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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Дата:2014
Автор: Nikolaenko-Kamyshova, T.P.
Формат: Стаття
Мова:English
Опубліковано: Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України 2014
Назва видання:Experimental Oncology
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Онлайн доступ:http://dspace.nbuv.gov.ua/handle/123456789/145339
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Назва журналу:Digital Library of Periodicals of National Academy of Sciences of Ukraine
Цитувати: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
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spelling irk-123456789-1453392019-01-21T01:24:21Z The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms Nikolaenko-Kamyshova, T.P. Original contributions 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. 2014 Article 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 http://dspace.nbuv.gov.ua/handle/123456789/145339 en Experimental Oncology Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України
institution Digital Library of Periodicals of National Academy of Sciences of Ukraine
collection DSpace DC
language English
topic Original contributions
Original contributions
spellingShingle Original contributions
Original contributions
Nikolaenko-Kamyshova, T.P.
The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms
Experimental Oncology
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.
format Article
author Nikolaenko-Kamyshova, T.P.
author_facet Nikolaenko-Kamyshova, T.P.
author_sort Nikolaenko-Kamyshova, T.P.
title The role of α-acidic glycoprotein in formation of bleeding abnormalities in patients with myeloproliferative neoplasms
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
publisher Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України
publishDate 2014
topic_facet Original contributions
url http://dspace.nbuv.gov.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.
series Experimental Oncology
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