New pathway of heparan sulphate degradation

Medeiros, Maria G.L.; Ferreira, Thais M.P.C.; Leite, Edda Lisboa; Toma, Leny; Dietrich, Carl P.; Nader, Helena B.

doi:10.1016/s0305-0491(98)00015-7

Cited by 10 publications

(2 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…There are two classes of GAG depolymerizing enzymes: prokaryotic lyases and eukaryotic glycosidases. 47 The cleavage of GAGs affords oligosaccharides with a new free reducing end, which enables the attachment of fluorescent tag for sensitive detection after separation. Among the most commonly used lyases are the HA lyases, CS lyases and HS lyases.…”

Section: Chemical and Enzymatic Degradation To Determine Gag Structurementioning

confidence: 99%

Proteoglycan sequence

Linhardt

2012

Mol. BioSyst.

103

View full text Add to dashboard Cite

Proteoglycans (PGs) are among the most structurally complex biomacromolecules in nature. They are present in all animal cells and frequently exert their critical biological functions through interactions with protein ligands and receptors. PGs are comprised of a core protein to which one or multiple, heterogeneous, and polydisperse glycosaminoglycan (GAG) chains are attached. Proteins, including the protein core of PGs, are now routinely sequenced either directly using proteomics or indirectly using molecular biology through their encoding DNA. The sequencing of the GAG component of PGs poses a considerably more difficult challenge because of the relatively underdeveloped state of glycomics and because the control of their biosynthesis in the endoplasmic reticulum and the Golgi is poorly understood and not believed to be template driven. Recently, the GAG chain of the simplest PG has been suggested to have a defined sequence based on its top-down Fourier transform mass spectral sequencing. This review examines the advances made over the past decade in the sequencing of GAG chains and the challenges the field face in sequencing complex PGs having critical biological functions in developmental biology and pathogenesis.

show abstract

Section: Chemical and Enzymatic Degradation To Determine Gag Structurementioning

confidence: 99%

Proteoglycan sequence

Linhardt

2012

Mol. BioSyst.

103

View full text Add to dashboard Cite

show abstract

“…They specifically hydrolyze β-linked D-glucuronides to D-glucuronic acid and aglycones [2,3]. In invertebrates various hydrolytic enzymes that participate in the breakdown and turnover of glycosaminoglycans have been reported [4][5][6]. In the mollusk Pomacea sp., several compounds with glycosidasic activities, such as β-glucuronidase, β-galactanase, heparan sulfate endo-β-glucuronidase, hexosaminidases and sulfatases were identified from its embryonic form [7].…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of a β-Glucuronidase Present During Embryogenesis of the Mollusk Pomacea sp.

Pereira¹,

Cruz²,

Albuquerque³

et al. 2005

PPL

View full text Add to dashboard Cite

A beta-glucuronidase was purified from Pomacea sp. eggs by ammonium sulfate fractionation, DEAE-BioGel and Heparin-Sepharose chromatographies. This enzyme showed a Mr 180 kDa, with subunits of 90 kDa. The kinetic parameters were: pH 4.0, temperature 60 degrees C, Km 2.7 x 10(-6) and Vmax 15.3 microM/h, activator Mg+2, and inhibitor: lactone of D-saccharic acid. beta-glucuronidase is an exoglucuronidase involved in glycosaminoglycans metabolism with kinetics parameters similar to those found in mammals.

show abstract

Sulfatasen: Struktur, Mechanismus, biologische Aktivität, Inhibition, Anwendung in Synthesen

2004

View full text Add to dashboard Cite

Sulfatasen – d. h. Sulfatester spaltende Enzyme – spielen eine entscheidende Rolle bei der Regulierung von Sulfatierungszuständen, die über die Funktion vieler physiologischer Moleküle entscheiden. Die Substrate der Sulfatasen reichen von kleinen cytosolischen Steroiden wie dem Östrogensulfat bis hin zu komplexen Kohlenhydraten auf Zelloberflächen, etwa den Glycosaminoglycanen. Die Umwandlung dieser Moleküle wurde mit wichtigen zellulären Funktionen in Verbindung gebracht, z. B. mit der Hormonregulation, dem zellulären Abbau und der Modulation von Signalisierungsprozessen. Sulfatasen hängen mit dem Ausbruch etlicher pathophysiologischer Erscheinungen zusammen, etwa mit hormonabhängigen Krebsformen. Bis heute sind zwar zahlreiche Sulfatasen identifiziert worden, die Aufklärung des weitreichenden Spektrums ihrer biologischen Aktivitäten befindet sich aber erst am Anfang. Dieser Aufsatz gibt einen Überblick über den derzeitigen Wissensstand zu den Strukturen, Mechanismen und der Inhibition von Sulfatasen.

show abstract

New pathway of heparan sulphate degradation

Cited by 10 publications

References 13 publications

Proteoglycan sequence

Proteoglycan sequence

Purification and Characterization of a β-Glucuronidase Present During Embryogenesis of the Mollusk Pomacea sp.

Sulfatasen: Struktur, Mechanismus, biologische Aktivität, Inhibition, Anwendung in Synthesen

Contact Info

Product

Resources

About

New pathway of heparan sulphate degradation

Cited by 10 publications

References 13 publications

Proteoglycan sequence

Proteoglycan sequence

Purification and Characterization of a &#946;-Glucuronidase Present During Embryogenesis of the Mollusk Pomacea sp.

Sulfatasen: Struktur, Mechanismus, biologische Aktivität, Inhibition, Anwendung in Synthesen

Contact Info

Product

Resources

About

Purification and Characterization of a β-Glucuronidase Present During Embryogenesis of the Mollusk Pomacea sp.