• Journal of Ginseng Research
• /
• v.15 no.2
• /
• pp.131-138
• /
• 1991

This study was carried out to investigate the development of endoplasmic reticulum and the formation of Protein body in the endosperm cell during seed formation of Panax ginseng C. A. Meyer with electron microscope. In the endosperm cell of early developmental process after pollination, vesicles that contain storage materials produced in rough endoplasmic reticulum incorporated into central vacuole. The central vacuole is gradually subdivided into several small-sized vacuoles and increased in number. Amorphous proteinaceous materials of high electron density are produced in rough endoplasmic reticulum. Rough endoplasmic reticulum increase in number and surround the protein body and vesicles circularly. Spherical proteinaceous granules with limited membrane appeared from the amorphous granules at the peripheral region of the rough endoplasmic reticulum. Gradually, storage materials are accumulated within the vacuole surrounded by spherosomes. Protein bodies are formed by interfusing between vacuoles and vesicles derived from rough endoplasmic reticulum which contained the amorphous protein of high electron density.

• Journal of Life Science
• /
• v.9 no.1
• /
• pp.90-92
• /
• 1999

Deficient thyroglobulin is one of the important causes of congenital hypothyroid goiter with a prevalence of -1/40,000 humans. We now demonstrate that in cog/cog mice showing hypothyroidism, four endoplasmic reticulum-molecular chaperones stably bind to thyroglobulin, providing insight into physiologic regulation of endoplasmic reticulum storage diseases.

• Applied Microscopy
• /
• v.18 no.2
• /
• pp.141-152
• /
• 1988

The developmental processes of the protein body are studied on endosperm cells of Panax ginseng during seed maturation periods. The spherosome, mitochondria, rough endoplasmic reticulum, and ribosome are observed and then are gradually increased in early endosperm cells. Protein body developed from vesicles produced by the rough endoplasmic reticulum and was formed at the enlarged ends of rough endoplasmic reticulum. Also, vacuole-like protein body was observed in associated with rough endoplasmic reticulum. Golgi complex is observed in associated with vacuole and its vesicles containing proteinaceous granules moved and accumulated to the vacuole. Proteinaceous granules are deposited in the spherical or oval shaped vacuole and gradually, vacuole is surrounded by the multi-membranous structure. Rough endoplasmic reticulum, ribosome, Golgi complex, and vacuole are observed in associated with protein body formation.

• BMB Reports
• /
• v.43 no.3
• /
• pp.151-157
• /
• 2010

$Ca^{2+}$ is a universal signalling molecule that affects a variety of cellular processes including cardiac development. The majority of intracellular $Ca^{2+}$ is stored in the endoplasmic and sarcoplasmic reticulum of muscle and non-muscle cells. Calreticulin is a well studied $Ca^{2+}$-buffering protein in the endoplasmic reticulum, and calreticulin deficiency is embryonic lethal due to impaired cardiac development. Despite calsequestrin being the most abundant $Ca^{2+}$-buffering protein in the sarcoplasmic reticulum, viability is maintained in embryos without calsequestrin and normal $Ca^{2+}$ release and contractile function is observed. The $Ca^{2+}$ homeostasis regulated by the endoplasmic and sarcoplasmic reticulum is critical for the development and proper function of the heart.

• Applied Microscopy
• /
• v.27 no.1
• /
• pp.47-56
• /
• 1997

The objective of the present study was to investigate the cytotoxicity of adriamycin in liver cells (group A), and the protective effect of squalene to the hepatocytes to which adriamycin-induced cytotcxicity (group B) was examined by transmission electron micro-scope. In the group A, The cisternae of rough endoplasmic reitculum and smooth endoplasmic reticulum are dilated/disoriented at 24 hours and 48 hours. The inner and outer membrane of mitochondria are detached or destructed , and attached ribosomes of rough endoplasmic reticulum are diminished in number. The cisternae of the smooth endoplasmic reticulum are dilated, and the cristae of mitochondria are disrupted at 72 hours and 96 hours. In the group B, the cisternae of the rough endoplasmic reticulum and smooth endoplasmic resticulum are dilated at 24 hours. The cisternae of the smooth endoplasmic reticulum are dilated at 48 hours. The cell organelles of hepatocytes are recovered from cytotoxicity at 72 hours. These results suggest that 50 is not only concerned with composition of the membrane system of the cell organelles but also decreased the cytotoxicity of the hepatocytes.

• Biomedical Science Letters
• /
• v.11 no.2
• /
• pp.249-252
• /
• 2005

The mammalian unfolded protein response (UPR) protects the cell. against the stress of unfolded or misfolded proteins in the endoplasmic reticulum (ER). It has recently demonstrated that IRE1, PERK, ATF6, and X-box protein 1 (XBP-l) directly or indirectly participate in this process. Upon accumulation of unfolded/misfolded proteins in the ER lumen, release of BiP from Ire1p permits dimerization and autophosphorylation to activate its kinase and endoribonulease activities to initiate XBP-1 mRNA splicing. Spliced XBP-1 mRNA removed middle part of 23 bp and encodes a potent transcription factor, XBP-l protein that binds to the unfolded protein response element (UPRE) or endoplasmic reticulum stress element (ERSE) sequence of many UPR target genes and produces several kind of ER chaperones. In this study, we described both the result and the detailed experimental procedures of XBP-1 mRNA splicing induced by ER stress, this result might help to elucidate the roles of the UPR and early diagnosis in a number of human diseases involving endoplasmic reticulum storage disease (ERSD).

• Clinical and Experimental Reproductive Medicine
• /
• v.17 no.2
• /
• pp.185-196
• /
• 1990

These experiments were performed to know ultrastructural changes of the cumulus expansion in virot. SEM:In expanded oocyte-cumulus complex, the cell surface are characterized by the presence of many evaginations:they are relatively short and round shape. The mucous extracellular material were deposited between cumulus cells. TEM:In compact cumulus cells, golgi apparatus and rough endoplasmic reticulum developed. In expanded cumulus cells, rough endoplasmic reticulum decreased and the smooth endoplasmic reticulum increased. Also, there were numbers of mitochondria. Extracellular mucous material which is presumed to be hyaluronic acid appears when cumulus cell were expanded. In expanded cumulus cell, numbers of smooth endoplasmic reticulum help cumulus cell to develop in steroidogenic cell.

• Journal of Breast Cancer
• /
• v.21 no.4
• /
• pp.354-362
• /
• 2018

Cellular stress severely disrupts endoplasmic reticulum (ER) function, leading to the abnormal accumulation of unfolded or misfolded proteins in the ER and subsequent development of endoplasmic reticulum stress (ERS). To accommodate the occurrence of ERS, cells have evolved a highly conserved, selfprotecting signal transduction pathway called the unfolded protein response. Notably, ERS signaling is involved in the development of a variety of diseases and is closely related to tumor development, particularly in breast cancer. This review discusses recent research regarding associations between ERS and tumor metastasis. The information presented here will help researchers elucidate the precise mechanisms underlying ERS-mediated tumor metastasis and provide new directions for tumor therapies.

• Applied Microscopy
• /
• v.28 no.4
• /
• pp.603-613
• /
• 1998

The present study was designed in order to observe relationship between the endoplasmic reticulum and the Golgi complex during spermiogenesis of the long-fingered bat (Miniopterus schreibersi fuliginosus). The testes were obtained from adult bats and treated with the prolonged osmification or fixed with ferrocyanide reduced osmiun. In the Golgi phase, The Golgi complex shows an oval shape, and was composed of a cortex and a medullar enclosing acrosome. The Golgi vacuoles with electron-dense granules of crescent shape were fused with each other. The smooth endoplasrnic reticulum was scattered in all the area of the cytoplasm. In the cap phase, The Golgi complex was crescent in shape, and faced to a nucleus. Large and small vesicles were fused with each other, and then fused with a acrosomal vacuole. The rough endoplasmic reticulum was close to the large Golgi vacuole. In the acrosome phase, The Golgi complex was moved to behind of the acrosome face. Small vesicles were fused with an acrosome, and cisternae of the trans-face of Golgi complex was connected with an acrosome in the early acrosome phase. The smooth endoplasmic reticulum was distributed in the cytoplasm. The annulate lamellar was originated from a radial body-annulate lammellae complex. In the maturation phase, The Golgi complex with dilated cistrern appeared in the cytoplasm, and also, annulate lamellar was observed in the cytoplasm. The connection of the annulate lamellar with the cistern of radial body suggests that an annulate lamellar seems to be closely related to radial body. The smooth endoplasmic reticulum was scattered in the cytoplasm in the early Golgi phase, but annulate lamellar-radial body complex which might be a residual and disappearing form of the smooth endoplasmic reticulum appeared in the acrosome phase. The Golgi complex steadily remained in the late maturation phase when the endoplasmic reticulum began to disappear from the cytoplasm: the Golgi complex was still occurred after acrosome formation. The observations obtained in the present study, which was characterized by the presence of the Golgi complex in the late maturation phase, suggests that the Golgi complex may play an important role also even after the acrosome formation.

• Fisheries and Aquatic Sciences
• /
• v.1 no.2
• /
• pp.293-295
• /
• 1998