scholarly journals HEPARAN SULFATES EXPRESSION IN SURGERY MATERIAL OF OVARIAN ENDOMETRIAL CYSTS

2020 ◽  
Vol 76 (4) ◽  
pp. 96-99
Author(s):  
S.V. Aidagulova ◽  
◽  
Yu.S. Timofeeva ◽  
A.V. Volchek ◽  
V.M. Kuleshov ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycans ◽  
Simultaneous Increase ◽  
Ovarian Endometriosis ◽  
Core Proteins ◽  
Heparan Sulfates ◽  
Pathological Tissues

The expression of heparan sulfate proteoglycans in eutopic and heterotopic endometrium in patients with ovarian endometriosis was studied using the method of immunohistochemistry. The simultaneous increase in the level of expression of core proteins of all studied heparan sulfate proteoglycans and the content of heparan sulfate in pathological tissues indicates the important role of glycosylated molecules in the pathogenesis of ovarian endometriosis.

scholarly journals Role of heparan sulfate proteoglycans in the binding and uptake of apolipoprotein E-enriched remnant lipoproteins by cultured cells

1993 ◽  
Vol 268 (14) ◽  
pp. 10160-10167
Author(s):  
Z.S. Ji ◽  
W.J. Brecht ◽  
R.D. Miranda ◽  
M.M. Hussain ◽  
T.L. Innerarity ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Heparan Sulfate ◽  
Cultured Cells ◽  
Heparan Sulfate Proteoglycans ◽  
Remnant Lipoproteins

scholarly journals Role of Cellular Heparan Sulfate Proteoglycans in Infection of Human Adenovirus Serotype 3 and 35

2008 ◽  
Vol 4 (10) ◽  
pp. e1000189 ◽  
Author(s):  
Sebastian Tuve ◽  
Hongjie Wang ◽  
Jeffrey D. Jacobs ◽  
Roma C. Yumul ◽  
David F. Smith ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Human Adenovirus ◽  
Heparan Sulfate Proteoglycans ◽  
Adenovirus Serotype

scholarly journals The Uptake of Lipoprotein-Borne Phylloquinone (Vitamin K1) by Osteoblasts and Osteoblast-Like Cells: Role of Heparan Sulfate Proteoglycans and Apolipoprotein E

2002 ◽  
Vol 17 (3) ◽  
pp. 426-433 ◽  
Author(s):  
Paul Newman ◽  
Fiona Bonello ◽  
Anthony S. Wierzbicki ◽  
Peter Lumb ◽  
Geoffrey F. Savidge ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycans ◽  
Vitamin K1

scholarly journals SARS-CoV-2 Infection and Transmission Depends on Heparan Sulfates and Is Blocked by Low Molecular Weight Heparins

2020 ◽  
Author(s):  
Marta Bermejo-Jambrina ◽  
Julia Eder ◽  
Tanja M. Kaptein ◽  
Leanne C. Helgers ◽  
Philip J.M. Brouwer ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Dendritic Cells ◽  
Epithelial Cells ◽  
Heparan Sulfate ◽  
Alveolar Macrophages ◽  
Neutralizing Antibodies ◽  
Heparan Sulfate Proteoglycans ◽  
Low Molecular Weight ◽  
Low Molecular Weight Heparins ◽  
Heparan Sulfates

AbstractThe current pandemic caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) and new outbreaks worldwide highlight the need for preventive treatments. Although angiotensin converting enzyme 2 (ACE2) is the primary receptor for SARS-CoV-2, we identified heparan sulfate proteoglycans expressed by epithelial cells, alveolar macrophages and dendritic cells as co-receptors for SARS-CoV-2. Low molecular weight heparins (LMWH) blocked SARS-CoV-2 infection of epithelial cells and alveolar macrophages, and virus dissemination by dendritic cells. Notably, potent neutralizing antibodies from COVID-19 patients interfered with SARS-CoV-2 binding to heparan sulfate proteoglycans, underscoring the importance of heparan sulfate proteoglycans as receptors and uncover that SARS-CoV-2 binding to heparan sulfates is an important mechanism for neutralization. These results have imperative implications for our understanding of SARS-CoV-2 host cell entry and reveal an important target for novel prophylactic intervention.

Heparinoids and cellular interactions in the vascular system

1996 ◽  
Vol 16 (01) ◽  
pp. 28-34
Author(s):  
K. T. Preissner
Keyword(s):  
Heparan Sulfate ◽  
Vascular System ◽  
Vascular Diseases ◽  
Basement Membranes ◽  
Heparan Sulfate Proteoglycans ◽  
The Body ◽  
Pharmacological Intervention ◽  
Cellular Interactions ◽  
Heparin Binding ◽  
Core Proteins

SummaryHeparin and related polysaccharides have long been used for therapautic intervention in different disease states related to thromboembolic complications. The localization and functional availability of heparin-like components in the body is mostly confined to cell surfaces and extracellular matrix/basement membranes. Their strategic position particularly in the vascular system enables heparinoids linked to various core proteins (designated as heparan sulfate proteoglycans) to interact with a variety of heparin-binding proteins such as apolipoproteins, lipases, proteases and protease inhibitors, matrix proteins as well as surface receptors on other cells and microorganisms. The variety in gene expression of respective core proteins and differences in glycosaminoglycan side chains are relevant factors for the selectivity of these interactions. Heparinoid-associated core proteins serve as co-receptors for a number of metabolic properties of vascular cells as well as for the regulation of cellular processes, particular as they relate to cell growth and differentiation in angiogenesis. Moreover, heparan sulfate proteoglycans contribute to the process of lipoprotein retention in the vessel wall and the onset of atherosclerosis. Elucidation of molecular properties, functions and their role in vascular diseases can lead to valuable information for the design of heparinoid analogues to be used for pharmacological intervention.

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