvostrukog taloţenja etanolom dobijen je visoko prečišćen fibrinogen, pogodan za dalj...u karakterizaciju.Kako je poznato da fibrinogen interaguje sa IGFBP-3 proteinom, postavilo se pitanje da li još neki protein iz grupe vezujućih proteina za IGF, pri fiziološkim uslovima, ima tu sposobnost. Upotrebom većeg broja afinitetnih metoda je pokazano da IGFBP-1 interaguje sa fibrinogenom i da je to opšta fiziološka pojava. Značaj ove interakcije treba sagledavati imajući u vidu da i IGFBP-1 podstiče zarastanje tkivnih povreda, samostalno i kao transporter IGF molekula.Brojne patologije pri kojima se javljaju i koagulopatije, kao što su dijabetes melitus tipa 2 i ciroza jetre, karakteriše izmenjena koncentracija i struktura fibrinogena, što za posledicu ima stvaranje abnormalnog, trombogenog fibrina. Detaljno izučavanje pojedinačnih proteina uključenih u koagulopatiju moţe dati bliţu sliku mehanizma odgovornog za ovu pojavu. Sa druge strane, promene na nivou posttranslacionih modifikacija i strukture fibrinogena sa starenjem mogu doprineti boljem razumevanju prisustva ili odsustva odreĎenih patologija kod starijih ljudi.Struktura fibrinogena sa starenjem se menja. Primenom lektinskog eseja uočeno je povećanje visoko-manoznih i/ili hibridnih N-glikana, tri-/tertaantenarnih kompleksnih glikana sa većim sadrţajem Gal i GlcNAc. Spektrofluorimetrijska analiza je pokazala da kod zdravih ljudi preko 60 godina starosti, fibrinogen ima kompaktniju tercijarnustrukturu...

Fibrinogen is an important protein of primary and main protein of secondary hemostasis. Upon injury, fibrinogen is converted to insoluble fibrin by the action of thrombin. Fibrin further cross-links and creates fibrin network which reinforces blood clotting at the site of injury. There is a significant contribution of posttranslational modifications as well as interactions with other proteins necessary for fulfillment of fibrinogen biochemical role. Posttranslational modifications of fibrinogen influence its structure, fibrin structure and interactions with other proteins. Fibrin is not only a passive network that supports blood clot, but also an active structure that regulates its synthesis and degradation by interacting with many different proteins. For this reason, it is important to identify new proteins which interact with fibrinogen and may also have a role in wound healing.The procedure for isolation and analysis of fibrinogen was optimized in this dissertation. Application of d...ouble precipitation using ethanol resulted in highly purified fibrinogen, suitable for further characterisation.Since it is known that fibrinogen interacts with IGFBP-3 protein, the question was raised weather some other protein from the family of the IGF-binding proteins has this ability under physiological conditions. By using several affinity methods, it was shown that IGFBP-1 interacts with fibrinogen and this is a general physiological event. The significance of this interaction should be evaluated taking into consideration that IGFBP-1 itself may have beneficial effect on tissue wound healing, alone and as a transporter of the IGF molecule.Several pathologies accompanied by coagulopathies, such as diabetes mellitus type 2 and cirrhosis, are characterised by altered concentration and structure of fibrinogen, which in turn creates abnormal, thrombogenic fibrin. Detailed study of individual proteins included in coagulopathy may enable closer look at mechanisms responsible for this outcome. On the other hand, changes in posttranslational modifications and structure of fibrinogen with aging may lead to better understanding of presence or absence of certain pathologies associated with ageing.The structure of fibrinogen alteres with aging. An increase of high-mannose and/or hybrid N-glycans, tri-/tetraantennary complex glycans with greater amounts ofGal and GlcNAc was detected by lectin array...

Keywords:
fibrinogen, posttranslacione modifikacije proteina, struktura proteina, koagulacione osobine, starenje, ciroza, dijabetes melitus tipa 2, protein-protein interakcije, hemijske modifikacije proteina / fibrinogen, posttranslational modifications of protein, protein structure, coagulation properties, aging, cirrhosis, diabetes mellitus type 2, protein-protein interactions, chemical modifications of protein
Source:
Универзитет у Београду, 2018
Publisher:
  • Универзитет у Београду, Хемијски факултет
Funding / projects:
  • Structural characterisation of the insulin-like growth factor (IGF) binding proteins and IGF receptors, their interactions with other physiological molecules and alterations in metabolic disorders (RS-173042)
[ Google Scholar ]
Handle
https://hdl.handle.net/21.15107/rcub_nardus_10480
URI
http://eteze.bg.ac.rs/application/showtheses?thesesId=6386
https://fedorabg.bg.ac.rs/fedora/get/o:19076/bdef:Content/download
http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=50770447
http://nardus.mpn.gov.rs/123456789/10480
https://cherry.chem.bg.ac.rs/handle/123456789/3162
Collections
  • Doktorati
Institution/Community
Hemijski fakultet
TY  - THES
AU  - Gligorijević, Nikola
PY  - 2018
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=6386
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:19076/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=50770447
UR  - http://nardus.mpn.gov.rs/123456789/10480
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3162
AB  - Fibrinogen je vaţan protein primarne i glavni protein sekundarne hemostaze. Nakon povrede, on se dejstvom trombina pretvara u nerastvorni fibrin koji se dalje umreţava, pri čemu nastaje fibrinska mreţa koja ojačava krvni ugrušak na mestu povrede. Da bi fibrinogen obavljao svoju biohemijsku ulogu, bitni su odreĎeni faktori, u koje spadaju njegove posttranslacione modifikacije i interakcije sa drugim proteinima. Posttranslacione modifikacije fibrinogena utiču na njegovu strukturu, strukturu fibrina i interakcije sa drugim proteinima. Fibrin nije pasivna mreţa koja samo daje potporu krvnom ugrušku, već je aktivna struktura koja reguliše svoju sintezu i razgradnju interakcijom sa brojnim proteinima. Zato je vaţno otkriti nove proteine koji sa njim interaguju, a koji imaju uticaj na proces zarastanja povreda.U okviru ove diseretacije, optimizovana je procedura za izolovanje i analizu fibrinogena. Upotrebom dvostrukog taloţenja etanolom dobijen je visoko prečišćen fibrinogen, pogodan za dalju karakterizaciju.Kako je poznato da fibrinogen interaguje sa IGFBP-3 proteinom, postavilo se pitanje da li još neki protein iz grupe vezujućih proteina za IGF, pri fiziološkim uslovima, ima tu sposobnost. Upotrebom većeg broja afinitetnih metoda je pokazano da IGFBP-1 interaguje sa fibrinogenom i da je to opšta fiziološka pojava. Značaj ove interakcije treba sagledavati imajući u vidu da i IGFBP-1 podstiče zarastanje tkivnih povreda, samostalno i kao transporter IGF molekula.Brojne patologije pri kojima se javljaju i koagulopatije, kao što su dijabetes melitus tipa 2 i ciroza jetre, karakteriše izmenjena koncentracija i struktura fibrinogena, što za posledicu ima stvaranje abnormalnog, trombogenog fibrina. Detaljno izučavanje pojedinačnih proteina uključenih u koagulopatiju moţe dati bliţu sliku mehanizma odgovornog za ovu pojavu. Sa druge strane, promene na nivou posttranslacionih modifikacija i strukture fibrinogena sa starenjem mogu doprineti boljem razumevanju prisustva ili odsustva odreĎenih patologija kod starijih ljudi.Struktura fibrinogena sa starenjem se menja. Primenom lektinskog eseja uočeno je povećanje visoko-manoznih i/ili hibridnih N-glikana, tri-/tertaantenarnih kompleksnih glikana sa većim sadrţajem Gal i GlcNAc. Spektrofluorimetrijska analiza je pokazala da kod zdravih ljudi preko 60 godina starosti, fibrinogen ima kompaktniju tercijarnustrukturu...
AB  - Fibrinogen is an important protein of primary and main protein of secondary hemostasis. Upon injury, fibrinogen is converted to insoluble fibrin by the action of thrombin. Fibrin further cross-links and creates fibrin network which reinforces blood clotting at the site of injury. There is a significant contribution of posttranslational modifications as well as interactions with other proteins necessary for fulfillment of fibrinogen biochemical role. Posttranslational modifications of fibrinogen influence its structure, fibrin structure and interactions with other proteins. Fibrin is not only a passive network that supports blood clot, but also an active structure that regulates its synthesis and degradation by interacting with many different proteins. For this reason, it is important to identify new proteins which interact with fibrinogen and may also have a role in wound healing.The procedure for isolation and analysis of fibrinogen was optimized in this dissertation. Application of double precipitation using ethanol resulted in highly purified fibrinogen, suitable for further characterisation.Since it is known that fibrinogen interacts with IGFBP-3 protein, the question was raised weather some other protein from the family of the IGF-binding proteins has this ability under physiological conditions. By using several affinity methods, it was shown that IGFBP-1 interacts with fibrinogen and this is a general physiological event. The significance of this interaction should be evaluated taking into consideration that IGFBP-1 itself may have beneficial effect on tissue wound healing, alone and as a transporter of the IGF molecule.Several pathologies accompanied by coagulopathies, such as diabetes mellitus type 2 and cirrhosis, are characterised by altered concentration and structure of fibrinogen, which in turn creates abnormal, thrombogenic fibrin. Detailed study of individual proteins included in coagulopathy may enable closer look at mechanisms responsible for this outcome. On the other hand, changes in posttranslational modifications and structure of fibrinogen with aging may lead to better understanding of presence or absence of certain pathologies associated with ageing.The structure of fibrinogen alteres with aging. An increase of high-mannose and/or hybrid N-glycans, tri-/tetraantennary complex glycans with greater amounts ofGal and GlcNAc was detected by lectin array...
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju
UR  - https://hdl.handle.net/21.15107/rcub_nardus_10480
ER  - 
@phdthesis{
author = "Gligorijević, Nikola",
year = "2018",
abstract = "Fibrinogen je vaţan protein primarne i glavni protein sekundarne hemostaze. Nakon povrede, on se dejstvom trombina pretvara u nerastvorni fibrin koji se dalje umreţava, pri čemu nastaje fibrinska mreţa koja ojačava krvni ugrušak na mestu povrede. Da bi fibrinogen obavljao svoju biohemijsku ulogu, bitni su odreĎeni faktori, u koje spadaju njegove posttranslacione modifikacije i interakcije sa drugim proteinima. Posttranslacione modifikacije fibrinogena utiču na njegovu strukturu, strukturu fibrina i interakcije sa drugim proteinima. Fibrin nije pasivna mreţa koja samo daje potporu krvnom ugrušku, već je aktivna struktura koja reguliše svoju sintezu i razgradnju interakcijom sa brojnim proteinima. Zato je vaţno otkriti nove proteine koji sa njim interaguju, a koji imaju uticaj na proces zarastanja povreda.U okviru ove diseretacije, optimizovana je procedura za izolovanje i analizu fibrinogena. Upotrebom dvostrukog taloţenja etanolom dobijen je visoko prečišćen fibrinogen, pogodan za dalju karakterizaciju.Kako je poznato da fibrinogen interaguje sa IGFBP-3 proteinom, postavilo se pitanje da li još neki protein iz grupe vezujućih proteina za IGF, pri fiziološkim uslovima, ima tu sposobnost. Upotrebom većeg broja afinitetnih metoda je pokazano da IGFBP-1 interaguje sa fibrinogenom i da je to opšta fiziološka pojava. Značaj ove interakcije treba sagledavati imajući u vidu da i IGFBP-1 podstiče zarastanje tkivnih povreda, samostalno i kao transporter IGF molekula.Brojne patologije pri kojima se javljaju i koagulopatije, kao što su dijabetes melitus tipa 2 i ciroza jetre, karakteriše izmenjena koncentracija i struktura fibrinogena, što za posledicu ima stvaranje abnormalnog, trombogenog fibrina. Detaljno izučavanje pojedinačnih proteina uključenih u koagulopatiju moţe dati bliţu sliku mehanizma odgovornog za ovu pojavu. Sa druge strane, promene na nivou posttranslacionih modifikacija i strukture fibrinogena sa starenjem mogu doprineti boljem razumevanju prisustva ili odsustva odreĎenih patologija kod starijih ljudi.Struktura fibrinogena sa starenjem se menja. Primenom lektinskog eseja uočeno je povećanje visoko-manoznih i/ili hibridnih N-glikana, tri-/tertaantenarnih kompleksnih glikana sa većim sadrţajem Gal i GlcNAc. Spektrofluorimetrijska analiza je pokazala da kod zdravih ljudi preko 60 godina starosti, fibrinogen ima kompaktniju tercijarnustrukturu..., Fibrinogen is an important protein of primary and main protein of secondary hemostasis. Upon injury, fibrinogen is converted to insoluble fibrin by the action of thrombin. Fibrin further cross-links and creates fibrin network which reinforces blood clotting at the site of injury. There is a significant contribution of posttranslational modifications as well as interactions with other proteins necessary for fulfillment of fibrinogen biochemical role. Posttranslational modifications of fibrinogen influence its structure, fibrin structure and interactions with other proteins. Fibrin is not only a passive network that supports blood clot, but also an active structure that regulates its synthesis and degradation by interacting with many different proteins. For this reason, it is important to identify new proteins which interact with fibrinogen and may also have a role in wound healing.The procedure for isolation and analysis of fibrinogen was optimized in this dissertation. Application of double precipitation using ethanol resulted in highly purified fibrinogen, suitable for further characterisation.Since it is known that fibrinogen interacts with IGFBP-3 protein, the question was raised weather some other protein from the family of the IGF-binding proteins has this ability under physiological conditions. By using several affinity methods, it was shown that IGFBP-1 interacts with fibrinogen and this is a general physiological event. The significance of this interaction should be evaluated taking into consideration that IGFBP-1 itself may have beneficial effect on tissue wound healing, alone and as a transporter of the IGF molecule.Several pathologies accompanied by coagulopathies, such as diabetes mellitus type 2 and cirrhosis, are characterised by altered concentration and structure of fibrinogen, which in turn creates abnormal, thrombogenic fibrin. Detailed study of individual proteins included in coagulopathy may enable closer look at mechanisms responsible for this outcome. On the other hand, changes in posttranslational modifications and structure of fibrinogen with aging may lead to better understanding of presence or absence of certain pathologies associated with ageing.The structure of fibrinogen alteres with aging. An increase of high-mannose and/or hybrid N-glycans, tri-/tetraantennary complex glycans with greater amounts ofGal and GlcNAc was detected by lectin array...",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju",
url = "https://hdl.handle.net/21.15107/rcub_nardus_10480"
}
Gligorijević, N.. (2018). Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_10480
Gligorijević N. Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju. in Универзитет у Београду. 2018;.
https://hdl.handle.net/21.15107/rcub_nardus_10480 .
Gligorijević, Nikola, "Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju" in Универзитет у Београду (2018),
https://hdl.handle.net/21.15107/rcub_nardus_10480 .

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