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Article ; Online: Three-dimensional organization of transzonal projections and other cytoplasmic extensions in the mouse ovarian follicle.

Baena, Valentina / Terasaki, Mark

2019 Volume 9, Issue 1, Page(s) 1262

Abstract: Each mammalian oocyte is nurtured by its own multi-cellular structure, the ovarian follicle. We used new methods for serial section electron microscopy to examine entire cumulus and mural granulosa cells and their projections in mouse antral ovarian ... ...

Abstract	Each mammalian oocyte is nurtured by its own multi-cellular structure, the ovarian follicle. We used new methods for serial section electron microscopy to examine entire cumulus and mural granulosa cells and their projections in mouse antral ovarian follicles. Transzonal projections (TZPs) are thin cytoplasmic projections that connect cumulus cells to the oocyte and are crucial for normal oocyte development. We studied these projections in detail and found that most TZPs do not reach the oocyte, and that they often branch and make gap junctions with each other. Furthermore, the TZPs that connect to the oocyte are usually contacted on their shaft by oocyte microvilli. Mural granulosa cells were found to possess randomly oriented cytoplasmic projections that are strikingly similar to the free-ended TZPs. We propose that granulosa cells use cytoplasmic projections to search for the oocyte, and cumulus cell differentiation results from a contact-mediated paracrine interaction with the oocyte.
MeSH term(s)	Animals ; Cell Communication ; Cell Surface Extensions/ultrastructure ; Cumulus Cells/cytology ; Cumulus Cells/ultrastructure ; Cytoplasm/ultrastructure ; Female ; Gap Junctions/ultrastructure ; Granulosa Cells/cytology ; Granulosa Cells/ultrastructure ; Mice/anatomy & histology ; Mice, Inbred C57BL ; Microscopy, Electron ; Microvilli/ultrastructure ; Oocytes/cytology ; Ovarian Follicle/cytology ; Ovarian Follicle/ultrastructure ; Pseudopodia/ultrastructure
Language	English
Publishing date	2019-02-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-018-37766-2
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Ultrastructural Analysis of Cell-Cell Interactions in Drosophila Ovary.

Antel, Matthew / Baena, Valentina / Terasaki, Mark / Inaba, Mayu

Methods in molecular biology (Clifton, N.J.)

2020 Volume 2346, Page(s) 79–90

Abstract: The Drosophila ovary is an exceptional model for studying cell-cell interactions in vivo. Cells communicate with each other in a highly coordinated manner. Accurate spatiotemporal regulation of cell-cell interaction is critical for the development of ... ...

Abstract	The Drosophila ovary is an exceptional model for studying cell-cell interactions in vivo. Cells communicate with each other in a highly coordinated manner. Accurate spatiotemporal regulation of cell-cell interaction is critical for the development of eggs. Ultrastructural analysis using electron microscopy (EM) permits the visualization of both cells and subcellular signaling structures with high resolution. Here we describe a method for the processing of intact fly ovaries by scanning electron microscopy (SEM).
MeSH term(s)	Animals ; Cell Communication ; Drosophila ; Female ; Ovary/cytology ; Ovary/ultrastructure
Language	English
Publishing date	2020-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/7651_2020_342
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Article ; Online: Three-dimensional organization of transzonal projections and other cytoplasmic extensions in the mouse ovarian follicle

Valentina Baena / Mark Terasaki

Scientific Reports, Vol 9, Iss 1, Pp 1-

2019 Volume 13

Abstract: Abstract Each mammalian oocyte is nurtured by its own multi-cellular structure, the ovarian follicle. We used new methods for serial section electron microscopy to examine entire cumulus and mural granulosa cells and their projections in mouse antral ... ...

Abstract	Abstract Each mammalian oocyte is nurtured by its own multi-cellular structure, the ovarian follicle. We used new methods for serial section electron microscopy to examine entire cumulus and mural granulosa cells and their projections in mouse antral ovarian follicles. Transzonal projections (TZPs) are thin cytoplasmic projections that connect cumulus cells to the oocyte and are crucial for normal oocyte development. We studied these projections in detail and found that most TZPs do not reach the oocyte, and that they often branch and make gap junctions with each other. Furthermore, the TZPs that connect to the oocyte are usually contacted on their shaft by oocyte microvilli. Mural granulosa cells were found to possess randomly oriented cytoplasmic projections that are strikingly similar to the free-ended TZPs. We propose that granulosa cells use cytoplasmic projections to search for the oocyte, and cumulus cell differentiation results from a contact-mediated paracrine interaction with the oocyte.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2019-02-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
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Article ; Online: OPA1 helical structures give perspective to mitochondrial dysfunction.

Nyenhuis, Sarah B / Wu, Xufeng / Strub, Marie-Paule / Yim, Yang-In / Stanton, Abigail E / Baena, Valentina / Syed, Zulfeqhar A / Canagarajah, Bertram / Hammer, John A / Hinshaw, Jenny E

Nature

2023 Volume 620, Issue 7976, Page(s) 1109–1116

Abstract: Dominant optic atrophy is one of the leading causes of childhood blindness. Around 60-80% of ... ...

Abstract	Dominant optic atrophy is one of the leading causes of childhood blindness. Around 60-80% of cases
MeSH term(s)	Cryoelectron Microscopy ; GTP Phosphohydrolases/chemistry ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; GTP Phosphohydrolases/ultrastructure ; Membrane Fusion ; Mitochondria/enzymology ; Mitochondria/metabolism ; Mitochondria/pathology ; Mitochondrial Dynamics ; Mitochondrial Membranes/metabolism ; Mutation ; Nucleotides/metabolism ; Protein Binding/genetics ; Protein Domains ; Protein Folding ; Protein Multimerization ; Protein Structure, Secondary ; Humans
Chemical Substances	GTP Phosphohydrolases (EC 3.6.1.-) ; Nucleotides ; OPA1 protein, human (EC 3.6.1.-)
Language	English
Publishing date	2023-08-23
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-023-06462-1
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Article: A versatile enhanced freeze-substitution protocol for volume electron microscopy.

Bélanger, Sébastien / Berensmann, Heather / Baena, Valentina / Duncan, Keith / Meyers, Blake C / Narayan, Kedar / Czymmek, Kirk J

Frontiers in cell and developmental biology

2022 Volume 10, Page(s) 933376

Abstract: Volume electron microscopy, a powerful approach to generate large three-dimensional cell and tissue volumes at electron microscopy resolutions, is rapidly becoming a routine tool for understanding fundamental and applied biological questions. One of the ... ...

Abstract	Volume electron microscopy, a powerful approach to generate large three-dimensional cell and tissue volumes at electron microscopy resolutions, is rapidly becoming a routine tool for understanding fundamental and applied biological questions. One of the enabling factors for its adoption has been the development of conventional fixation protocols with improved heavy metal staining. However, freeze-substitution with organic solvent-based fixation and staining has not realized the same level of benefit. Here, we report a straightforward approach including osmium tetroxide, acetone and up to 3% water substitution fluid (compatible with traditional or fast freeze-substitution protocols), warm-up and transition from organic solvent to aqueous 2% osmium tetroxide. Once fully hydrated, samples were processed in aqueous based potassium ferrocyanide, thiocarbohydrazide, osmium tetroxide, uranyl acetate and lead acetate before resin infiltration and polymerization. We observed a consistent and substantial increase in heavy metal staining across diverse and difficult-to-fix test organisms and tissue types, including plant tissues (
Language	English
Publishing date	2022-08-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2022.933376
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Article ; Online: Cytonemes with complex geometries and composition extend into invaginations of target cells.

Wood, Brent M / Baena, Valentina / Huang, Hai / Jorgens, Danielle M / Terasaki, Mark / Kornberg, Thomas B

The Journal of cell biology

2021 Volume 220, Issue 5

Abstract: Cytonemes are specialized filopodia that mediate paracrine signaling in Drosophila and other animals. Studies using fluorescence confocal microscopy (CM) established their general paths, cell targets, and essential roles in signaling. To investigate ... ...

Abstract	Cytonemes are specialized filopodia that mediate paracrine signaling in Drosophila and other animals. Studies using fluorescence confocal microscopy (CM) established their general paths, cell targets, and essential roles in signaling. To investigate details unresolvable by CM, we used high-pressure freezing and EM to visualize cytoneme structures, paths, contents, and contacts. We observed cytonemes previously seen by CM in the Drosophila wing imaginal disc system, including disc, tracheal air sac primordium (ASP), and myoblast cytonemes, and identified cytonemes extending into invaginations of target cells, and cytonemes connecting ASP cells and connecting myoblasts. Diameters of cytoneme shafts vary between repeating wide (206 ± 51.8 nm) and thin (55.9 ± 16.2 nm) segments. Actin, ribosomes, and membranous compartments are present throughout; rough ER and mitochondria are in wider proximal sections. These results reveal novel structural features of filopodia and provide a basis for understanding cytoneme cell biology and function.
MeSH term(s)	Actins/metabolism ; Animals ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Fibroblast Growth Factors/metabolism ; Myoblasts/metabolism ; Pseudopodia/metabolism ; Signal Transduction/physiology ; Wings, Animal/metabolism
Chemical Substances	Actins ; Drosophila Proteins ; Fibroblast Growth Factors (62031-54-3)
Language	English
Publishing date	2021-05-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202101116
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Article: Serial-section electron microscopy using automated tape-collecting ultramicrotome (ATUM).

Baena, Valentina / Schalek, Richard Lee / Lichtman, Jeff William / Terasaki, Mark

Methods in cell biology

2019 Volume 152, Page(s) 41–67

Abstract: The Automated Tape-Collecting Ultramicrotome (ATUM) is a tape-reeling device that is placed in a water-filled diamond knife boat to collect serial sections as they are cut by a conventional ultramicrotome. The ATUM can collect thousands of sections of ... ...

Abstract	The Automated Tape-Collecting Ultramicrotome (ATUM) is a tape-reeling device that is placed in a water-filled diamond knife boat to collect serial sections as they are cut by a conventional ultramicrotome. The ATUM can collect thousands of sections of many different shapes and sizes, which are subsequently imaged by a scanning electron microscope. This method has been used for large-scale connectomics projects of mouse brain, and is well suited for other smaller-scale studies of tissues, cells, and organisms. Here, we describe basic procedures for preparing a block for ATUM sectioning, handling of the ATUM, tape preparation, post-treatment of sections, and considerations for mapping, imaging, and aligning the serial sections.
MeSH term(s)	Animals ; Brain/physiology ; Image Processing, Computer-Assisted/methods ; Imaging, Three-Dimensional/methods ; Mice ; Microscopy, Electron, Scanning/methods ; Microtomy/methods
Language	English
Publishing date	2019-06-08
Publishing country	United States
Document type	Journal Article
ISSN	0091-679X
ISSN	0091-679X
DOI	10.1016/bs.mcb.2019.04.004
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Article ; Online: A versatile enhanced freeze-substitution protocol for volume electron microscopy

Sébastien Bélanger / Heather Berensmann / Valentina Baena / Keith Duncan / Blake C. Meyers / Kedar Narayan / Kirk J. Czymmek

Frontiers in Cell and Developmental Biology, Vol

2022 Volume 10

Abstract	Volume electron microscopy, a powerful approach to generate large three-dimensional cell and tissue volumes at electron microscopy resolutions, is rapidly becoming a routine tool for understanding fundamental and applied biological questions. One of the enabling factors for its adoption has been the development of conventional fixation protocols with improved heavy metal staining. However, freeze-substitution with organic solvent-based fixation and staining has not realized the same level of benefit. Here, we report a straightforward approach including osmium tetroxide, acetone and up to 3% water substitution fluid (compatible with traditional or fast freeze-substitution protocols), warm-up and transition from organic solvent to aqueous 2% osmium tetroxide. Once fully hydrated, samples were processed in aqueous based potassium ferrocyanide, thiocarbohydrazide, osmium tetroxide, uranyl acetate and lead acetate before resin infiltration and polymerization. We observed a consistent and substantial increase in heavy metal staining across diverse and difficult-to-fix test organisms and tissue types, including plant tissues (Hordeum vulgare), nematode (Caenorhabditis elegans) and yeast (Saccharomyces cerevisiae). Our approach opens new possibilities to combine the benefits of cryo-preservation with enhanced contrast for volume electron microscopy in diverse organisms.
Keywords	freeze-substitution fixation ; volume electron microscopy (vEM) ; OTO ; C. elegans ; Saccharomyces cerevisiae ; plant specimens ; Biology (General) ; QH301-705.5
Subject code	669
Language	English
Publishing date	2022-08-01T00:00:00Z
Publisher	Frontiers Media S.A.
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Evolution of the ribbon-like organization of the Golgi apparatus in animal cells.

Cell reports

2024 Volume 43, Issue 3, Page(s) 113791

Abstract: The "ribbon," a structural arrangement in which Golgi stacks connect to each other, is considered to be restricted to vertebrate cells. Although ribbon disruption is linked to various human pathologies, its functional role in cellular processes remains ... ...

Abstract	The "ribbon," a structural arrangement in which Golgi stacks connect to each other, is considered to be restricted to vertebrate cells. Although ribbon disruption is linked to various human pathologies, its functional role in cellular processes remains unclear. In this study, we investigate the evolutionary origin of the Golgi ribbon. We observe a ribbon-like architecture in the cells of several metazoan taxa suggesting its early emergence in animal evolution predating the appearance of vertebrates. Supported by AlphaFold2 modeling, we propose that the evolution of Golgi reassembly and stacking protein (GRASP) binding by golgin tethers may have driven the joining of Golgi stacks resulting in the ribbon-like configuration. Additionally, we find that Golgi ribbon assembly is a shared developmental feature of deuterostomes, implying a role in embryogenesis. Overall, our study points to the functional significance of the Golgi ribbon beyond vertebrates and underscores the need for further investigations to unravel its elusive biological roles.
MeSH term(s)	Animals ; Humans ; Membrane Proteins/metabolism ; Golgi Apparatus/metabolism ; Cytoskeleton/metabolism ; HeLa Cells ; Vertebrates
Chemical Substances	Membrane Proteins
Language	English
Publishing date	2024-02-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2024.113791
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Article ; Online: Localization of phosphorylated connexin 43 using serial section immunogold electron microscopy.

Norris, Rachael P / Baena, Valentina / Terasaki, Mark

Journal of cell science

2017 Volume 130, Issue 7, Page(s) 1333–1340

Abstract: Gap junction turnover occurs through the internalization of both of the plasma membranes of a gap junction plaque, forming a double membrane-enclosed vesicle, or connexosome. Phosphorylation has a key role in regulation, but further progress requires the ...

Abstract	Gap junction turnover occurs through the internalization of both of the plasma membranes of a gap junction plaque, forming a double membrane-enclosed vesicle, or connexosome. Phosphorylation has a key role in regulation, but further progress requires the ability to clearly distinguish gap junctions and connexosomes, and to precisely identify proteins associated with them. We examined, by using electron microscopy, serial sections of mouse preovulatory ovarian follicles that had been collected with an automated tape collecting ultramicrotome (ATUM). We found that connexosomes can form from adjacent cell bodies, from thin cell processes or from the same cell. By immunolabeling serial sections, we found that residue S368 of connexin 43 (also known as GJA1) is phosphorylated on gap junctions and connexosomes, whereas connexin 43 residue S262 is phosphorylated only on some connexosomes. These data suggest that phosphorylation at S262 contributes to connexosome formation or processing, and they provide more precise evidence that phosphorylation has a key role in gap junction internalization. Serial section electron microscopy of immunogold-labeled tissues offers a new way to investigate the three-dimensional organization of cells in their native environment.
MeSH term(s)	Animals ; Connexin 43/metabolism ; Female ; Gap Junctions/metabolism ; Gap Junctions/ultrastructure ; Horses ; Mice, Inbred C57BL ; Microscopy, Electron/methods ; Phosphorylation ; Phosphoserine/metabolism ; Staining and Labeling
Chemical Substances	Connexin 43 ; Phosphoserine (17885-08-4)
Language	English
Publishing date	2017-04-01
Publishing country	England
Document type	Journal Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.198408
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Zs.MG 14: Show issues

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