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...
Збережено в:
Дата: | 2014 |
---|---|
Автор: | |
Формат: | Стаття |
Мова: | English |
Опубліковано: |
Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України
2014
|
Назва видання: | Experimental Oncology |
Теми: | |
Онлайн доступ: | http://dspace.nbuv.gov.ua/handle/123456789/145339 |
Теги: |
Додати тег
Немає тегів, Будьте першим, хто поставить тег для цього запису!
|
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. |
Репозитарії
Digital Library of Periodicals of National Academy of Sciences of Ukraineid |
irk-123456789-145339 |
---|---|
record_format |
dspace |
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 |
work_keys_str_mv |
AT nikolaenkokamyshovatp theroleofaacidicglycoproteininformationofbleedingabnormalitiesinpatientswithmyeloproliferativeneoplasms AT nikolaenkokamyshovatp roleofaacidicglycoproteininformationofbleedingabnormalitiesinpatientswithmyeloproliferativeneoplasms |
first_indexed |
2023-05-20T17:21:53Z |
last_indexed |
2023-05-20T17:21:53Z |
_version_ |
1796153127989149696 |