scholarly journals Microperoxisomes in the late pregnancy corpus luteum of rhesus monkeys (Macaca mulatta).

1975 ◽  
Vol 23 (5) ◽  
pp. 359-368 ◽  
Author(s):  
B J Gulys ◽  
L C Yuan
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Droplet ◽  
Macaca Mulatta ◽  
Rhesus Monkeys ◽  
Lipid Droplets ◽  
Late Pregnancy ◽  
Corpora Lutea ◽  
Adjacent Area ◽  
Electron Lucent ◽  
Specific Inhibitors

Microperoxisomes were identified in the franulosa lutein cells from the corpora lutea of rhesus monkeys (Macaca mulatta). These organelles were histochemically visualized in aldehyde-fixed tissues icubated in alkaline 3,3'-diaminobenzidine (DAB). The DAB staining of the microperoxisomes was abolished when the tissues were preincubated in specific inhibitors for catalse or when the H2O2 was omitted from the DAB medium. Microperoxisomes were differentiated from primary lysosmes by the Gomori acid phosphatase staining. Tortuous undulating agranular endoplasmic reticulum (ER) was usually closely associated with microperoxisomes. Those regions of the granular ER which were closely associated with microperoxosomes lacked ribsomes. Micropersoxisomes were often contiguous with lipid droplets, and in some instances the limiting membrane of the moroperosisomes appeared discontinous at the point of contiguity, and the DAB staining substance diffused onto the surface of the lipid droplet. In these instances, the adjacent area of the lipid droplet showed electron-lucent staining.

scholarly journals Mdm1 maintains endoplasmic reticulum homeostasis by spatially regulating lipid droplet biogenesis

2019 ◽  
Vol 218 (4) ◽  
pp. 1319-1334 ◽  
Author(s):  
Hanaa Hariri ◽  
Natalie Speer ◽  
Jade Bowerman ◽  
Sean Rogers ◽  
Gang Fu ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Endoplasmic Reticulum ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
Fatty Acyl ◽  
Nutrient Depletion ◽  
Coenzyme A Ligase ◽  
Response To Stress ◽  
Acyl Coenzyme A ◽  
Er Homeostasis

Lipid droplets (LDs) serve as cytoplasmic reservoirs for energy-rich fatty acids (FAs) stored in the form of triacylglycerides (TAGs). During nutrient stress, yeast LDs cluster adjacent to the vacuole/lysosome, but how this LD accumulation is coordinated remains poorly understood. The ER protein Mdm1 is a molecular tether that plays a role in clustering LDs during nutrient depletion, but its mechanism of function remains unknown. Here, we show that Mdm1 associates with LDs through its hydrophobic N-terminal region, which is sufficient to demarcate sites for LD budding. Mdm1 binds FAs via its Phox-associated domain and coenriches with fatty acyl–coenzyme A ligase Faa1 at LD bud sites. Consistent with this, loss of MDM1 perturbs free FA activation and Dga1-dependent synthesis of TAGs, elevating the cellular FA level, which perturbs ER morphology and sensitizes yeast to FA-induced lipotoxicity. We propose that Mdm1 coordinates FA activation adjacent to the vacuole to promote LD production in response to stress, thus maintaining ER homeostasis.

scholarly journals A conserved family of proteins facilitates nascent lipid droplet budding from the ER

2015 ◽  
Vol 211 (2) ◽  
pp. 261-271 ◽  
Author(s):  
Vineet Choudhary ◽  
Namrata Ojha ◽  
Andy Golden ◽  
William A. Prinz
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Lipid Metabolism ◽  
Caenorhabditis Elegans ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
De Novo ◽  
Fat Storage ◽  
Higher Eukaryotes ◽  
Er Membrane

Lipid droplets (LDs) are found in all cells and play critical roles in lipid metabolism. De novo LD biogenesis occurs in the endoplasmic reticulum (ER) but is not well understood. We imaged early stages of LD biogenesis using electron microscopy and found that nascent LDs form lens-like structures that are in the ER membrane, raising the question of how these nascent LDs bud from the ER as they grow. We found that a conserved family of proteins, fat storage-inducing transmembrane (FIT) proteins, is required for proper budding of LDs from the ER. Elimination or reduction of FIT proteins in yeast and higher eukaryotes causes LDs to remain in the ER membrane. Deletion of the single FIT protein in Caenorhabditis elegans is lethal, suggesting that LD budding is an essential process in this organism. Our findings indicated that FIT proteins are necessary to promote budding of nascent LDs from the ER.

INTRA-UTERINE TISSUES FROM LATE-PREGNANT RHESUS MONKEYS (MACACA MULATTA) PRODUCE 6-OXO-PROSTAGLANDIN F1α IN VITRO

1979 ◽  
Vol 81 (3) ◽  
pp. 339-343 ◽  
Author(s):  
M. D. MITCHELL ◽  
B. R. HICKS ◽  
G. D. THORBURN ◽  
J. S. ROBINSON
Keyword(s):  
Caesarean Section ◽  
Macaca Mulatta ◽  
Rhesus Monkeys ◽  
Late Pregnancy ◽  
Unit Weight ◽  
Decidua Basalis ◽  
Prostaglandin F ◽  
Near Term

The rates of production of 6-oxo-prostaglandin F1α (6-oxo-PGF1α) in vitro by intra-uterine tissues taken from late-pregnant monkeys at Caesarean section have been determined. For tissues obtained between days 140 and 149 of pregnancy (late pregnancy) the general quantitative order of rates of production (per unit weight) was decidua basalis> placenta > decidua parietalis>amnion>chorion = myometrium. When tissues were taken between days 160 and 168 of pregnancy (near term) this order was placenta > decidua parietalis = amnion> myometrium = decidua basalis > chorion. There was a significant reduction near term in the rate of production of 6-oxo-PGF1α by decidua basalis; all other tissues exhibited similar rates of production at the two gestational periods investigated.

scholarly journals Seipin-Mediated Contacts as Gatekeepers of Lipid Flux at the Endoplasmic Reticulum–Lipid Droplet Nexus 

Contact ◽  
2020 ◽  
Vol 3 ◽  
pp. 251525642094582
Author(s):  
Veijo T. Salo ◽  
Maarit Hölttä-Vuori ◽  
Elina Ikonen
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Metabolism ◽  
Recent Work ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
Intimate Relationship

Lipid droplets (LDs) are dynamic cellular hubs of lipid metabolism. While LDs contact a plethora of organelles, they have the most intimate relationship with the endoplasmic reticulum (ER). Indeed, LDs are initially assembled at specialized ER subdomains, and recent work has unraveled an increasing array of proteins regulating ER-LD contacts. Among these, seipin, a highly conserved lipodystrophy protein critical for LD growth and adipogenesis, deserves special attention. Here, we review recent insights into the role of seipin in LD biogenesis and as a regulator of ER-LD contacts. These studies have also highlighted the evolving concept of ER and LDs as a functional continuum for lipid partitioning and pinpointed a role for seipin at the ER-LD nexus in controlling lipid flux between these compartments.

scholarly journals OBSERVATIONS ON THE FINE STRUCTURE OF LUTEIN CELLS

1964 ◽  
Vol 22 (1) ◽  
pp. 127-141 ◽  
Author(s):  
Allen C. Enders ◽  
W. R. Lyons
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Droplets ◽  
Normal Pregnancy ◽  
Perivascular Space ◽  
Limiting Factor ◽  
Corpora Lutea ◽  
General Effect ◽  
Multiple Characteristics ◽  
Old Rats ◽  
Dense Matrices

Corpus luteum formation was induced in 26-day-old rats which were subsequently hypophysectomized and injected with mammotrophic hormone (MH, LTH). Sections of corpora lutea from these animals were examined with the electron microscope and compared with similarly prepared (Caulfield's fixed, Araldite embedded) corpora from normal pregnancy and from controls, the latter consisting of corpora prior to hypophysectomy and corpora from uninjected rats 7 to 14 days after hypophysectomy. Lutein cells from corpora lutea of injected animals and of normal pregnancy are characterized by abundant, tortuous, tubular agranular endoplasmic reticulum and by mitochondria, many of which are disc-shaped with dense matrices and both villiform and lamelliform cristae. The endoplasmic reticulum is most abundant in lutein cells from pregnant animals, in which cells it is in the form of thin, highly tortuous tubules. The form of the lipid droplets seen in cells of stimulated animals varies greatly. Marginal foldings of the lutein cells on the perivascular space were found in all instances. Lutein cells from hypophysectomized animals have a less highly developed agranular endoplasmic reticulum. The mitochondria have irregular outlines and a relatively lucid matrix. The lipid droplets in these cells show less tendency to be extracted, but are not so large or abundant as in the cells of onset controls. Granules believed to contain lipid pigments are common in the lutein cells of these control animals. It is suggested that lutein cells from corpora lutea which are actively secreting progesterone may be readily distinguished from lutein cells from non-active corpora by means of the multiple characteristics enumerated. It is further suggested that mammotrophic hormone has a general effect on the metabolism of lutein cells rather than solely affecting a specific organelle, the abundance or composition of which may be the limiting factor in the production of progesterone.

scholarly journals Motility Plays an Important Role in the Lifetime of Mammalian Lipid Droplets

2021 ◽  
Vol 22 (8) ◽  
pp. 3802
Author(s):  
Yi Jin ◽  
Zhuqing Ren ◽  
Yanjie Tan ◽  
Pengxiang Zhao ◽  
Jian Wu
Keyword(s):  
Signal Transduction ◽  
Endoplasmic Reticulum ◽  
Lipid Droplet ◽  
Molecular Basis ◽  
Lipid Droplets ◽  
Neutral Lipids ◽  
Future Research ◽  
Biological Processes ◽  
Cellular Processes ◽  
Resistance To Stress

The lipid droplet is a kind of organelle that stores neutral lipids in cells. Recent studies have found that in addition to energy storage, lipid droplets also play an important role in biological processes such as resistance to stress, immunity, cell proliferation, apoptosis, and signal transduction. Lipid droplets are formed at the endoplasmic reticulum, and mature lipid droplets participate in various cellular processes. Lipid droplets are decomposed by lipase and lysosomes. In the life of a lipid droplet, the most important thing is to interact with other organelles, including the endoplasmic reticulum, mitochondria, peroxisomes, and autophagic lysosomes. The interaction between lipid droplets and other organelles requires them to be close to each other, which inevitably involves the motility of lipid droplets. In fact, through many microscopic observation techniques, researchers have discovered that lipid droplets are highly dynamic organelles that move quickly. This paper reviews the process of lipid droplet motility, focusing on explaining the molecular basis of lipid droplet motility, the factors that regulate lipid droplet motility, and the influence of motility on the formation and decomposition of lipid droplets. In addition, this paper also proposes several unresolved problems for lipid droplet motility. Finally, this paper makes predictions about the future research of lipid droplet motility.

scholarly journals Human VPS13A is associated with multiple organelles and influences mitochondrial morphology and lipid droplet motility

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Wondwossen M Yeshaw ◽  
Marianne van der Zwaag ◽  
Francesco Pinto ◽  
Liza L Lahaye ◽  
Anita IE Faber ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Droplet ◽  
Mammalian Cells ◽  
Lipid Droplets ◽  
Neurodegenerative Disorder ◽  
Close Contact ◽  
Mitochondrial Morphology ◽  
Published Data ◽  
Membrane Contact Sites ◽  
Contact Sites

The VPS13A gene is associated with the neurodegenerative disorder Chorea Acanthocytosis. It is unknown what the consequences are of impaired function of VPS13A at the subcellular level. We demonstrate that VPS13A is a peripheral membrane protein, associated with mitochondria, the endoplasmic reticulum and lipid droplets. VPS13A is localized at sites where the endoplasmic reticulum and mitochondria are in close contact. VPS13A interacts with the ER residing protein VAP-A via its FFAT domain. Interaction with mitochondria is mediated via its C-terminal domain. In VPS13A-depleted cells, ER-mitochondria contact sites are decreased, mitochondria are fragmented and mitophagy is decreased. VPS13A also localizes to lipid droplets and affects lipid droplet motility. In VPS13A-depleted mammalian cells lipid droplet numbers are increased. Our data, together with recently published data from others, indicate that VPS13A is required for establishing membrane contact sites between various organelles to enable lipid transfer required for mitochondria and lipid droplet related processes.

scholarly journals Seipin and Nem1 establish discrete ER subdomains to initiate yeast lipid droplet biogenesis

2020 ◽  
Vol 219 (7) ◽  
Author(s):  
Vineet Choudhary ◽  
Ola El Atab ◽  
Giulia Mizzon ◽  
William A. Prinz ◽  
Roger Schneiter
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
Fat Storage ◽  
Contact Sites ◽  
Yeast Lipid

Lipid droplets (LDs) are fat storage organelles that originate from the endoplasmic reticulum (ER). Relatively little is known about how sites of LD formation are selected and which proteins/lipids are necessary for the process. Here, we show that LDs induced by the yeast triacylglycerol (TAG)-synthases Lro1 and Dga1 are formed at discrete ER subdomains defined by seipin (Fld1), and a regulator of diacylglycerol (DAG) production, Nem1. Fld1 and Nem1 colocalize to ER–LD contact sites. We find that Fld1 and Nem1 localize to ER subdomains independently of each other and of LDs, but both are required for the subdomains to recruit the TAG-synthases and additional LD biogenesis factors: Yft2, Pex30, Pet10, and Erg6. These subdomains become enriched in DAG. We conclude that Fld1 and Nem1 are both necessary to recruit proteins to ER subdomains where LD biogenesis occurs.

Smooth Muscular Cells in the Mammalian Ovary

1971 ◽  
Vol 29 ◽  
pp. 508-509
Author(s):  
Z. Fumagalli ◽  
P. Motta ◽  
S. Calvieri
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Electron Microscope ◽  
Small Groups ◽  
Cortical Area ◽  
Lipid Droplets ◽  
Corpora Lutea ◽  
Ovarian Stroma ◽  
Theca Interna ◽  
Glycogen Particles

The presence of smooth muscular cells was demonstrated with the electron microscope in different areas of the ovary of cats, mice and rabbits. The myocytes were arranged in fascicles, small groups, or most frequently appeared isolated. They were scattered in the ovarian stroma, related to the interstitial cells, in the periphery of the corpora lutea (rarely between luteal cells) in the middle of the gland. Smooth muscular cells were seldom observed between cells of the theca interna and externa of developing follicles and in the middle of atresic follicles. Some smooth muscular cells were found in the cortical area of the ovaries.Each smooth muscular cell showed typical filaments, free ribosomes, lipid droplets and at times glycogen particles. Mitochondria were vesicular; the (Golgi) vesicular complex was often related to two centrioles (frequently in a process of ciliogenesis). The granular endoplasmic reticulum was moderately developed. The plasma membrane presented invaginations and micropinocytotic vesicles as well as tight junctions between adjacent cells. The nucleus was elongated and its envelope formed wide perinuclear cisternae.

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