Algorithm for Modern Electron Microscopic Examination of the Golgi Complex

Mirоnоv, Alexander A.; Beznoussenko, Galina V.

doi:10.1007/978-1-0716-2639-9_12

Cited by 5 publications

(5 citation statements)

References 161 publications

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“…Additionally, we did not find clathrin-coated buds on APM goblet cells. Moreover, our study of the images presented by Gustafsson et al [26] showed that, on all of them, these secreted structures looked similar to autophagosomes of multilayer bodies involved in the early formation of autophagosomes [81,82].…”

Section: The Role Of the Apical Endocytosis In Goblet Cellsmentioning

confidence: 61%

The Regulated Secretion and Models of Intracellular Transport: The Goblet Cell as an Example

Mirоnоv

Beznoussenko

2023

IJMS

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Transport models are extremely important to map thousands of proteins and their interactions inside a cell. The transport pathways of luminal and at least initially soluble secretory proteins synthesized in the endoplasmic reticulum can be divided into two groups: the so-called constitutive secretory pathway and regulated secretion (RS) pathway, in which the RS proteins pass through the Golgi complex and are accumulated into storage/secretion granules (SGs). Their contents are released when stimuli trigger the fusion of SGs with the plasma membrane (PM). In specialized exocrine, endocrine, and nerve cells, the RS proteins pass through the baso-lateral plasmalemma. In polarized cells, the RS proteins secrete through the apical PM. This exocytosis of the RS proteins increases in response to external stimuli. Here, we analyze RS in goblet cells to try to understand the transport model that can be used for the explanation of the literature data related to the intracellular transport of their mucins.

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Section: The Role Of the Apical Endocytosis In Goblet Cellsmentioning

confidence: 61%

The Regulated Secretion and Models of Intracellular Transport: The Goblet Cell as an Example

Mirоnоv

Beznoussenko

2023

IJMS

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“…Therefore, if a protein with one or more glycans is created, each glycan has a 50% chance to either have a Man8GlcNAc2 or a Man9GlcNAc2 structure. Species of monosaccharides and their potential bonding partners through the available sugar bonds [27] and a flow chart for the resulting process of glycosylation. Figure 5.…”

Section: Structure Of the Glycansmentioning

confidence: 99%

“…Although many studies of the Golgi apparatus structure have been performed by light and electron microscopy, the full shape of the Golgi apparatus remains mostly unclear due to the technical limitations of the applied microscopy techniques. However, recent advances in microscopy technology, such as the use of high-power magnification, cryo-electron microscopy and 3D electron tomography, allow a general understanding of the dimensions and structures of the Golgi apparatus [27,28]. Microscopic images of the Golgi apparatus show an average diameter of 500 nm for a cisterna [29].…”

Section: The Environment: the Golgi Apparatusmentioning

confidence: 99%

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Implementing an Agent-Based Modeling Approach for Protein Glycosylation in the Golgi Apparatus

Jetschni,

Götz

2023

Fermentation

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Glycoproteins are involved in various significant biological processes and have critical biological functions in physiology and pathology by regulating biological activities and molecular signaling pathways. The variety of enzymes used in protein glycosylation and the wide range of diversity in the resulting glycoproteins pose a challenging task when attempting to simulate these processes in silico. This study aimed to establish and define the necessary structures to simulate the process of N-glycosylation in silico. In this article, we represent the process of glycosylation in the Golgi structure in an agent-based model with defined movement patterns and reaction rules between the associated proteins and enzymes acting as agents. The Golgi structure is converted into a grid consisting of 150 × 400 patches representing four compartments which contain a specific distribution of the fundamental enzymes contributing to the process of glycosylation. The interacting glycoproteins and membrane-bound enzymes are perceived as agents, with their own rules for movement, complex formation, biochemical reaction and dissociation. The resulting structures were saved into an XML-format, a mass spectrometry file and a GlycoWorkbench2-compatible file for visualization.

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“…Glycosylation depends not only on the presence of glycosyltransferases in cells, but also on their localisation in the GC; the availability of nucleotide sugar transporters, which should localise nearby, as donors of nucleotide sugars are necessary for their synthesis; the final destination of the glycoprotein or lipid; as well as the action of decomposing glycosydases that cleave glycans. The structure of the GC varies significantly depending on the functional state and cell phase [113,[118][119][120]. Although GTA and GTB are mostly located at the trans-side of the medial GC in goblet cells, these enzymes were found throughout the Golgi stack in enterocytes containing microvilli [47].…”

Section: Golgi Glycosylation Mistakesmentioning

confidence: 99%

Mechanisms of Formation of Antibodies against Blood Group Antigens That Do Not Exist in the Body

Mironov,

Savin,

Zaitseva

et al. 2023

IJMS

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The system of the four different human blood groups is based on the oligosaccharide antigens A or B, which are located on the surface of blood cells and other cells including endothelial cells, attached to the membrane proteins or lipids. After transfusion, the presence of these antigens on the apical surface of endothelial cells could induce an immunological reaction against the host. The final oligosaccharide sequence of AgA consists of Gal-GlcNAc-Gal (GalNAc)-Fuc. AgB contains Gal-GlcNAc-Gal (Gal)-Fuc. These antigens are synthesised in the Golgi complex (GC) using unique Golgi glycosylation enzymes (GGEs). People with AgA also synthesise antibodies against AgB (group A [II]). People with AgB synthesise antibodies against AgA (group B [III]). People expressing AgA together with AgB (group AB [IV]) do not have these antibodies, while people who do not express these antigens (group O [0; I]) synthesise antibodies against both antigens. Consequently, the antibodies are synthesised against antigens that apparently do not exist in the body. Here, we compared the prediction power of the main hypotheses explaining the formation of these antibodies, namely, the concept of natural antibodies, the gut bacteria-derived antibody hypothesis, and the antibodies formed as a result of glycosylation mistakes or de-sialylation of polysaccharide chains. We assume that when the GC is overloaded with lipids, other less specialised GGEs could make mistakes and synthesise the antigens of these blood groups. Alternatively, under these conditions, the chylomicrons formed in the enterocytes may, under this overload, linger in the post-Golgi compartment, which is temporarily connected to the endosomes. These compartments contain neuraminidases that can cleave off sialic acid, unmasking these blood antigens located below the acid and inducing the production of antibodies.

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Algorithm for Modern Electron Microscopic Examination of the Golgi Complex

Cited by 5 publications

References 161 publications

The Regulated Secretion and Models of Intracellular Transport: The Goblet Cell as an Example

The Regulated Secretion and Models of Intracellular Transport: The Goblet Cell as an Example

Implementing an Agent-Based Modeling Approach for Protein Glycosylation in the Golgi Apparatus

Mechanisms of Formation of Antibodies against Blood Group Antigens That Do Not Exist in the Body

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