Publications by authors named "Hellec C"

Article Synopsis
  • The Golgi apparatus is a vital organelle responsible for processing proteins, and this study focused on the distribution of glycosyltransferases within it using advanced imaging techniques.
  • Researchers discovered that even glycosyltransferases thought to be in the same compartment have unique localizations influenced by their N-terminal regions.
  • The findings suggest that these N-terminal regions are critical for determining where glycosyltransferases are located, enhancing our understanding of Golgi organization and potentially informing clinical strategies for protein glycosylation.
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Ultrasound is currently recommended as the first-line examination for abdominal symptoms in children. However, a pediatric radiologist is not always available on site, especially during on-call duty. This study was aimed at evaluating the reliability of an innovative 3-D virtual abdominal tele-ultrasonography in this context.

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Heparan sulfate 3--sulfotransferases (HS3STs) catalyze the maturation step of heparan sulfate (HS) 3--sulfation. This modification is relatively rare. Moreover, only a few biological processes have been described to be influenced by 3--sulfated HS, and few ligands have been identified so far.

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Background: Heparan sulfate (HS) 3-O-sulfation can be catalysed by seven 3-O-sulfotransferases (HS3STs) in humans, still it is the rarest modification in HS and its biological function is yet misunderstood. HS3ST2 and HS3ST3B exhibit the same activity in vitro. They are however differently expressed in macrophages depending on cell environment, which suggests that they may be involved in distinct cellular processes.

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Heparan sulfate 3-O-sulfotransferases (HS3STs) catalyze the final maturation step of heparan sulfates. Although seven HS3ST isozymes have been described in human, 3-O-sulfation is a relatively rare modification, and only a few biological processes have been described to be influenced by 3-O-sulfated motifs. A conflicting literature has recently reported that HS3ST2, 3A, 3B and 4 may exhibit either tumor-promoting or anti-oncogenic properties, depending on the model used and cancer cell phenotype.

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Heparan sulfates (HS) are involved in numerous biological processes, which rely on their ability to interact with a large panel of proteins. Although the reaction of 3-O-sulfation can be catalysed by the largest family of HS sulfotransferases, very few mechanisms have been associated with this modification and to date, only glycoprotein D (gD) of herpes simplex virus-1 (HSV-1 gD) and cyclophilin B (CyPB) have been well-described as ligands for 3--sulfated HS. Here, we hypothesized that both ligands could induce the same responses via a mechanism dependent on 3--sulfated HS.

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Heparan sulfate (HS) 6-O-endosulfatases (Sulfs) have emerged recently as critical regulators of many physiological and pathological processes. By removing 6-O-sulfates from specific HS sequences, they modulate the activities of a variety of growth factors and morphogens, including fibroblast growth factor (FGF)-1. However, little is known about the functions of Sulfs in inflammation.

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The authors report on a prospective study about goitre in French Polynesia carried out in 1989, dealing with epidemiology and disease characterization in 39 patients. 1. Epidemiology of goitre in Tahiti; In schools: 517 children (236 boys and 281 girls) aged from 10 to 15.

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