Identifying N-linked glycan moiety and motifs in the cysteine-rich domain critical for N-glycosylation and intracellular trafficking of SR-AI and MARCO

Tsay, Huey Jen; Huang, Yung Cheng; Chen, Yi Jen; Lee, Yun Hao; Hsu, Shu Meng; Tsai, Keng‐Chang; Yang, Cheng; Huang, Fong Lee; Shie, Feng Shiun; Lee, Lin Chien; Shiao, Young‐Ji

doi:10.1186/s12929-016-0244-5

Cited by 9 publications

(5 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Glycans attached to proteins are closely related to protein stability, trafficking, signaling, and cell–cell interaction . N-linked glycosylation of proteins, one of the most prevalent post-translational modifications in eukaryotes, significantly affects protein folding, stability, and function. , However, the heterogeneity of N-glycan in natural and recombinant glycoproteins greatly hampered the investigation of the roles of glycan in various biological processes.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Site-Directed Glycosylation of Peptide/Protein with Homogeneous O-Linked Eukaryotic N-Glycans

Jiang

Zhu

et al. 2016

Bioconjugate Chem.

View full text Add to dashboard Cite

Here we report a facile and efficient method for site-directed glycosylation of peptide/protein. The method contains two sequential steps: generation of a GlcNAc-O-peptide/protein, and subsequent ligation of a eukaryotic N-glycan to the GlcNAc moiety. A pharmaceutical peptide, glucagon-like peptide-1 (GLP-1), and a model protein, bovine α-Crystallin, were successfully glycosylated using such an approach. It was shown that the GLP-1 with O-linked N-glycan maintained an unchanged secondary structure after glycosylation, suggesting the potential application of this approach for peptide/protein drug production. In summary, the coupled approach provides a general strategy to produce homogeneous glycopeptide/glycoprotein bearing eukaryotic N-glycans.

show abstract

mentioning

confidence: 99%

“…G lycans attached to proteins are closely related to protein stability, 1 trafficking, 2 signaling, 3 and cell−cell interaction. 4 N-linked glycosylation of proteins, one of the most prevalent post-translational modifications in eukaryotes, significantly affects protein folding, stability, and function.…”

mentioning

confidence: 99%

Site-Directed Glycosylation of Peptide/Protein with Homogeneous O-Linked Eukaryotic N-Glycans

Jiang

Zhu

et al. 2016

Bioconjugate Chem.

View full text Add to dashboard Cite

show abstract

“…To determine the binding region of MARCO-TST necessary for its association with PLOD2, we obtained a series of MARCO-TST truncation mutants ( SI Appendix , Fig. S6 E , Upper Panel ) according to the domains of MARCO ( 30 ). We found that the transmembrane domain of MARCO-TST was the major region binding to PLOD2 ( SI Appendix , Fig.…”

Section: Resultsmentioning

confidence: 99%

Superenhancer drives a tumor-specific splicing variant of MARCO to promote triple-negative breast cancer progression

Yang

Jin

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The transcription variation, leading to various forms of transcripts and protein diversity, remains largely unexplored in triple-negative breast cancers (TNBCs). Here, we presented a comprehensive analysis of RNA splicing in breast cancer to illustrate the biological function and clinical implications of tumor-specific transcripts (TSTs) arising from these splicing junctions. Aberrant RNA splicing or TSTs were frequently harbored in TNBC and were correlated with a poor outcome. We discovered a tumor-specific splicing variant of macrophage receptor with collagenous structure–TST (MARCO-TST), which was distinguished from myeloid cell-specific wild-type MARCO. MARCO-TST expression was associated with poor outcomes in TNBC patients and could promote tumor progression in vitro and in vivo. Mechanically, MARCO-TST interacted with PLOD2 and enhanced the stability of HIF-1α, which resulted in the metabolic dysregulation of TNBC to form a hypoxic tumor microenvironment. MARCO-TST was initiated from a de novo alternative transcription initiation site that was activated by a superenhancer. Tumors with MARCO-TST expression conferred greater sensitivity to bromodomain and extraterminal protein inhibitors. This treatment strategy was further validated in patient-derived organoids. In conclusion, our results revealed the transcription variation landscape of TNBC, highlighting MARCO-TST as a crucial oncogenic transcript and therapeutic target.

show abstract

“…Based on their protein sequence, SRs are classified into 10 families (A-J). It has been shown that scavenger receptor class A (SR-A) and class B type 1 (SR-B1), as well as CD36 participate in Aβ clearance [252–254]. SR-A which is expressed on microglial cells and macrophages is implicated in Aβ phagocytosis [255].…”

Section: Receptor-mediated Aβ Phagocytosismentioning

confidence: 99%

Potential microRNA-related targets in clearance pathways of amyloid-β: novel therapeutic approach for the treatment of Alzheimer’s disease

et al. 2019

View full text Add to dashboard Cite

Imbalance between amyloid-beta (Aβ) peptide synthesis and clearance results in Aβ deregulation. Failure to clear these peptides appears to cause the development of Alzheimer’s disease (AD). In recent years, microRNAs have become established key regulators of biological processes that relate among others to the development and progression of neurodegenerative diseases, such as AD. This review article gives an overview on microRNAs that are involved in the Aβ cascade and discusses their inhibitory impact on their target mRNAs whose products participate in Aβ clearance. Understanding of the mechanism of microRNA in the associated signal pathways could identify novel therapeutic targets for the treatment of AD.

show abstract

Identifying N-linked glycan moiety and motifs in the cysteine-rich domain critical for N-glycosylation and intracellular trafficking of SR-AI and MARCO

Cited by 9 publications

References 33 publications

Site-Directed Glycosylation of Peptide/Protein with Homogeneous O-Linked Eukaryotic N-Glycans

Site-Directed Glycosylation of Peptide/Protein with Homogeneous O-Linked Eukaryotic N-Glycans

Superenhancer drives a tumor-specific splicing variant of MARCO to promote triple-negative breast cancer progression

Potential microRNA-related targets in clearance pathways of amyloid-β: novel therapeutic approach for the treatment of Alzheimer’s disease

Contact Info

Product

Resources

About