Structural characterization of human liver heparan sulfate

Vongchan, Preeyanat; Warda, Mohamad; Toyoda, Hidenao; Toida, Toshihiko; Marks, Rebecca A.; Linhardt, Robert J.

doi:10.1016/j.bbagen.2004.09.007

Cited by 65 publications

(72 citation statements)

References 38 publications

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“…The average recovery of the camel heparin/HS GAGs from these two organs was much higher than that reported in our previous studies on human liver heparin/HS (Vongchan et al, 2005) but lower than reported for camel intestinal heparin/HS . The average molecular mass of isolated heparin/HS GAGs were determined by polyacrylamide gel electrophoresis from the broad band associated with isolated GAGs (Fig.…”

Section: Resultscontrasting

confidence: 74%

Dromedary glycosaminoglycans: Molecular characterization of camel lung and liver heparan sulfate

Warda

Linhardt

2006

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Glycosaminoglycans (GAGs) are the portion of a proteoglycan that determine its final shape and function. The molecular structure of predominant GAG species in camel liver and lung is reported for the first time. The one-humped camel survives in an extreme, arid habitat and, thus, offers a good model to study the role of glycomics on homeostasis. Heparan sulfate (HS) from the lung and liver of the one-humped camel were isolated. Characterization of these newly isolated glycosaminoglycans included 1 H NMR spectroscopy and disaccharide compositional analysis. The relative molecular weight of these GAGs was estimated by gradient polyacrylamide gel electrophoresis and their degree of sulfation was also assessed. Anticoagulant activity was determined using an anti-factor Xa assay and the HS from camel lung shows ~50% of heparin's activity. The structural differences of camel liver GAGs compared to human and porcine liver heparin and HS is discussed. Camel lung heparan sulfate resembles both heparin and HS in its structure and properties suggesting that it is either a highly sulfated form of HS, a mixture of heparin and HS or an undersulfated heparin.

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Section: Resultscontrasting

confidence: 74%

Dromedary glycosaminoglycans: Molecular characterization of camel lung and liver heparan sulfate

Warda

Linhardt

2006

Comparative Biochemistry and Physiology Part B: Biochemistry an

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“…Liver HS showed the highest percentage of trisulfated disaccharide (ΔUA2S-GlcNS6S). While this gave murine liver HS a relatively high degree of sulfation of 0.94-0.95, these values were higher than previously reported for mouse liver [13], but considerably lower than other mamallian liver HS (ranging from 1.05-1.21) and much lower than that of the 2.55 value reported for porcine intestinal heparin [8].…”

Section: Hs Disaccharide Compositioncontrasting

confidence: 68%

“…Our examination of porcine, bovine, and human liver HS [8,35] show that it is rich in highly sulfated sequences and that these are responsible for ApoE interaction [34]. Furthermore, these highly charged liver HS chains also appear to act as receptors for pathogens such as dengue virus [36] and malaria circumsporozoite [37].…”

Section: Discussionmentioning

confidence: 84%

“…HS has been isolated from a wide variety of animals ranging from C. elegans and D. melanogaster to humans [2][3][4][5][6]. Structural differences have been demonstrated for HS isolated from a given organ derived from different species [7,8] for different organ systems within a single species [9][10][11][12][13] and in the same organ system at different developmental stages [5]. Moreover, HSPGs can undergo structural changes during progressive pathological events [12,14].…”

Section: Introductionmentioning

confidence: 99%

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Isolation and characterization of heparan sulfate from various murine tissues

et al. 2006

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Heparan sulfate (HS), is a proteoglycan (PG) found both in the extracellular matrix and on cell surface. It may represent one of the most biologically important glycoconjugates, playing an essential role in a variety of different events at molecular level. The publication of the mouse genome, and the intensive investigations aimed at understanding the proteome it encodes, has motivated us to initiate studies in mouse glycomics focused on HS. The current study is aimed at determining the quantitative and qualitative organ distribution of HS in mice. HS from brain, eyes, heart, lung, liver, kidney, spleen, intestine and skin was purified from 6-8 week old male and female mice. The recovered yield of HS from these organs is compared with the recovered whole body yield of HS. Structural characterization of the resulting HS relied on disaccharide analysis and 1 H-NMR spectroscopy. Different organs revealed a characteristic HS structure. These data begin to provide a structural understanding of the role of HS in cell-cell interactions, cell signaling

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“…Liver heparan sulfates differs from other in the way that they have large number of N-sulfated glucosamine residues at distal end of core protein and low sulfation density in proximal end relative to core protein [34,71].…”

Section: Heparin Sulfatementioning

confidence: 99%

Deciphering the mystery of hepatitis B virus receptors: A historical perspective

2015

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Hepatitis B virus is one of the major reasons of viral hepatitis with an estimated 350 million infected patients worldwide. Although, the virus was discovered and cloned more than three decades ago, its entry mechanism has still been in investigation. Numerous potential candidates have been proposed and investigated rigorously to reveal HBV entry mechanism and to unveil the first door of viral entry to hepatocytes. This review provides a short account of role of receptors for entry of HBV into hepatocytes. The viral preS1 region of large surface protein is involved in the attachment of HBV to hepatocytes. The putative attachment site of HBV is located at amino acids 21-47 of preS1. So far, several proteins have been proposed to interact with these different regions of the preS1 domain which includes human immunoglobulin A receptor, glyceraldehyde-3-phosphate dehydrogenase, interleukin-6, a 31-kDa protein, HBV binding factor, asialoglycoprotein receptor, nascent polypeptide-associated complex a polypeptide, lipoprotein lipase, hepatocyteassociated heparan sulfate proteoglycans, glucose-regulated protein 75. However, none of them have appeared to be generally accepted as a true receptor for the virus until recently when sodium taurocholate cotransporting polypeptide identified as HBV entry receptor. Current review provides scientific historical perspective of various candidates known to be interacting with preS1 of HBV for their possible role in viral entry.

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Structural characterization of human liver heparan sulfate

Cited by 65 publications

References 38 publications

Dromedary glycosaminoglycans: Molecular characterization of camel lung and liver heparan sulfate

Dromedary glycosaminoglycans: Molecular characterization of camel lung and liver heparan sulfate

Isolation and characterization of heparan sulfate from various murine tissues

Deciphering the mystery of hepatitis B virus receptors: A historical perspective

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