Roles for Golgi Glycans in Oogenesis and Spermatogenesis

Akintayo, Ayodele; Stanley, Pamela

doi:10.3389/fcell.2019.00098

Cited by 15 publications

(9 citation statements)

References 70 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…GAG chains can interact with a wide variety of signaling macromolecules to regulate fundamental biological processes [ 20 ] and, thus, bestow PGs with a plethora of structural and functional variations [ 18 ]. The glycosylation of PGs is initiated in the endoplasmic reticulum, further orchestrated in the Golgi apparatus, and is mostly mediated by glycosyltransferases that reside in this complex organelle [ 24 ].…”

Section: Proteoglycansmentioning

confidence: 99%

Proteoglycans in the Pathogenesis of Hormone-Dependent Cancers: Mediators and Effectors

Tzanakakis

Giatagana

Kuskov

et al. 2020

Cancers

View full text Add to dashboard Cite

Hormone-dependent cancers exhibit high morbidity and mortality. In spite of advances in therapy, the treatment of hormone-dependent cancers remains an unmet health need. The tumor microenvironment (TME) exhibits unique characteristics that differ among various tumor types. It is composed of cancerous, non-cancerous, stromal, and immune cells that are surrounded and supported by components of the extracellular matrix (ECM). Therefore, the interactions among cancer cells, stromal cells, and components of the ECM determine cancer progression and response to therapy. Proteoglycans (PGs), hybrid molecules consisting of a protein core to which sulfated glycosaminoglycan chains are bound, are significant components of the ECM that are implicated in all phases of tumorigenesis. These molecules, secreted by both the stroma and cancer cells, are crucial signaling mediators that modulate the vital cellular pathways implicated in gene expression, phenotypic versatility, and response to therapy in specific tumor types. A plethora of deregulated signaling pathways contributes to the growth, dissemination, and angiogenesis of hormone-dependent cancers. Specific inputs from the endocrine and immune systems are some of the characteristics of hormone-dependent cancer pathogenesis. Importantly, the mechanisms involved in various aspects of cancer progression are executed in the ECM niche of the TME, and the PG components crucially mediate these processes. Here, we comprehensively discuss the mechanisms through which PGs affect the multifaceted aspects of hormone-dependent cancer development and progression, including cancer metastasis, angiogenesis, immunobiology, autophagy, and response to therapy.

show abstract

Section: Proteoglycansmentioning

confidence: 99%

Proteoglycans in the Pathogenesis of Hormone-Dependent Cancers: Mediators and Effectors

Tzanakakis

Giatagana

Kuskov

et al. 2020

Cancers

View full text Add to dashboard Cite

show abstract

“…Glycans are one of the fundamental building blocks of the cell and play key roles in development and physiology (Bishop et al , 2007; Kohyama‐Koganeya et al , 2011; Ryczko et al , 2016; Varki, 2017; Akintayo & Stanley, 2019). Cellular glycan profiles are sensitive to changes in cell state and/or differentiation and are also important contributors to the process (Russo et al , 2018b).…”

Section: Introductionmentioning

confidence: 99%

GRASP55 regulates intra‐Golgi localization of glycosylation enzymes to control glycosphingolipid biosynthesis

et al. 2021

View full text Add to dashboard Cite

The Golgi apparatus, the main glycosylation station of the cell, consists of a stack of discontinuous cisternae. Glycosylation enzymes are usually concentrated in one or two specific cisternae along the cis‐trans axis of the organelle. How such compartmentalized localization of enzymes is achieved and how it contributes to glycosylation are not clear. Here, we show that the Golgi matrix protein GRASP55 directs the compartmentalized localization of key enzymes involved in glycosphingolipid (GSL) biosynthesis. GRASP55 binds to these enzymes and prevents their entry into COPI‐based retrograde transport vesicles, thus concentrating them in the trans‐Golgi. In genome‐edited cells lacking GRASP55, or in cells expressing mutant enzymes without GRASP55 binding sites, these enzymes relocate to the cis‐Golgi, which affects glycosphingolipid biosynthesis by changing flux across metabolic branch points. These findings reveal a mechanism by which a matrix protein regulates polarized localization of glycosylation enzymes in the Golgi and controls competition in glycan biosynthesis.

show abstract

“…Increasing evidence indicates that glycosylation plays an irreplaceable role in the whole process of spermatogenesis, maturation, capacitation , sperm–egg recognition, and final fertilization . Proteins are first assembled and modified with glycans in the endoplasmic reticulum/Golgi to finally form thick glycocalyx spermatozoa in the testes during spermatogenesis, while such spermatozoa with glycocalyx are insufficient to recognize and penetrate into the egg . Spermatozoa plasma membrane glycocalyx is necessary to be further modified through deglycosylation, glycosylation, and integration in epididymis to reach maturation .…”

Section: Introductionmentioning

confidence: 99%

Biological Functions and Large-Scale Profiling of Protein Glycosylation in Human Semen

et al. 2020

View full text Add to dashboard Cite

Glycosylation is one of the most important post-translational modifications of proteins and plays an essential role in spermatogenesis, maturation, extracellular quality control, capacitation, sperm−egg recognition, and final fertilization. Spermatozoa are synthesized in the testes inactively with a thick glycocalyx and passed through the epididymis for further modification by glycosylation, deglycosylation, and integration to reach maturation. Subsequently, sperm capacitation and further fertilization require redistribution of glycoconjugates and dramatic glycocalyx modification of the spermatozoa surface. Furthermore, glycoproteins and glycans in seminal plasma are functional in maintaining spermatozoa structure and stability. Therefore, aberrant glycosylation may cause alteration of semen function and even infertility. Currently, mass spectrometry-based technologies have allowed large-scale profiling of glycans and glycoproteins in human semen. Quantitative analysis of semen glycosylation has also indicated many involved glycoproteome issues in male infertility and the potential biomarkers for diagnosis of male infertility in clinical. This review summarizes the role of glycosylation during spermatozoa development, the large-scale profiling of glycome and glycoproteome in human semen, as well as the association of aberrant glycosylation with infertility.

show abstract

Roles for Golgi Glycans in Oogenesis and Spermatogenesis

Cited by 15 publications

References 70 publications

Proteoglycans in the Pathogenesis of Hormone-Dependent Cancers: Mediators and Effectors

Proteoglycans in the Pathogenesis of Hormone-Dependent Cancers: Mediators and Effectors

GRASP55 regulates intra‐Golgi localization of glycosylation enzymes to control glycosphingolipid biosynthesis

Biological Functions and Large-Scale Profiling of Protein Glycosylation in Human Semen

Contact Info

Product

Resources

About