The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms

Aim: To compare glycoforms of alpha-acid glycoprotein (AGP) in myeloproliferative neoplasms (MPN) with hepatic lesions. Materials and Methods: 110 patients with MPN (31 with polycythaemia vera (PV), 75 with primary myelofibrosis (PMF), 4 with essential thrombocythemia (ET)) were examined. 92 patient...

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Published in:Experimental Oncology
Date:2014
Main Author: Nikolaenko-Kamyshova, T.P.
Format: Article
Language:English
Published: Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України 2014
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Online Access:https://nasplib.isofts.kiev.ua/handle/123456789/145339
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Cite this:The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms / T.P. Nikolaenko-Kamyshova // Experimental Oncology. — 2014. — Т. 36, № 2. — С. 101-106. — Бібліогр.: 12 назв. — англ.

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Digital Library of Periodicals of National Academy of Sciences of Ukraine
id nasplib_isofts_kiev_ua-123456789-145339
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spelling Nikolaenko-Kamyshova, T.P.
2019-01-20T16:42:55Z
2019-01-20T16:42:55Z
2014
The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms / T.P. Nikolaenko-Kamyshova // Experimental Oncology. — 2014. — Т. 36, № 2. — С. 101-106. — Бібліогр.: 12 назв. — англ.
1812-9269
https://nasplib.isofts.kiev.ua/handle/123456789/145339
Aim: To compare glycoforms of alpha-acid glycoprotein (AGP) in myeloproliferative neoplasms (MPN) with hepatic lesions. Materials and Methods: 110 patients with MPN (31 with polycythaemia vera (PV), 75 with primary myelofibrosis (PMF), 4 with essential thrombocythemia (ET)) were examined. 92 patients with atherosclerotic lesions of lower extremities and 10 healthy people comprised the control. AGP concentration in blood serum was determined by rocket electrophoresis and affinity chromatography. The carbohydrate moiety of AGP was studied by lectin blotting with panel comprising eight lectins. The total content of sialic acids and the type of chemical linkage with galactose were determined. Results: High-molecular fragments of AGP detected in MPN (MM 68, 84, and 126 kDa) have been shown as deriving from leukocytes with glycan moiety identified as neutrophilic component. In MPN with thrombotic complications, AGP fragments with MM 84 and 126 kDa prevailed with hypersialic components suggesting the leukocyte component (originated from polymorphonuclear neutrophils) as the principal element in the development of thrombotic complications. Furthermore, in MPN with thrombotic complications, strong direct correlation was established between high levels of lactate dehydrogenase (LDH) and C-reactive protein on the one hand and high-molecular fragments of AGP with MM 84 and 126 kDa on the other hand. AGP level depended on primary diagnosis: in PV AGP level decreased, PMF (leukocytosis > 20 G/l) was characterized by normal level of AGP due to neutrophilic component. In MPN, glycosylation of AGP was reduced due to the N-glycans. Increase in the amount of branched glycans and sialylation of AGP in MPN seemed to originate from the high activity of neutrophils. Conclusion: It is determined that the deficiency of platelets and leucocytes function plays an important role in progression of myeloproliferative syndrome with myelofibrosis formation. Key Words: α-acidic glycoprotein, myeloproliferative neoplasms, polymorphonuclear neutrophils, thrombohemorrhagic complications.
en
Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України
Experimental Oncology
Original contributions
The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms
Article
published earlier
institution Digital Library of Periodicals of National Academy of Sciences of Ukraine
collection DSpace DC
title The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms
spellingShingle The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms
Nikolaenko-Kamyshova, T.P.
Original contributions
title_short The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms
title_full The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms
title_fullStr The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms
title_full_unstemmed The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms
title_sort role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms
author Nikolaenko-Kamyshova, T.P.
author_facet Nikolaenko-Kamyshova, T.P.
topic Original contributions
topic_facet Original contributions
publishDate 2014
language English
container_title Experimental Oncology
publisher Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України
format Article
description Aim: To compare glycoforms of alpha-acid glycoprotein (AGP) in myeloproliferative neoplasms (MPN) with hepatic lesions. Materials and Methods: 110 patients with MPN (31 with polycythaemia vera (PV), 75 with primary myelofibrosis (PMF), 4 with essential thrombocythemia (ET)) were examined. 92 patients with atherosclerotic lesions of lower extremities and 10 healthy people comprised the control. AGP concentration in blood serum was determined by rocket electrophoresis and affinity chromatography. The carbohydrate moiety of AGP was studied by lectin blotting with panel comprising eight lectins. The total content of sialic acids and the type of chemical linkage with galactose were determined. Results: High-molecular fragments of AGP detected in MPN (MM 68, 84, and 126 kDa) have been shown as deriving from leukocytes with glycan moiety identified as neutrophilic component. In MPN with thrombotic complications, AGP fragments with MM 84 and 126 kDa prevailed with hypersialic components suggesting the leukocyte component (originated from polymorphonuclear neutrophils) as the principal element in the development of thrombotic complications. Furthermore, in MPN with thrombotic complications, strong direct correlation was established between high levels of lactate dehydrogenase (LDH) and C-reactive protein on the one hand and high-molecular fragments of AGP with MM 84 and 126 kDa on the other hand. AGP level depended on primary diagnosis: in PV AGP level decreased, PMF (leukocytosis > 20 G/l) was characterized by normal level of AGP due to neutrophilic component. In MPN, glycosylation of AGP was reduced due to the N-glycans. Increase in the amount of branched glycans and sialylation of AGP in MPN seemed to originate from the high activity of neutrophils. Conclusion: It is determined that the deficiency of platelets and leucocytes function plays an important role in progression of myeloproliferative syndrome with myelofibrosis formation. Key Words: α-acidic glycoprotein, myeloproliferative neoplasms, polymorphonuclear neutrophils, thrombohemorrhagic complications.
issn 1812-9269
url https://nasplib.isofts.kiev.ua/handle/123456789/145339
citation_txt The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms / T.P. Nikolaenko-Kamyshova // Experimental Oncology. — 2014. — Т. 36, № 2. — С. 101-106. — Бібліогр.: 12 назв. — англ.
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