Glycobiology: Progress, problems, and perspectives

Wiederschain, G. Ya.

doi:10.1134/s0006297913070018

Cited by 32 publications

(20 citation statements)

References 87 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Besides the increase in total activity of some lysosomal enzymes in glycosidoses, the concentration of protein activators/ chaperones that are components of the intralysosomal matrix is significantly increased. Based on these data, we suppose that the hyperactivation of the lysosomal hydrolytic system could be a protective reaction of the cell to product accumulation [17]. The elucidation of mechanisms regulating these processes possibly through certain signaling messengers of lysosomes-cytoplasmnucleus-cell membranes may lead to discovery of other important pathways of intracellular communication.…”

Section: Discussionmentioning

confidence: 93%

Secondary biochemical and morphological consequences in lysosomal storage diseases

Alroy

Garganta

Wiederschain

2014

Biochemistry Moscow

View full text Add to dashboard Cite

More than 50 hereditary lysosomal storage disorders (LSDs) are currently described. Most of these disorders are due to a deficiency of certain hydrolases/glycosidases and subsequent accumulation of nonhydrolyzable carbohydrate-containing compounds in lysosomes. Such accumulation causing hypertrophy of the lysosomal compartment is a characteristic feature of affected cells in LSDs. The investigation of biochemical and cellular parameters is of particular interest for understanding "life" of lysosomes in the normal state and in LSDs. This review highlights the wide spectrum of biochemical and morphological changes during developing LSDs that are extremely critical for many metabolic processes inside the various cells and tissues of affected persons. The data presented will help establish new complex strategies for metabolic correction of LSDs.

show abstract

Section: Discussionmentioning

confidence: 93%

Secondary biochemical and morphological consequences in lysosomal storage diseases

Alroy

Garganta

Wiederschain

2014

Biochemistry Moscow

View full text Add to dashboard Cite

show abstract

“…At the same time, it affects the function of proteins, such as glycosylation plays an important role in protein folding, transport and location [41,42]. According to the connection modes, it can be divided into four types: N-glycosylation, O-glycosylation, C-glycosylation and glycosylphosphatidylinositol (GPI) anchored connection [43,44]. FLT3 has been reported to be N-glycosylated in the endoplasmic reticulum [45][46][47], which may be due to the difficulty in O-glycosylation research.…”

Section: Flt3 Glycosylation In Endoplasmic Reticulummentioning

confidence: 99%

Targeting on glycosylation of mutant FLT3 in acute myeloid leukemia

Chen

2019

Hematology

View full text Add to dashboard Cite

Objective: To summarize the abnormal location of FLT3 caused by different glycosylation status which further leads to the distinguishing signaling pathways and discuss targeting on FLT3 glycosylation by drugs reported in recent literatures. Methods: We review FLT3 glycosylation in endoplasmic reticulum. The abnormal signal of mutant FLT3 with different glycosylation status is discussed. We also address potential FLT3 glycosylation-targeting strategies for the treatment. Results: Inhibition of FLT3 mutant cells by drugs reported in recent literatures involves the influence of glycosylation of FLT3: 2-deoxy-D-glucose, Tunicamycin and Fluvastatin are reported to inhibit N-glycosylation of FLT3; Pim-1 inhibitors are proved to block the inhibition of Pim-1 on FLT3 Oglycosylation; HSP90 inhibitors and Tyrosine Kinase Inhibitors are shown to increase fully glycosylated form of FLT3. Discussion: The FMS-like tyrosine kinase 3 (FLT3) gene expressed only in CD34+ progenitor cells in bone marrow is located on chromosome 13q12 encoding FLT3 protein. FLT3 is initially synthesized as a 110 KD protein, which glycosylated in the endoplasmic reticulum to a 130 KD immature protein rich in mannose, and further processed into a mature 160 KD protein in the Golgi apparatus, which could be transferred to the cell surface. Therapy targeting on FLT3 glycosylation is a promising direction for AML treatment. Conclusions: The abnormal location of FLT3 caused by different glycosylation status leads to the distinguishing signaling pathways. Targeting on FLT3 glycosylation may provide a new perspective for therapeutic strategies.

show abstract

“…Glycosylation of a protein imposes comprehensive effects on its folding, localization, trafficking, solubility, antigenicity and many other aspects, thus endows the modified protein with new functions [2]. Depending on the linkage between the amino acid and glycans, protein glycosylation are divided into four categories, namely N- linked glycosylation ( N -glycosylation), O-linked glycosylation, C-mannosylation and glycosylphosphatidylinositol (GPI) anchor attachments [2,3]. An analysis of the 75,000 glycosylated protein entries in SWISS-PROT estimated that N- glycosylated proteins accounted for over two thirds with a frequency of 3.1 sites per protein, representing the richest glycosylation type in eukaryotes [4].…”

Section: Introductionmentioning

confidence: 99%

“…Although the cellular machinery used to N- glycosylate is well conserved, the capacity to form hybrid or complex N- glycans does vary between species and between cell types [6]. N -glycosylation is involved in protein folding, ER-associated degradation and protein sorting, processes which underpin growth, development, morphogenesis and stress signaling [3,7–9]. In human, the aberrant status and structure of N- glycan in cell surface receptors have been associated with the cancer cell progression and metastasis [10].…”

Section: Introductionmentioning

confidence: 99%

Mapping the N-linked glycosites of rice (Oryza sativa L.) germinating embryos

et al. 2017

View full text Add to dashboard Cite

Germination is a key event in the angiosperm life cycle. N-glycosylation of proteins is one of the most common post-translational modifications, and has been recognized to be an important regulator of the proteome of the germinating embryo. Here, we report the first N-linked glycosites mapping of rice embryos during germination by using a hydrophilic interaction chromatography (HILIC) glycopeptides enrichment strategy associated with high accuracy mass spectrometry identification. A total of 242 glycosites from 191 unique proteins was discovered. Inspection of the motifs and sequence structures involved suggested that all the glycosites were concentrated within [NxS/T] motif, while 82.3% of them were in a coil structure. N-glycosylation preferentially occurred on proteins with glycoside hydrolase activities, which were significantly enriched in the starch and sucrose metabolism pathway, suggesting that N-glycosylation is involved in embryo germination by regulating carbohydrate metabolism. Notably, protein-protein interaction analysis revealed a network with several Brassinosteroids signaling proteins, including XIAO and other BR-responsive proteins, implying that glycosylation-mediated Brassinosteroids signaling may be a key mechanism regulating rice embryo germination. In summary, this study expanded our knowledge of protein glycosylation in rice, and provided novel insight into the PTM regulation in rice seed germination.

show abstract

Glycobiology: Progress, problems, and perspectives

Cited by 32 publications

References 87 publications

Secondary biochemical and morphological consequences in lysosomal storage diseases

Secondary biochemical and morphological consequences in lysosomal storage diseases

Targeting on glycosylation of mutant FLT3 in acute myeloid leukemia

Mapping the N-linked glycosites of rice (Oryza sativa L.) germinating embryos

Contact Info

Product

Resources

About