105054-56-6Relevant articles and documents
Discovery of human Golgi β-galactosidase with no identified glycosidase using a QMC substrate design platform for exo-glycosidase
Miura, Kazuki,Hakamata, Wataru,Tanaka, Ayako,Hirano, Takako,Nishio, Toshiyuki
, p. 1369 - 1375 (2016)
Post-translational modifications (PTMs) of proteins play important roles in the physiology of eukaryotes. In the PTMs, non-reversible glycosylations are classified as N-glycosylations and O-glycosylations, and are catalyzed by various glycosidases and glycosyltransferases. However, β-glycosidases are not known to play a role in N- and O-glycan processing, although both glycans provide partial structures as substrates for β-galactosidase and β-N-acetylglucosaminidase in the Golgi apparatus of human cells. We explored human Golgi β-galactosidase using fluorescent substrates based on a quinone methide cleavage (QMC) substrate design platform that was previously developed to image exo-type glycosidases in living cells. As a result, we discovered a novel Golgi β-galactosidase in human cells. It is possible to predict a novel and important function in glycan processing of this β-galactosidase, because various β-galactosyl linkages in N- and O-glycans exist in Golgi apparatus. In addition, these results show that the QMC platform is excellent for imaging exo-type glycosidases.
Identification of a novel glycan processing enzyme with exo-acting β-allosidase activity in the Golgi apparatus using a new platform for the synthesis of fluorescent substrates
Hakamata, Wataru,Miura, Kazuki,Hirano, Takako,Nishio, Toshiyuki
, p. 73 - 79 (2015)
The majority of eukaryotic proteins undergo post-translational modifications (PTMs) involving the attachment of complex glycans, predominantly through N-glycosylation and O-glycosylation. PTMs play important roles in virtually all cellular processes, and aberrant regulation of protein glycosylation and glycan processing has been implicated in various diseases. However, glycan processing on proteins in various cellular contexts has not been visualized. We had previously developed a quinone methide cleavage (QMC) platform for enhanced substrate design. This platform was applied here to screen for novel glycan-processing enzymes. We designed and synthesized fluorescent substrates with β-allopyranoside residues using the QMC platform. When applied in cell-based assays, the fluorescent substrates allowed rapid and clear visualization of β-allosidase activity in the Golgi apparatus of human cultured cells. The QMC platform will likely find broad applications in visualizing the activities of glycan processing enzymes in living cells and in studying PTMs.
Fluorescent probe for rapidly detecting β - galactosidase and preparation method and application thereof
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, (2021/10/27)
The invention relates to a fluorescent probe for rapidly detecting β - galactosidase and a preparation method and application thereof. The fluorescent probe for rapidly detecting β - galactosidase has a chemical structural formula as shown in (I). The nea
Cyano vinylene derivative fluorescent dye as well as preparation method and application thereof
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Paragraph 0015; 0017, (2020/05/05)
The invention relates to a cyanovinylene derivative fluorescent dye as well as a preparation method and application thereof, and discloses a compound represented by a structural general formula (I), and the compound R1 is independently selected from H, NH2, OH, CN, CH3, COOH, SO3H, F, Cl, Br or NO2; R2 is a group described in the specification. The compound probe molecule provided by the inventioncan realize quantitative detection of beta-Gal in a buffer solution test system, is not interfered by other proteases, biological mercaptan, active oxygen and common cations, and is successfully applied to in-situ detection of beta-Gal in biological cells of SKOV3 cells.
A General Approach to Enzyme-Responsive Liposomes
Lou, Jinchao,Best, Michael D.
, p. 8597 - 8607 (2020/07/04)
Liposomes are effective nanocarriers due to their ability to deliver encapsulated drugs to diseased cells. Nevertheless, liposome delivery would be improved by enhancing the ability to control the release of contents at the target site. While various stimuli have been explored for triggering liposome release, enzymes provide excellent targets due to their common overexpression in diseased cells. We present a general approach to enzyme-responsive liposomes exploiting targets that are commonly aberrant in disease, including esterases, phosphatases, and β-galactosidases. Responsive lipids correlating with each enzyme family were designed and synthesized bearing an enzyme substrate moiety attached via a self-immolating linker to a non-bilayer lipid scaffold, such that enzymatic hydrolysis triggers lipid decomposition to disrupt membrane integrity and release contents. Liposome dye leakage assays demonstrated that each enzyme-responsive liposome yielded significant content release upon enzymatic treatment compared to minimal release in controls. Results also showed that fine-tuning liposome composition was critical for controlling release. DLS analysis showed particle size increases in the cases of esterase- and β-galactosidase-responsive lipids, supporting alterations to membrane properties. These results showcase an effective modular strategy that can be tailored to target different enzymes, providing a promising new avenue for advancing liposomal drug delivery.
