Role of angiostatins in diabetic complications

Tykhomyrov, А. A.; Shram, S. I.; Grinenko, T. V.

doi:10.18097/pbmc20156101041

Cited by 8 publications

(4 citation statements)

References 116 publications

(100 reference statements)

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“…14 Activation of oxidative stress causes a large number of oxygen-free radicals to form, which oxidizes with microvascular endothelial cells and glomerular basement membrane cells and causes cell damage, which will further cause proteins to leak through the glomerulus and enter the urine, causing proteinuria. 15,16 MDA is a lipid peroxide degradation product that reflects the degree of damage of oxygenfree radicals to cells. 17 SOD is a scavenger that eliminates harmful substances produced by organisms during metabolism.…”

Section: Discussionmentioning

confidence: 99%

Effects of Liraglutide Combined with Insulin on Oxidative Stress and Serum MCP-1 and NF-kB Levels in Type 2 Diabetes

Liu¹,

Huang²,

Li³

et al. 2019

J Coll Physicians Surg Pak

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Section: Discussionmentioning

confidence: 99%

Effects of Liraglutide Combined with Insulin on Oxidative Stress and Serum MCP-1 and NF-kB Levels in Type 2 Diabetes

Liu¹,

Huang²,

Li³

et al. 2019

J Coll Physicians Surg Pak

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“…It consists of several domains: the N-terminal domain, five sequential homologous kringle domains (K1, K2, K3, K4, and K5) and the proteinase domain. Lysine-binding sites (LBSs) of kringle domains allow the interaction of plasminogen with various proteins and receptors [3][4][5][6]. Glu-plasminogen exists in the closed conformation in plasma, it is stabilized by intramolecular interactions of the Nterminal domain with the K5 [7].…”

Section: Identification Of the Binding Site For Plasminogen Kringle 5 In The α-Chain Of Fibrin(ogen) D-fragment Introductionmentioning

confidence: 99%

Identification of the binding site for plasminogen kringle 5 in the ?-chain of fibrin(ogen) D-fragment

Kapustianenko¹,

Grinenko²,

Rebriev³

et al. 2020

Ukr.Biochem.J.

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The interaction of the fifth kringle of Glu-plasminogen with fibrin triggers activation and initiation of fibrinolysis, yet the site on fibrin that binds kringle 5 remains unknown. The aim of our work was to determine an amino acid sequence in the D-fragment of fibrin(ogen) molecule, which is complementary to the lysine-binding site (LBS) in kringle 5. We studied the interaction between kringle 5 of plasminogen with polypeptide chains of the D-fragments of fibrin and cyanogen bromide fragments FCB-2 and t-NDSK and showed that kringle 5 bound specifically to α-and γ-chains of the D-fragment and the α-chain of FCB-2. Tryptic peptides of D-fragment α-chain were obtained, separated by their ability to bind with the immobilized kringle 5, and then all studied peptides were characterized by MALDI-TOF analysis. The critical amino acid residues of the α-chain of D-fragment, which provide its interaction with kringle 5, turned out to be α171Arg and/or α176Lys. The binding site of Glu-plasminogen complementary to the LBS of kringle 5 is located within Аα168Ala−183Lys, a sequence in a weakly structured loop between two supercoils in the α-chain of the Dfragment of the fibrin(ogen) molecule. K e y w o r d s: plasminogen, kringle 5, fibrin(ogen), binding site, α-chain of fibrin D-fragment, fibrinolysis.

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“…[1][2] In addition, the limited proteolysis of macromolecules makes it possible to obtain functionally active fragments that can be used in medicine. 3 Over the past decade, powerful fibrinolytic enzymes from various sources have been discovered, such as earthworms, 4 snake poisons, 5 insects, 6 microorganisms 7 and marine species. 8 An attractive source of various biologically active compounds are fungi.…”

Section: Introductionmentioning

confidence: 99%

Fibrinogenolytic activity of protease from the culture fluid of <em>Pleurotus ostreatus</em>

et al. 2020

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The use of proteases makes it possible to obtain partially hydrolyzed forms of macromolecules with unique properties. The importance of proteases for studying the structure and functions of fibrinogen forces scientists to search for new sources of highly specific proteases. Thus, the aim of this work was to study the content of the Pleurotus ostreatus culture fluid in search of fibrinogen- specific proteases. P. ostreatus was cultured for 14 days at 27°C. The culture fluid was collected and the protein fraction was salted out with NaCl and then dialyzed. Fibrinogen hydrolysis products by P. ostreatus protease were characterized using SDS PAGE under reducing conditions followed by immunoprobing using murine monoclonal antibodies I-5A (anti-Aα505-610) and 2d2a (anti-Bβ26-42). The study of turbidity and platelet aggregation was performed using a Multiskan FC spectrophotometric microplate reader and a SOLAR-2110 aggregometer, respectively. Electron microscopy of fibrils formed by truncated compared with native fibrins was performed using a transmission electron microscope N-600. Analysis of the products of fibrinogen hydrolysis with a fungal protease using SDS-PAGE demonstrated the cleavage of the alpha chain of fibrinogen exclusively with the formation of a truncated form of fibrinogen in which there are no C-terminal portions of αC regions with a molecular weight of 25 kDa. A study of turbidity showed that the polymerization of truncated fibrin is significantly impaired. The rate of lateral association of protofibrils significantly decreased from 1.5 to 2.2 times in the case of truncated fibrinogen compared to the native one depending on the initial concentration of fibrinogen. It was shown that platelet aggregation in the presence of fibrinogen without 25 kDa fragments of αC regions was less effective than in the presence of native fibrinogen. Application of the preparation of the fungal protease allows us to obtain high molecular forms of the fibrinogen molecule with cleaved 25 kDa peptides, which provide new information on the role of these peptides in the fibrinogen functioning.

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Role of angiostatins in diabetic complications

Cited by 8 publications

References 116 publications

Effects of Liraglutide Combined with Insulin on Oxidative Stress and Serum MCP-1 and NF-kB Levels in Type 2 Diabetes

Effects of Liraglutide Combined with Insulin on Oxidative Stress and Serum MCP-1 and NF-kB Levels in Type 2 Diabetes

Identification of the binding site for plasminogen kringle 5 in the ?-chain of fibrin(ogen) D-fragment

Fibrinogenolytic activity of protease from the culture fluid of <em>Pleurotus ostreatus</em>

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