Diversity and functions of glycosaminoglycan sulfotransferases

Habuchi, Osami

doi:10.1016/s0304-4165(00)00016-7

Cited by 163 publications

(118 citation statements)

References 110 publications

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“…Glycoproteins and mucin could make the major contribution to this component [47,48]. Several strong Raman peaks of the second component are assigned to acetates (632, 1295, 1434, and 1744 cm -1 ) [49][50][51] and carbohydrates (323 cm -1 and 521 cm -1 ) [46,52], which are also present in saliva [53][54][55]. This spectral component shows (Figure 1.C, curve c) minute spectral regions with a flat horizontal shape (zero intensity level), which are the result of the nonegativity constrain used for calculating meaningful Raman spectral components.…”

Section: Raman Spectroscopic Signature Of Salivamentioning

confidence: 99%

Discriminant Analysis of Raman Spectra for Body Fluid Identification for Forensic Purposes

Sikirzhytski

Virkler

Lednev

et al. 2010

AIP Conference Proceedings

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Detection and identification of blood, semen and saliva stains, the most common body fluids encountered at a crime scene, are very important aspects of forensic science today. This study targets the development of a nondestructive, confirmatory method for body fluid identification based on Raman spectroscopy coupled with advanced statistical analysis. Dry traces of blood, semen and saliva obtained from multiple donors were probed using a confocal Raman microscope with a 785-nm excitation wavelength under controlled laboratory conditions. Results demonstrated the capability of Raman spectroscopy to identify an unknown substance to be semen, blood or saliva with high confidence.

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Section: Raman Spectroscopic Signature Of Salivamentioning

confidence: 99%

Discriminant Analysis of Raman Spectra for Body Fluid Identification for Forensic Purposes

Sikirzhytski

Virkler

Lednev

et al. 2010

AIP Conference Proceedings

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“…By action of a large family of enzymes known as sulfotransferases (STs), the sulfate group of PAPS is transferred to numerous endogenous as well as exogenous chemicals. For example, a Golgi-membrane ST sulfates glucosaminoglycans and thereby converts the common polysaccharides to unique binding sites that can be recognized by a biological signal molecule essential for cell growth and/or development (4,5). N-Sulfation of the GlcNAc moiety by heparan sulfate N-deacetylase/N-sulfotransferases (NDSTs) is the first step in the biosynthesis of heparan/heparin sulfates, followed by 2O-, 3O-, and 6O-sulfations.…”

mentioning

confidence: 99%

“…Since the late 1980s, nearly a hundred ST cDNAs have been cloned, including cytosolic and membrane enzymes (5,14). One difficulty soon realized was the lack of overall amino acid sequence homology between the cytosolic and membrane STs.…”

mentioning

confidence: 99%

Structure and Function of Sulfotransferases

Negishi

Pedersen

Petrotchenko

et al. 2001

Archives of Biochemistry and Biophysics

311

231

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Sulfotransferases (STs) catalyze the transfer reaction of the sulfate group from the ubiquitous donor 3 -phosphoadenosine 5 -phosphosulfate (PAPS) to an acceptor group of numerous substrates. This reaction, often referred to as sulfuryl transfer, sulfation, or sulfonation, is widely observed from bacteria to humans and plays a key role in various biological processes such as cell communication, growth and development, and defense. The cytosolic STs sulfate small molecules such as steroids, bioamines, and therapeutic drugs, while the Golgi-membrane counterparts sulfate large molecules including glucosaminylglycans and proteins. We have now solved the X-ray crystal structures of four cytosolic and one membrane ST. All five STs are globular proteins composed of a single ␣/␤ domain with the characteristic five-stranded ␤-sheet. The ␤-sheet constitutes the core of the Paps-binding and catalytic sites. Structural analysis of the PAPS-, PAP-, substrate-, and/or orthovanadate (VO 4 3؊ )-bound enzymes has also revealed the common molecular mechanism of the transfer reaction catalyzed by sulfotransferses. The X-ray crystal structures have opened a new era for the study of sulfotransferases.

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“…18 Glycosaminoglycans (GAGs), including chondroitin sulfate (CS), are involved in a wide variety of biological processes. [20][21][22][23] Part of the CS biosynthesis in the Golgi entails the transfer of sulfate groups to specific carbon positions of the disaccharide units by sulfotransferase enzymes. [20][21][22][23] The balance of chondroitin sulfation is tightly controlled through spatial and temporal expression of distinct chondroitin sulfotransferase genes.…”

Section: Introductionmentioning

confidence: 99%

“…[20][21][22][23] Part of the CS biosynthesis in the Golgi entails the transfer of sulfate groups to specific carbon positions of the disaccharide units by sulfotransferase enzymes. [20][21][22][23] The balance of chondroitin sulfation is tightly controlled through spatial and temporal expression of distinct chondroitin sulfotransferase genes. 21,24,25 Moreover, this tightly controlled chondroitin sulfation balance has been shown to be disturbed in human disease and malignancies.…”

Section: Introductionmentioning

confidence: 99%

C4ST-1/CHST11-controlled chondroitin sulfation interferes with oncogenic HRAS signaling in Costello syndrome

et al. 2012

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Costello syndrome is a pediatric genetic disorder linked to oncogenic germline mutations in the HRAS gene. The disease is characterized by multiple developmental abnormalities, as well as predisposition to malignancies. Our recent observation that heart tissue from patients with Costello syndrome showed a loss of the glycosaminoglycan chondroitin-4-sulfate (C4S) inspired our present study aimed to explore a functional involvement of the chondroitin sulfate (CS) biosynthesis gene Carbohydrate sulfotransferase 11/Chondroitin-4-sulfotransferase-1 (CHST11/C4ST-1), as well as an impaired chondroitin sulfation balance, as a downstream mediator of oncogenic HRAS in Costello syndrome. Here we demonstrate a loss of C4S, as well as a reduction in C4ST-1 mRNA and protein expression, in primary fibroblasts from Costello syndrome patients. We go on to show that expression of oncogenic HRAS in normal fibroblasts can repress C4ST-1 expression, whereas interference with oncogenic HRAS signaling in Costello syndrome fibroblasts elevated C4ST-1 expression, thus identifying C4ST-1 as a negatively regulated target gene of HRAS signaling. Importantly, we show that forced expression of C4ST-1 in Costello fibroblasts could rescue the proliferation and elastogenesis defects associated with oncogenic HRAS signaling in these cells. Our results indicate reduced C4ST-1 expression and chondroitin sulfation imbalance mediating the effects of oncogenic HRAS signaling in the pathogenesis of Costello syndrome. Thus, our work identifies C4ST-1-dependent chondroitin sulfation as a downstream vulnerability in oncogenic RAS signaling, which might be pharmacologically exploited in future treatments of not only Costello syndrome and other RASopathies, but also human cancers associated with activating RAS mutations.

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Diversity and functions of glycosaminoglycan sulfotransferases

Cited by 163 publications

References 110 publications

Discriminant Analysis of Raman Spectra for Body Fluid Identification for Forensic Purposes

Discriminant Analysis of Raman Spectra for Body Fluid Identification for Forensic Purposes

Structure and Function of Sulfotransferases

C4ST-1/CHST11-controlled chondroitin sulfation interferes with oncogenic HRAS signaling in Costello syndrome

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