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Cells
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Glycosylation and Deglycosylation in Animal Development
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Glycosylation and Deglycosylation in Animal Development

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Proliferation and Division".

Deadline for manuscript submissions: closed (31 August 2021) | Viewed by 26559

Special Issue Editor

Dr. Hamed Jafar-Nejad

E-Mail Website
Guest Editor
Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA
Interests: glycosylation; N-glycanase 1; Notch signaling; BMP signaling; AMPK signaling
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Over the last two decades, it has become clear that glycosylation, which is the addition of carbohydrates to proteins and other biological molecules, plays critical roles in animal development. At least 1 in 50 human genes encodes proteins that directly or indirectly contribute to glycosylation. Moreover, it is estimated that around half of the proteins in a given cell are glycosylated. In keeping with these numbers, mutations in genes involved in glycosylation and deglycosylation play a causative role in more than 130 human diseases, affecting various tissues and organ systems. Importantly, new techniques in molecular biology, genetics, and genome engineering have helped scientists to identify specific roles for multiple forms of glycosylation in modulating the activity of various developmental signaling pathways. In addition, advances in glycomics and glycoproteomics have increasingly enabled us to learn the proteome-wide and protein/site-specific distribution of glycans in various cell types in health and disease. As a result, the field of developmental glycobiology has shown a rapid growth in recent years, both in terms of number of papers published and in terms of the depth of analysis now possible in these studies. The present Special Issue aims to highlight some of the major advances in this field. Contributions to this collection can be primary research articles or review articles discussing how the addition or removal of glycans from proteins or lipids can impact metazoan development and/or human diseases. I invite colleagues to submit articles covering the roles of glycans as seen through the lenses of structural biology, cellular biology, model organisms, and/or human disease pathophysiology.

Dr. Hamed Jafar-Nejad
Guest Editor

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

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Keywords

  • developmental biology
  • developmental signaling pathways
  • N-glycan
  • O-glycan
  • proteoglycan
  • C-mannosylation
  • glycolipid
  • nucleocytoplasmic glycosylation
  • deglycosylation
  • lectin
  • model organism research
  • congenital disorders of glycosylation
  • glycosyltransferase
  • glycosyl hydrolase
  • nucleotide sugar transporter
  • mass spectrometry
  • structural biology

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Published Papers (6 papers)

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Research

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13 pages, 1700 KiB  
Article
Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes
by Ilhan Akan, Adnan Halim, Sergey Y. Vakhrushev, Henrik Clausen and John A. Hanover
Cells 2021, 10(5), 1026; https://doi.org/10.3390/cells10051026 - 27 Apr 2021
Cited by 6 | Viewed by 3149
Abstract
The reversible posttranslational O-GlcNAc modification of serine or threonine residues of intracellular proteins is involved in many cellular events from signaling cascades to epigenetic and transcriptional regulation. O-GlcNAcylation is a conserved nutrient-dependent process involving two enzymes, with O-GlcNAc transferase (OGT) [...] Read more.
The reversible posttranslational O-GlcNAc modification of serine or threonine residues of intracellular proteins is involved in many cellular events from signaling cascades to epigenetic and transcriptional regulation. O-GlcNAcylation is a conserved nutrient-dependent process involving two enzymes, with O-GlcNAc transferase (OGT) adding O-GlcNAc and with O-GlcNAcase (OGA) removing it in a manner that’s protein- and context-dependent. O-GlcNAcylation is essential for epigenetic regulation of gene expression through its action on Polycomb and Trithorax and COMPASS complexes. However, the important role of O-GlcNAc in adult life and health span has been largely unexplored, mainly due the lack of available model systems. Cataloging the O-GlcNAc proteome has proven useful in understanding the biology of this modification in vivo. In this study, we leveraged a recently developed oga knockout fly mutant to identify the O-GlcNAcylated proteins in adult Drosophilamelanogaster. The adult O-GlcNAc proteome revealed many proteins related to cell and organismal growth, development, differentiation, and epigenetics. We identified many O-GlcNAcylated proteins that play a role in increased growth and decreased longevity, including HCF, SIN3A, LOLA, KISMET, ATX2, SHOT, and FOXO. Interestingly, oga mutant flies are larger and have a shorter life span compared to wild type flies, suggesting increased O-GlcNAc results in increased growth. Our results suggest that O-GlcNAc alters the function of many proteins related to transcription, epigenetic modification and signaling pathways that regulate growth rate and longevity. Therefore, our findings highlight the importance of O-GlcNAc in growth and life span in adult Drosophila. Full article
(This article belongs to the Special Issue Glycosylation and Deglycosylation in Animal Development)
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17 pages, 2507 KiB  
Article
Placental Glycoredox Dysregulation Associated with Disease Progression in an Animal Model of Superimposed Preeclampsia
by Sandra M. Blois, Paula D. Prince, Sophia Borowski, Monica Galleano and Gabriela Barrientos
Cells 2021, 10(4), 800; https://doi.org/10.3390/cells10040800 - 3 Apr 2021
Cited by 9 | Viewed by 2490
Abstract
Pregnancies carried by women with chronic hypertension are at increased risk of superimposed preeclampsia, but the placental pathways involved in disease progression remain poorly understood. In this study, we used the stroke-prone spontaneously hypertensive rat (SHRSP) model to investigate the placental mechanisms promoting [...] Read more.
Pregnancies carried by women with chronic hypertension are at increased risk of superimposed preeclampsia, but the placental pathways involved in disease progression remain poorly understood. In this study, we used the stroke-prone spontaneously hypertensive rat (SHRSP) model to investigate the placental mechanisms promoting superimposed preeclampsia, with focus on cellular stress and its influence on galectin–glycan circuits. Our analysis revealed that SHRSP placentas are characterized by a sustained activation of the cellular stress response, displaying significantly increased levels of markers of lipid peroxidation (i.e., thiobarbituric acid reactive substances (TBARS)) and protein nitration and defective antioxidant enzyme expression as early as gestation day 14 (which marks disease onset). Further, lectin profiling showed that such redox imbalance was associated with marked alterations of the placental glycocode, including a prominent decrease of core 1 O-glycan expression in trophoblasts and increased decidual levels of sialylation in SHRSP placentas. We also observed significant changes in the expression of galectins 1, 3 and 9 with pregnancy progression, highlighting the important role of the galectin signature as dynamic interpreters of placental microenvironmental challenges. Collectively, our findings uncover a new role for the glycoredox balance in the pathogenesis of superimposed preeclampsia representing a promising target for interventions in hypertensive disorders of pregnancy. Full article
(This article belongs to the Special Issue Glycosylation and Deglycosylation in Animal Development)
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8 pages, 4683 KiB  
Communication
Induction of CXCL10-Mediated Cell Migration by Different Types of Galectins
by Dina B. AbuSamra, Noorjahan Panjwani and Pablo Argüeso
Cells 2021, 10(2), 274; https://doi.org/10.3390/cells10020274 - 30 Jan 2021
Cited by 1 | Viewed by 2727
Abstract
Chemokines are an extended group of chemoattractant cytokines responsible for the recruitment of leukocytes into tissues. Among them, interferon-γ-inducible protein 10 (CXCL10) is abundantly expressed following inflammatory stimuli and participates in the trafficking of monocytes and activated T cells into sites of injury. [...] Read more.
Chemokines are an extended group of chemoattractant cytokines responsible for the recruitment of leukocytes into tissues. Among them, interferon-γ-inducible protein 10 (CXCL10) is abundantly expressed following inflammatory stimuli and participates in the trafficking of monocytes and activated T cells into sites of injury. Here, we report that different members of the galectin family of carbohydrate-binding proteins promote the expression and synthesis of CXCL10 independently of interferon-γ. Interestingly, CXCL10 induction was observed when galectins came in contact with stromal fibroblasts isolated from human cornea but not other cell types such as epithelial, monocytic or endothelial cells. Induction of CXCL10 by the tandem repeat galectin-8 was primarily associated with the chemotactic migration of THP-1 monocytic cells, whereas the prototype galectin-1 promoted the CXCL10-dependent migration of Jurkat T cells. These results highlight the potential importance of the galectin signature in dictating the recruitment of specific leukocyte populations into precise tissue locations. Full article
(This article belongs to the Special Issue Glycosylation and Deglycosylation in Animal Development)
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Review

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35 pages, 8787 KiB  
Review
NGLY1 Deficiency, a Congenital Disorder of Deglycosylation: From Disease Gene Function to Pathophysiology
by Ashutosh Pandey, Joshua M. Adams, Seung Yeop Han and Hamed Jafar-Nejad
Cells 2022, 11(7), 1155; https://doi.org/10.3390/cells11071155 - 29 Mar 2022
Cited by 19 | Viewed by 5608
Abstract
N-Glycanase 1 (NGLY1) is a cytosolic enzyme involved in removing N-linked glycans of misfolded N-glycoproteins and is considered to be a component of endoplasmic reticulum-associated degradation (ERAD). The 2012 identification of recessive NGLY1 mutations in a rare multisystem disorder has [...] Read more.
N-Glycanase 1 (NGLY1) is a cytosolic enzyme involved in removing N-linked glycans of misfolded N-glycoproteins and is considered to be a component of endoplasmic reticulum-associated degradation (ERAD). The 2012 identification of recessive NGLY1 mutations in a rare multisystem disorder has led to intense research efforts on the roles of NGLY1 in animal development and physiology, as well as the pathophysiology of NGLY1 deficiency. Here, we present a review of the NGLY1-deficient patient phenotypes, along with insights into the function of this gene from studies in rodent and invertebrate animal models, as well as cell culture and biochemical experiments. We will discuss critical processes affected by the loss of NGLY1, including proteasome bounce-back response, mitochondrial function and homeostasis, and bone morphogenetic protein (BMP) signaling. We will also cover the biologically relevant targets of NGLY1 and the genetic modifiers of NGLY1 deficiency phenotypes in animal models. Together, these discoveries and disease models have provided a number of avenues for preclinical testing of potential therapeutic approaches for this disease. Full article
(This article belongs to the Special Issue Glycosylation and Deglycosylation in Animal Development)
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26 pages, 1295 KiB  
Review
Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation
by Zinia D’Souza, Farhana Taher Sumya, Amrita Khakurel and Vladimir Lupashin
Cells 2021, 10(12), 3275; https://doi.org/10.3390/cells10123275 - 23 Nov 2021
Cited by 8 | Viewed by 4729
Abstract
The Golgi is the central organelle of the secretory pathway and it houses the majority of the glycosylation machinery, which includes glycosylation enzymes and sugar transporters. Correct compartmentalization of the glycosylation machinery is achieved by retrograde vesicular trafficking as the secretory cargo moves [...] Read more.
The Golgi is the central organelle of the secretory pathway and it houses the majority of the glycosylation machinery, which includes glycosylation enzymes and sugar transporters. Correct compartmentalization of the glycosylation machinery is achieved by retrograde vesicular trafficking as the secretory cargo moves forward by cisternal maturation. The vesicular trafficking machinery which includes vesicular coats, small GTPases, tethers and SNAREs, play a major role in coordinating the Golgi trafficking thereby achieving Golgi homeostasis. Glycosylation is a template-independent process, so its fidelity heavily relies on appropriate localization of the glycosylation machinery and Golgi homeostasis. Mutations in the glycosylation enzymes, sugar transporters, Golgi ion channels and several vesicle tethering factors cause congenital disorders of glycosylation (CDG) which encompass a group of multisystem disorders with varying severities. Here, we focus on the Golgi vesicle tethering and fusion machinery, namely, multisubunit tethering complexes and SNAREs and their role in Golgi trafficking and glycosylation. This review is a comprehensive summary of all the identified CDG causing mutations of the Golgi trafficking machinery in humans. Full article
(This article belongs to the Special Issue Glycosylation and Deglycosylation in Animal Development)
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16 pages, 1075 KiB  
Review
Glycosylation of Immune Receptors in Cancer
by Ruoxuan Sun, Alyssa Min Jung Kim and Seung-Oe Lim
Cells 2021, 10(5), 1100; https://doi.org/10.3390/cells10051100 - 4 May 2021
Cited by 37 | Viewed by 6981
Abstract
Evading host immune surveillance is one of the hallmarks of cancer. Immune checkpoint therapy, which aims to eliminate cancer progression by reprogramming the antitumor immune response, currently occupies a solid position in the rapidly expanding arsenal of cancer therapy. As most immune checkpoints [...] Read more.
Evading host immune surveillance is one of the hallmarks of cancer. Immune checkpoint therapy, which aims to eliminate cancer progression by reprogramming the antitumor immune response, currently occupies a solid position in the rapidly expanding arsenal of cancer therapy. As most immune checkpoints are membrane glycoproteins, mounting attention is drawn to asking how protein glycosylation affects immune function. The answers to this fundamental question will stimulate the rational development of future cancer diagnostics and therapeutic strategies. Full article
(This article belongs to the Special Issue Glycosylation and Deglycosylation in Animal Development)
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