Targeting cancer via Golgi α-mannosidase II inhibition: How far have we come in developing effective inhibitors?

Lee, Zheng Yang; Loo, Jason Siau Ee; Wibowo, Agustono; Mohammat, Mohd Fazli; Foo, Jhi Biau

doi:10.1016/j.carres.2021.108395

Cited by 17 publications

(12 citation statements)

References 116 publications

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“…Molecular docking and QM/MM geometry optimization. The X-ray structure of dGMII (PDB ID: 3BLB) 25,34 was used as a model of Golgi α-mannosidase II because of high sequence identity and similarity 15 of the active site to human (hGMII), and Caenorhabditis elegans Golgi α-mannosidase 35 (AMAN-2, used in inhibitory assays in this work). In Fig.…”

Section: Molecular Modelingmentioning

confidence: 99%

“…1) [10][11][12][13][14] and the relevant literature has been reviewed in detail. [15][16][17][18] Other types of promising α-glycosidase inhibitors are multivalent compounds 19,20 and allosteric-site inhibitors. 21 Golgi α-mannosidase II (GMII, E.C.3.2.1.114), a transmembrane protein encoded by the MAN2A1 gene in mammals, 22 catalyzes sequential trimming of two mannosyl residues from high-mannose N-glycans (from GlcNAcMan 5 GlcNAc 2 to GlcNAcMan 3 GlcNAc 2 ) in the biosynthesis of complex N-glycans in the Golgi apparatus.…”

Section: Introductionmentioning

confidence: 99%

“…3 Based on the available X-ray structures of GH38 enzymes, dGMII, 18,[25][26][27][28][29] bovine lysosomal α-mannosidase II (bLMan) 30 and plant jack bean α-mannosidase (JBMan), 31 the active sites of Golgi and acidic α-mannosidases are structurally identical, approximately 6 Å around the Zn 2+ ion. 15,21 However, the protonation forms of ionizable amino acids, such as Asp, Glu, His or Arg, are not revealed from the X-ray data. Because the enzymes work under different pH conditions the amino acid residues placed in the same position in the active sites of the enzymes do not need to have the same protonation form.…”

Section: Introductionmentioning

confidence: 99%

“…1) 10–14 and the relevant literature has been reviewed in detail. 15–18 Other types of promising α-glycosidase inhibitors are multivalent compounds 19,20 and allosteric-site inhibitors. 21…”

Section: Introductionmentioning

confidence: 99%

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1,4-Dideoxy-1,4-imino-d- andl-lyxitol-based inhibitors bind to Golgi α-mannosidase II in different protonation forms

et al. 2022

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Section: Molecular Modelingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

1,4-Dideoxy-1,4-imino-d- andl-lyxitol-based inhibitors bind to Golgi α-mannosidase II in different protonation forms

et al. 2022

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“…It is composed of many different classes, including -Mannosidases I, -Mannosidases II, and unclassified -Mannosidase [14]. Evidence indicating alphamannosidase has a role in the progression of cancer has been accumulating steadily over the years [15][16][17]. However, the potential function of MAN1B1 in tumors was rarely reported.…”

Section: Introductionmentioning

confidence: 99%

Identification of MAN1B1 as a Novel Marker for Bladder Cancer and Its Relationship with Immune Cell Infiltration

Wang

Chen

Cao

et al. 2022

Journal of Oncology

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Bladder cancer (BC) is a common malignant tumor of the genitourinary system, and there are not enough tumor biomarker tests that are specific, trustworthy, and noninvasive for the diagnosis and prognosis. The purpose of this study is to investigate the clinical relevance, prognostic value, and immunological signature of Mannosidase alpha class 1B member 1(MAN1B1) expressions in BC. The Cancer Genome Atlas (TCGA) and Genotype-Tissue Expression (GTEx) databases provided the raw information that was used to analyze the expression of MAN1B1 in tumor patients. Then, a statistical study was carried out to assess the correlations of MAN1B1 expression with the clinical characteristics and the prognosis of BC. The correlation between MAN1B1 expression and tumor immune infiltration was explored via single-sample gene set enrichment analysis (ssGSEA). In human cancers, MAN1B1 expressions were shown to be generally higher in tumors than in normal specimens. We confirmed that MAN1B1 expression was distinctly increased in BC specimens compared with nontumor specimens. BC specimens with advanced T stage and M stage showed a higher level of MAN1B1. Survival analysis revealed that the overall survival (OS), disease-specific survival (DSS), and progression-free interval (PFI) of patients with high MAN1B1 expressions were distinctly worse than those with low MAN1B1 expressions. Importantly, multivariate analyses only confirmed that MAN1B1 expression was an independent prognostic factor for OS of the patients with BC. Furthermore, we observed that MAN1B1 expression level was significantly correlated with abundance of multiple immune infiltrates including Th2 cells, macrophages, Th1 cells, neutrophils, T helper cells, and NK CD56 bright cells. In conjunction with all of these findings, elevated MAN1B1 expression is associated with a poor prognosis and a higher number of immune cells in BC. MAN1B1 has the potential to act as a biomarker that can evaluate both the patient’s prognosis and the degree of immune infiltration in BC.

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Functional Materials for Subcellular Targeting Strategies in Cancer Therapy: Progress and Prospects

Cheng,

Qu,

Jiang

et al. 2023

Advanced Materials

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Neoadjuvant and adjuvant therapies have made significant progress in cancer treatment. However, tumor adjuvant therapy still faces challenges due to the intrinsic heterogeneity of cancer, genomic instability, and the formation of an immunosuppressive tumor microenvironment. Functional materials possess unique biological properties such as long circulation times, tumor‐specific targeting, and immunomodulation. The combination of functional materials with natural substances and nanotechnology has led to the development of smart biomaterials with multiple functions, high biocompatibilities, and negligible immunogenicities, which can be used for precise cancer treatment. Recently, subcellular structure‐targeting functional materials have received particular attention in various biomedical applications including the diagnosis, sensing, and imaging of tumors and drug delivery. Subcellular organelle‐targeting materials can precisely accumulate therapeutic agents in organelles, considerably reduce the threshold dosages of therapeutic agents, and minimize drug‐related side effects. This review provides a systematic and comprehensive overview of the research progress in subcellular organelle‐targeted cancer therapy based on functional nanomaterials. Moreover, it explains the challenges and prospects of subcellular organelle‐targeting functional materials in precision oncology. We believe that our review will serve as an excellent cutting‐edge guide for researchers in the field of subcellular organelle‐targeted cancer therapy.This article is protected by copyright. All rights reserved

show abstract

Targeting cancer via Golgi α-mannosidase II inhibition: How far have we come in developing effective inhibitors?

Cited by 17 publications

References 116 publications

1,4-Dideoxy-1,4-imino-d- andl-lyxitol-based inhibitors bind to Golgi α-mannosidase II in different protonation forms

1,4-Dideoxy-1,4-imino-d- andl-lyxitol-based inhibitors bind to Golgi α-mannosidase II in different protonation forms

Identification of MAN1B1 as a Novel Marker for Bladder Cancer and Its Relationship with Immune Cell Infiltration

Functional Materials for Subcellular Targeting Strategies in Cancer Therapy: Progress and Prospects

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