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Article ; Online: Granulosa Cells Alone, Without Theca Cells, Can Mediate LH-induced Oocyte Meiotic Resumption.

Norris, Rachael P / Jaffe, Laurinda A

2024 Volume 165, Issue 3

Abstract: Signaling in the granulosa cells of mammalian ovarian follicles is necessary for maintaining prophase arrest in the oocyte and for mediating the resumption of meiosis in response to luteinizing hormone (LH). However, the follicle also includes an outer ... ...

Abstract	Signaling in the granulosa cells of mammalian ovarian follicles is necessary for maintaining prophase arrest in the oocyte and for mediating the resumption of meiosis in response to luteinizing hormone (LH). However, the follicle also includes an outer layer of theca cells, some of which express receptors for LH. To investigate whether theca cells are required for maintaining meiotic arrest and reinitiating meiosis in response to LH, we mechanically separated the granulosa cells and oocyte from the theca and basal lamina. This was accomplished by cutting a slit in the outer surface of isolated follicles such that the mural granulosa cells and cumulus-oocyte complex were extruded from the theca shell, forming a lawn of cells on an organotypic membrane. The remnant of theca cells and basal lamina was then removed. The separation of the granulosa cells from the theca cells and basal lamina was demonstrated by immunofluorescence localization of endomucin (blood vessels of the theca) and laminin gamma (basal lamina). Cells comprising these granulosa cell-oocyte complexes expressed LH receptors and were connected by gap junctions. Oocytes within these granulosa cell complexes maintained meiotic arrest and resumed meiosis in response to LH, showing that the granulosa cells alone, without theca cells, transduce these signals. This semi-intact and mostly 2-dimensional preparation could facilitate imaging studies of follicle physiology.
MeSH term(s)	Female ; Animals ; Luteinizing Hormone/pharmacology ; Theca Cells ; Oocytes ; Granulosa Cells ; Ovarian Follicle ; Meiosis ; Mammals
Chemical Substances	Luteinizing Hormone (9002-67-9)
Language	English
Publishing date	2024-01-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	427856-2
ISSN	1945-7170 ; 0013-7227
ISSN (online)	1945-7170
ISSN	0013-7227
DOI	10.1210/endocr/bqad200
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Article ; Online: Transfer of mitochondria and endosomes between cells by gap junction internalization.

Norris, Rachael P

Traffic (Copenhagen, Denmark)

2021 Volume 22, Issue 6, Page(s) 174–179

Abstract: Intercellular organelle transfer has been documented in several cell types and has been proposed to be important for cell-cell communication and cellular repair. However, the mechanisms by which organelle transfer occurs are uncertain. Recent studies ... ...

Abstract	Intercellular organelle transfer has been documented in several cell types and has been proposed to be important for cell-cell communication and cellular repair. However, the mechanisms by which organelle transfer occurs are uncertain. Recent studies indicate that the gap junction protein, connexin 43 (Cx43), is required for mitochondrial transfer but its specific role is unknown. Using three-dimensional electron microscopy and immunogold labeling of Cx43, this report shows that whole organelles including mitochondria and endosomes are incorporated into double-membrane vesicles, called connexosomes or annular gap junctions, that form as a result of gap junction internalization. These findings demonstrate a novel mechanism for intercellular organelle transfer mediated by Cx43 gap junctions.
MeSH term(s)	Cell Communication ; Cell Line ; Endosomes/metabolism ; Gap Junctions/metabolism ; Mitochondria
Language	English
Publishing date	2021-04-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/tra.12786
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Article ; Online: Gap junction internalization and processing

Norris, Rachael P / Terasaki, Mark

Journal of cell science

2021 Volume 134, Issue 1

Abstract: Gap junctions have well-established roles in cell-cell communication by way of forming permeable intercellular channels. Less is understood about their internalization, which forms double membrane vesicles containing cytosol and membranes from another ... ...

Abstract	Gap junctions have well-established roles in cell-cell communication by way of forming permeable intercellular channels. Less is understood about their internalization, which forms double membrane vesicles containing cytosol and membranes from another cell called connexosomes or annular gap junctions. Here, we systematically investigated the fate of connexosomes in intact ovarian follicles. High-pressure frozen, serial-sectioned tissue was immunogold labeled for connexin 43 (Cx43, also known as GJA1). Within a volume corresponding to ∼35 cells, every labeled structure was categorized and had its surface area measured. Measurements support the concept that multiple connexosomes form from larger invaginated gap junctions. Subsequently, the inner and outer membranes separate, Cx43 immunogenicity is lost from the outer membrane, and the inner membrane appears to undergo fission. One pathway for processing involves lysosomes, based on localization of cathepsin B to some processed connexosomes. In summary, this study demonstrates new technology for high-resolution analyses of gap junction processing.This article has an associated First Person interview with the first author of the paper.
MeSH term(s)	Cell Communication ; Female ; Gap Junctions ; Humans ; Lysosomes ; Microscopy, Electron ; Microscopy, Immunoelectron ; Ovarian Follicle
Language	English
Publishing date	2021-01-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.252726
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Article ; Online: Gap junction internalization and processing in vivo: a 3D immuno-electron microscopy study

Norris, Rachael P. / Terasaki, Mark

bioRxiv

Abstract	Gap junctions have well-established roles in cell-cell communication by way of forming permeable intercellular channels. Less is understood about their internalization, which forms double membrane vesicles containing cytosol and membranes from another cell, called connexosomes or annular gap junctions. Here, we systematically studied the fate of connexosomes in intact ovarian follicles. High pressure frozen, serial sectioned tissue was immunogold labeled for Connexin 43. Within a volume of electron micrographs, every labeled structure was categorized and counted. Surface area measurements indicate that large connexosomes undergo fission. Subsequent modifications are separation of inner and outer membranes, loss of Cx43 from the outer membrane, and outward budding of the modified membranes. We also documented several clear examples of organelle transfer from one cell to another by gap junction internalization. We discuss how connexosome formation and processing may be a novel means for gap junctions to mediate cell-cell communication.
Keywords	covid19
Publisher	BioRxiv
Document type	Article ; Online
DOI	10.1101/2020.06.29.178475
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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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Article ; Online: Redistribution of Gαs in mouse salivary glands following β-adrenergic stimulation.

Hand, Arthur R / Elder, Kareen O / Norris, Rachael P

Archives of oral biology

2015 Volume 60, Issue 5, Page(s) 715–723

Abstract: Objective: Signalling via β-adrenergic receptors activates heterotrimeric G-proteins, which dissociate into α and βγ subunits. In salivary glands, the α subunit of Gs stimulates adenylate cyclase, increasing cyclic AMP levels and promoting exocytosis. ... ...

Abstract	Objective: Signalling via β-adrenergic receptors activates heterotrimeric G-proteins, which dissociate into α and βγ subunits. In salivary glands, the α subunit of Gs stimulates adenylate cyclase, increasing cyclic AMP levels and promoting exocytosis. The goals of this study were to determine Gαs localization in salivary glands and whether it undergoes redistribution upon activation. Methods: Mouse parotid and submandibular (SMG) glands were fixed with paraformaldehyde and prepared for immunofluorescence labelling with anti-Gαs. Results: In unstimulated parotid and SMG acinar cells, Gαs was localized mainly to basolateral membranes. Some parotid acinar cells also exhibited cytoplasmic fluorescence. Isoproterenol (IPR) stimulation resulted in decreased membrane fluorescence and increased cytoplasmic fluorescence, which appeared relatively uniform by 30 min. Beginning about 2 h after IPR, cytoplasmic fluorescence decreased and membrane fluorescence increased, approaching unstimulated levels in SMG acini by 4 h. Some parotid acini exhibited cytoplasmic fluorescence up to 8 h after IPR. The IPR-induced redistribution of Gαs was prevented (SMG) or reduced (parotid) by prior injection of propranolol. Striated duct cells of unstimulated mice exhibited general cytoplasmic fluorescence, which was unchanged after IPR. Conclusions: Gαs is localized to basolateral membranes of unstimulated salivary acinar cells. Activation of Gαs causes its release from the cell membrane and movement into the cytoplasm. Reassociation of Gαs with the membrane begins about 2 h after stimulation in the SMG, but complete reassociation takes several hours in the parotid gland. The presence of Gαs in striated duct cells suggests a role in signal transduction of secretion and/or electrolyte transport processes.
MeSH term(s)	Acinar Cells/drug effects ; Acinar Cells/metabolism ; Adenylyl Cyclases/metabolism ; Animals ; Cyclic AMP/metabolism ; GTP-Binding Protein alpha Subunits/metabolism ; Isoproterenol/pharmacology ; Mice ; Microscopy, Fluorescence ; Parotid Gland/drug effects ; Parotid Gland/metabolism ; Propranolol/pharmacology ; Signal Transduction/drug effects ; Submandibular Gland/drug effects ; Submandibular Gland/metabolism
Chemical Substances	GTP-Binding Protein alpha Subunits ; Propranolol (9Y8NXQ24VQ) ; Cyclic AMP (E0399OZS9N) ; Adenylyl Cyclases (EC 4.6.1.1) ; Isoproterenol (L628TT009W)
Language	English
Publishing date	2015-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80227-x
ISSN	1879-1506 ; 0003-9969
ISSN (online)	1879-1506
ISSN	0003-9969
DOI	10.1016/j.archoralbio.2015.01.010
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Article ; Online: FGF signaling induces mesoderm in the hemichordate Saccoglossus kowalevskii.

Green, Stephen A / Norris, Rachael P / Terasaki, Mark / Lowe, Christopher J

Development (Cambridge, England)

2013 Volume 140, Issue 5, Page(s) 1024–1033

Abstract: FGFs act in vertebrate mesoderm induction and also play key roles in early mesoderm formation in ascidians and amphioxus. However, in sea urchins initial characterizations of FGF function do not support a role in early mesoderm induction, making the ... ...

Abstract	FGFs act in vertebrate mesoderm induction and also play key roles in early mesoderm formation in ascidians and amphioxus. However, in sea urchins initial characterizations of FGF function do not support a role in early mesoderm induction, making the ancestral roles of FGF signaling and mechanisms of mesoderm specification in deuterostomes unclear. In order to better characterize the evolution of mesoderm formation, we have examined the role of FGF signaling during mesoderm development in Saccoglossus kowalevskii, an experimentally tractable representative of hemichordates. We report the expression of an FGF ligand, fgf8/17/18, in ectoderm overlying sites of mesoderm specification within the archenteron endomesoderm. Embryological experiments demonstrate that mesoderm induction in the archenteron requires contact with ectoderm, and loss-of-function experiments indicate that both FGF ligand and receptor are necessary for mesoderm specification. fgf8/17/18 gain-of-function experiments establish that FGF8/17/18 is sufficient to induce mesoderm in adjacent endomesoderm. These experiments suggest that FGF signaling is necessary from the earliest stages of mesoderm specification and is required for all mesoderm development. Furthermore, they suggest that the archenteron is competent to form mesoderm or endoderm, and that FGF signaling from the ectoderm defines the location and amount of mesoderm. When considered in a comparative context, these data support a phylogenetically broad requirement for FGF8/17/18 signaling in mesoderm specification and suggest that FGF signaling played an ancestral role in deuterostome mesoderm formation.
MeSH term(s)	Animals ; Chordata/embryology ; Chordata/genetics ; Chordata/metabolism ; Ectoderm/embryology ; Ectoderm/metabolism ; Embryo, Nonmammalian ; Embryonic Induction/genetics ; Embryonic Induction/physiology ; Endoderm/embryology ; Endoderm/metabolism ; Fibroblast Growth Factors/genetics ; Fibroblast Growth Factors/metabolism ; Fibroblast Growth Factors/physiology ; Gastrulation/genetics ; Gastrulation/physiology ; Gene Expression Regulation, Developmental ; Mesoderm/embryology ; Mesoderm/metabolism ; Models, Biological ; Receptors, Fibroblast Growth Factor/genetics ; Receptors, Fibroblast Growth Factor/metabolism ; Receptors, Fibroblast Growth Factor/physiology ; Signal Transduction/genetics ; Signal Transduction/physiology
Chemical Substances	Receptors, Fibroblast Growth Factor ; Fibroblast Growth Factors (62031-54-3)
Language	English
Publishing date	2013-01-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.083790
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Article ; Online: Phosphorylation of serine residues in the C-terminal cytoplasmic tail of connexin43 regulates proliferation of ovarian granulosa cells.

Dyce, Paul W / Norris, Rachael P / Lampe, Paul D / Kidder, Gerald M

The Journal of membrane biology

2012 Volume 245, Issue 5-6, Page(s) 291–301

Abstract: Connexin43 (Cx43) forms gap junctions that couple the granulosa cells of ovarian follicles. In Cx43 knockout mice, follicle growth is restricted as a result of impaired granulosa cell proliferation. We have used these mice to examine the importance of ... ...

Abstract	Connexin43 (Cx43) forms gap junctions that couple the granulosa cells of ovarian follicles. In Cx43 knockout mice, follicle growth is restricted as a result of impaired granulosa cell proliferation. We have used these mice to examine the importance of specific Cx43 phosphorylation sites in follicle growth. Serines at residues 255, 262, 279, and 282 are MAP kinase substrates that, when phosphorylated, reduce junctional conductance. Mutant forms of Cx43 were constructed with these serines replaced with amino acids that cannot be phosphorylated. These mutants were transduced into Cx43 knockout ovarian somatic cells that were combined with wild-type oocytes and grafted into immunocompromised female mice permitting follicle growth in vivo. Despite residues 255 or 262 being mutated to prevent their being phosphorylated, recombinant ovaries constructed with these mutants were able to rescue the null phenotype, restoring complete folliculogenesis. In contrast, Cx43 with serine to alanine mutations at both residues 279 and 282 or at all four residues failed to rescue folliculogenesis; the mutant molecules were largely confined to intracellular sites, with few gap junctions. Using an in vitro proliferation assay, we confirmed a decrease in proliferation of granulosa cells expressing the double mutant construct. These results indicate that Cx43 phosphorylation by MAP kinase at serines 279 and 282 occurs in granulosa cells of early follicles and that this is involved in regulating follicle development.
MeSH term(s)	Animals ; Cell Proliferation ; Connexin 43/metabolism ; Female ; Granulosa Cells/cytology ; Granulosa Cells/metabolism ; Mice ; Mitogen-Activated Protein Kinases/metabolism ; Ovarian Follicle/cytology ; Ovarian Follicle/metabolism ; Ovary/cytology ; Ovary/growth & development ; Ovary/metabolism ; Phosphorylation ; Serine/metabolism
Chemical Substances	Connexin 43 ; Serine (452VLY9402) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2012-06-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3082-x
ISSN	1432-1424 ; 0022-2631
ISSN (online)	1432-1424
ISSN	0022-2631
DOI	10.1007/s00232-012-9450-6
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Article ; Online: Epidermal growth factor receptor kinase activity is required for gap junction closure and for part of the decrease in ovarian follicle cGMP in response to LH.

Norris, Rachael P / Freudzon, Marina / Nikolaev, Viacheslav O / Jaffe, Laurinda A

Reproduction (Cambridge, England)

2010 Volume 140, Issue 5, Page(s) 655–662

Abstract: The meiotic cell cycle in mouse oocytes is arrested in prophase, and then restarted when LH acts on the surrounding granulosa cells. The granulosa cells keep meiosis arrested by providing a source of cGMP that diffuses into the oocyte through gap ... ...

Abstract	The meiotic cell cycle in mouse oocytes is arrested in prophase, and then restarted when LH acts on the surrounding granulosa cells. The granulosa cells keep meiosis arrested by providing a source of cGMP that diffuses into the oocyte through gap junctions, and LH restarts the cell cycle by closing the junctions and by decreasing granulosa cell cGMP, thus lowering oocyte cGMP. Epidermal growth factor receptor (EGFR) activation is an essential step in triggering LH-induced meiotic resumption, but its relationship to the cGMP decrease in the follicle is incompletely understood, and its possible function in causing gap junction closure has not been investigated. Here, we use EGFR agonists (epiregulin and amphiregulin) and an EGFR kinase inhibitor (AG1478) to study the function of the EGFR in the signaling pathways leading to the release of oocytes from prophase arrest. Our results indicate that the EGFR kinase contributes to LH-induced meiotic resumption in two different ways. First, it is required for gap junction closure. Second, it is required for an essential component of the decrease in follicle cGMP. Our data show that the EGFR kinase-dependent component of the cGMP decrease is required for LH-induced meiotic resumption, but they also indicate that an as yet unidentified pathway accounts for a large part of the cGMP decrease.
MeSH term(s)	Amphiregulin ; Animals ; Cyclic GMP/physiology ; EGF Family of Proteins ; Epidermal Growth Factor/pharmacology ; Epiregulin ; ErbB Receptors/physiology ; Female ; Gap Junctions/physiology ; Glycoproteins/pharmacology ; Immunoblotting ; Intercellular Signaling Peptides and Proteins/pharmacology ; Luteinizing Hormone/physiology ; Meiosis/physiology ; Mice ; Mice, Inbred C57BL ; Microscopy, Fluorescence ; Ovarian Follicle/physiology ; Quinazolines ; Tyrphostins/pharmacology
Chemical Substances	Amphiregulin ; Areg protein, mouse ; EGF Family of Proteins ; Epiregulin ; Ereg protein, mouse ; Glycoproteins ; Intercellular Signaling Peptides and Proteins ; Quinazolines ; Tyrphostins ; RTKI cpd (170449-18-0) ; Epidermal Growth Factor (62229-50-9) ; Luteinizing Hormone (9002-67-9) ; ErbB Receptors (EC 2.7.10.1) ; Cyclic GMP (H2D2X058MU)
Language	English
Publishing date	2010-09-08
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2034501-X
ISSN	1741-7899 ; 1470-1626 ; 1476-3990
ISSN (online)	1741-7899
ISSN	1470-1626 ; 1476-3990
DOI	10.1530/REP-10-0288
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Article ; Online: Anteroposterior axis patterning by early canonical Wnt signaling during hemichordate development.

Darras, Sébastien / Fritzenwanker, Jens H / Uhlinger, Kevin R / Farrelly, Ellyn / Pani, Ariel M / Hurley, Imogen A / Norris, Rachael P / Osovitz, Michelle / Terasaki, Mark / Wu, Mike / Aronowicz, Jochanan / Kirschner, Marc / Gerhart, John C / Lowe, Christopher J

PLoS biology

2018 Volume 16, Issue 1, Page(s) e2003698

Abstract: The Wnt family of secreted proteins has been proposed to play a conserved role in early specification of the bilaterian anteroposterior (A/P) axis. This hypothesis is based predominantly on data from vertebrate embryogenesis as well as planarian ... ...

Abstract	The Wnt family of secreted proteins has been proposed to play a conserved role in early specification of the bilaterian anteroposterior (A/P) axis. This hypothesis is based predominantly on data from vertebrate embryogenesis as well as planarian regeneration and homeostasis, indicating that canonical Wnt (cWnt) signaling endows cells with positional information along the A/P axis. Outside of these phyla, there is strong support for a conserved role of cWnt signaling in the repression of anterior fates, but little comparative support for a conserved role in promotion of posterior fates. We further test the hypothesis by investigating the role of cWnt signaling during early patterning along the A/P axis of the hemichordate Saccoglossus kowalevskii. We have cloned and investigated the expression of the complete Wnt ligand and Frizzled receptor complement of S. kowalevskii during early development along with many secreted Wnt modifiers. Eleven of the 13 Wnt ligands are ectodermally expressed in overlapping domains, predominantly in the posterior, and Wnt antagonists are localized predominantly to the anterior ectoderm in a pattern reminiscent of their distribution in vertebrate embryos. Overexpression and knockdown experiments, in combination with embryological manipulations, establish the importance of cWnt signaling for repression of anterior fates and activation of mid-axial ectodermal fates during the early development of S. kowalevskii. However, surprisingly, terminal posterior fates, defined by posterior Hox genes, are unresponsive to manipulation of cWnt levels during the early establishment of the A/P axis at late blastula and early gastrula. We establish experimental support for a conserved role of Wnt signaling in the early specification of the A/P axis during deuterostome body plan diversification, and further build support for an ancestral role of this pathway in early evolution of the bilaterian A/P axis. We find strong support for a role of cWnt in suppression of anterior fates and promotion of mid-axial fates, but we find no evidence that cWnt signaling plays a role in the early specification of the most posterior axial fates in S. kowalevskii. This posterior autonomy may be a conserved feature of early deuterostome axis specification.
MeSH term(s)	Animals ; Biological Transport ; Body Patterning/physiology ; Cell Lineage/physiology ; Ectoderm ; Embryonic Development/physiology ; Frizzled Receptors/physiology ; Gene Expression Regulation, Developmental/physiology ; Genes, Homeobox ; Homeostasis ; Planarians ; Polychaeta/embryology ; Polychaeta/physiology ; Wnt Signaling Pathway/physiology
Chemical Substances	Frizzled Receptors
Language	English
Publishing date	2018-01-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.2003698
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