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equipment designed to serve a specific function (同)setup
(anatomy) a group of body parts that work together to perform a given function; "the breathing apparatus"
Italian histologist noted for work on the structure of the nervous system and for his discovery of Golgi bodies (1844-1926) (同)Camillo Golgi

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〈U〉〈C〉(一式の)『器具』;装置 / 《集合的に》(ある機能を営む一系統の身体の)器官 / 〈U〉〈C〉(ある目的のための)道具立て
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/01/24 19:37:44」(JST)

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For the song, see Junta (album).

Micrograph of Golgi apparatus, visible as a stack of semicircular black rings near the bottom. Numerous circular vesicles can be seen in proximity to the organelle.

The Golgi apparatus (/ˈɡoʊldʒiː/), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells.^[1] It was identified in 1897 by the Italian physician Camillo Golgi and named after him in 1898.^[2]

Part of the cellular endomembrane system, the Golgi apparatus packages proteins inside the cell before they are sent to their destination; it is particularly important in the processing of proteins for secretion.

Discovery

Owing to its large size, the Golgi apparatus was one of the first organelles to be discovered and observed in detail. It was discovered in 1898 by Italian physician Camillo Golgi during an investigation of the nervous system.^[2] After first observing it under his microscope, he termed the structure the internal reticular apparatus. Some doubted the discovery at first, arguing that the appearance of the structure was merely an optical illusion created by the observation technique used by Golgi. With the development of modern microscopes in the 20th century, the discovery was confirmed.^[3] Early references to the Golgi referred to it by various names including the "Golgi–Holmgren apparatus", "Golgi–Holmgren ducts", and "Golgi–Kopsch apparatus".^[2] The term "Golgi apparatus" was used in 1910 and first appeared in scientific literature in 1913.^[2]

Structure

Diagram of the Golgi apparatus

3D Rendering of Golgi Apparatus

Found within the cytoplasm of both plant and animal cells, the Golgi is composed of stacks of membrane-bound structures known as cisternae (singular: cisterna). An individual stack is sometimes called a dictyosome (from Greek dictyon: net + soma: body),^[4] especially in plant cells.^[5] A mammalian cell typically contains 40 to 100 stacks.^[6] Between four and eight cisternae are usually present in a stack; however, in some protists as many as sixty have been observed.^[3] Each cisterna comprises a flat, membrane enclosed disc that includes special Golgi enzymes which modify or help to modify cargo proteins that travel through it.^[7]

The cisternae stack has four functional regions: the cis-Golgi network, medial-Golgi, endo-Golgi, and trans-Golgi network. Vesicles from the endoplasmic reticulum (via the vesicular-tubular clusters) fuse with the network and subsequently progress through the stack to the trans Golgi network, where they are packaged and sent to their destination. Each region contains different enzymes which selectively modify the contents depending on where they reside.^[8] The cisternae also carry structural proteins important for their maintenance as flattened membranes which stack upon each other.^[9]

Function of a golgi body

Cells synthesize a large number of different macromolecules. The Golgi apparatus is integral in modifying, sorting, and packaging these macromolecules for cell secretion^[10] (exocytosis) or use within the cell.^[11] It primarily modifies proteins delivered from the rough endoplasmic reticulum but is also involved in the transport of lipids around the cell, and the creation of lysosomes.^[11] In this respect it can be thought of as similar to a post office; it packages and labels items which it then sends to different parts of the cell.

Enzymes within the cisternae are able to modify the proteins by addition of carbohydrates (glycosylation)^[12] and phosphates (phosphorylation). In order to do so, the Golgi imports substances such as nucleotide sugars from the cytosol. These modifications may also form a signal sequence which determines the final destination of the protein. For example, the Golgi apparatus adds a mannose-6-phosphate label to proteins destined for lysosomes.

The Golgi plays an important role in the synthesis of proteoglycans, which are molecules present in the extracellular matrix of animals. It is also a major site of carbohydrate synthesis.^[13] This includes the production of glycosaminoglycans (GAGs), long unbranched polysaccharides which the Golgi then attaches to a protein synthesised in the endoplasmic reticulum to form proteoglycans.^[14] Enzymes in the Golgi polymerize several of these GAGs via a xylose link onto the core protein. Another task of the Golgi involves the sulfation of certain molecules passing through its lumen via sulfotranferases that gain their sulfur molecule from a donor called PAPS. This process occurs on the GAGs of proteoglycans as well as on the core protein. Sulfation is generally performed in the trans-Golgi network. The level of sulfation is very important to the proteoglycans' signalling abilities as well as giving the proteoglycan its overall negative charge.^[13]

The phosphorylation of molecules requires that ATP is imported into the lumen of the Golgi^[15] and utilised by resident kinases such as casein kinase 1 and casein kinase 2. One molecule that is phosphorylated in the Golgi is Apolipoprotein, which forms a molecule known as VLDL that is a constituent of blood serum. It is thought that the phosphorylation of these molecules is important to help aid in their sorting for secretion into the blood serum.^[16]

The Golgi has a putative role in apoptosis, with several Bcl-2 family members localised there, as well as to the mitochondria. A newly characterized protein, GAAP (Golgi anti-apoptotic protein), almost exclusively resides in the Golgi and protects cells from apoptosis by an as-yet undefined mechanism.^[17]

Vesicular transport

Diagram of secretory process from endoplasmic reticulum (orange) to Golgi apparatus (pink). 1. Nuclear membrane; 2. Nuclear pore; 3. Rough endoplasmic reticulum (RER); 4. Smooth endoplasmic reticulum (SER); 5. Ribosome attached to RER; 6. Macromolecules; 7. Transport vesicles; 8. Golgi apparatus; 9. Cis face of Golgi apparatus; 10. Trans face of Golgi apparatus; 11. Cisternae of the Golgi Apparatus

The vesicles that leave the rough endoplasmic reticulum are transported to the cis face of the Golgi apparatus, where they fuse with the Golgi membrane and empty their contents into the lumen. Once inside the lumen, the molecules are modified, then sorted for transport to their next destinations. The Golgi apparatus tends to be larger and more numerous in cells that synthesize and secrete large amounts of substances; for example, the plasma B cells and the antibody-secreting cells of the immune system have prominent Golgi complexes.

Those proteins destined for areas of the cell other than either the endoplasmic reticulum or Golgi apparatus are moved towards the trans face, to a complex network of membranes and associated vesicles known as the trans-Golgi network (TGN). This area of the Golgi is the point at which proteins are sorted and shipped to their intended destinations by their placement into one of at least three different types of vesicles, depending upon the molecular marker they carry.

Types	Description	Example
Exocytotic vesicles (continuous)	Vesicle contains proteins destined for extracellular release. After packaging, the vesicles bud off and immediately move towards the plasma membrane, where they fuse and release the contents into the extracellular space in a process known as constitutive secretion.	Antibody release by activated plasma B cells
Secretory vesicles (regulated)	Vesicle contains proteins destined for extracellular release. After packaging, the vesicles bud off and are stored in the cell until a signal is given for their release. When the appropriate signal is received they move towards the membrane and fuse to release their contents. This process is known as regulated secretion.	Neurotransmitter release from neurons
Lysosomal vesicles	Vesicle contains proteins and ribosomes destined for the lysosome, an organelle of degradation containing many acid hydrolases, or to lysosome-like storage organelles. These proteins include both digestive enzymes and membrane proteins. The vesicle first fuses with the late endosome, and the contents are then transferred to the lysosome via unknown mechanisms.	Digestive proteases destined for the lysosome

Transport mechanism

The transport mechanism which proteins use to progress through the Golgi apparatus is not yet clear; however a number of hypotheses currently exist. Until recently, the vesicular transport mechanism was favoured but now more evidence is coming to light to support cisternal maturation. The two proposed models may actually work in conjunction with each other, rather than being mutually exclusive. This is sometimes referred to as the combined model.^[13]

Cisternal maturation model: the cisternae of the Golgi apparatus move by being built at the cis face and destroyed at the trans face. Vesicles from the endoplasmic reticulum fuse with each other to form a cisterna at the cis face, consequently this cisterna would appear to move through the Golgi stack when a new cisterna is formed at the cis face. This model is supported by the fact that structures larger than the transport vesicles, such as collagen rods, were observed microscopically to progress through the Golgi apparatus.^[13] This was initially a popular hypothesis, but lost favour in the 1980s. Recently it has made a comeback, as laboratories at the University of Chicago and the University of Tokyo have been able to use new technology to directly observe Golgi compartments maturing.^[18] Additional evidence comes from the fact that COPI vesicles move in the retrograde direction, transporting endoplasmic reticulum proteins back to where they belong by recognizing a signal peptide.^[19]

Vesicular transport model: Vesicular transport views the Golgi as a very stable organelle, divided into compartments in the cis to trans direction. Membrane bound carriers transport material between the endoplasmic reticulum and the different compartments of the Golgi.^[20] Experimental evidence includes the abundance of small vesicles (known technically as shuttle vesicles) in proximity to the Golgi apparatus. To direct the vesicles, actin filaments connect packaging proteins to the membrane to ensure that they fuse with the correct compartment.^[13]

Fate during mitosis

In animal cells, the Golgi apparatus will break up and disappear following the onset of mitosis, or cellular division. During the telophase of mitosis, the Golgi apparatus reappears. As of December 2009^[update] it is uncertain how this occurs.^[21] In contrast, Golgi stacks have been observed to remain intact in plant or yeast cells throughout the cell cycle. The reason for this difference is not yet known, but it may, in part, be a consequence of golgin proteins.

References

^ Pavelk M, Mironov AA (2008). The Golgi Apparatus: State of the art 110 years after Camillo Golgi's discovery. Berlin: Springer. ISBN 3-211-76309-0. ^{[page needed]}
^ ^a ^b ^c ^d Fabene PF, Bentivoglio M (1998). "1898–1998: Camillo Golgi and "the Golgi": one hundred years of terminological clones". Brain Res. Bull. 47 (3): 195–8. doi:10.1016/S0361-9230(98)00079-3. PMID 9865849.
^ ^a ^b Davidson MW (2004-12-13). "The Golgi Apparatus". Molecular Expressions. Florida State University. Retrieved 2010-09-20.
^ "Dictyosome". Dictionary.com. Retrieved 2010-09-20.
^ Wolfe SA (1993). Molecular and Cellular Biology. Belmont, CA: Wadsworth Pub. Co. p. 828. ISBN 0-534-12408-9.
^ Duran JM, Kinseth M, Bossard C, Rose DW, Polishchuk R, Wu CC, Yates J, Zimmerman T, Malhotra V (2008). "The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis". Mol. Biol. Cell 19 (6): 2579–87. doi:10.1091/mbc.E07-10-0998. PMC 2397314. PMID 18385516.
^ Becker, Kleinsmith, Hardin, Bertoni (2009). the World of the Cell. San Francisco, CA: Pearson Benjamin Cummings. pp. 333, 339. ISBN 0-321-55418-3.
^ Krieger M, Scott MP, Matsudaira PT, Lodish HF, Darnell JE. Lawrence Z, Kaiser C, Arnold B (2004). Molecular cell biology (5th edn ed.). New York: W.H. Freeman and CO. ISBN 0-7167-4366-3.
^ Chiu, Chi-Fang; Ghanekar, Yashoda; Frost, Laura; Diao, Aipo; Morrison, Daniel; McKenzie, Eddie; Lowe, Martin (2008). "ZFPL1, a novel ring finger protein required for cis-Golgi integrity and efficient ER-to-Golgi transport". The EMBO Journal 27 (7): 934–47. doi:10.1038/emboj.2008.40. PMC 2323254. PMID 18323775.
^ "Regulated Secretion (Golgi): The Movie". North Dakota State University. Retrieved 2010-11-14.
^ ^a ^b Campbell, Neil A (1996). Biology (4 ed.). Menlo Park, CA: Benjamin/Cummings. pp. 122, 123. ISBN 0-8053-1957-3.
^ William G. Flynne (2008). Biotechnology and Bioengineering. Nova Publishers. pp. 45–. ISBN 978-1-60456-067-1. Retrieved 13 November 2010.
^ ^a ^b ^c ^d ^e Alberts, Bruce; et al.. Molecular Biology of the Cell. Garland Publishing. ISBN 978-0-8153-1619-0. Cite uses deprecated parameters (help)
^ Prydz K, Dalen KT (January 2000). "Synthesis and sorting of proteoglycans". J. Cell. Sci. 113 Pt 2: 193–205. PMID 10633071.
^ Capasso JM, Keenan TW, Abeijon C, Hirschberg CB (1989). "Mechanism of phosphorylation in the lumen of the Golgi apparatus. Translocation of adenosine 5'-triphosphate into Golgi vesicles from rat liver and mammary gland". J. Biol. Chem. 264 (9): 5233–40. PMID 2925690.
^ Swift LL (1996). "Role of the Golgi apparatus in the phosphorylation of apolipoprotein B". J. Biol. Chem. 271 (49): 31491–5. doi:10.1074/jbc.271.49.31491. PMID 8940163.
^ Gubser C, Bergamaschi D, Hollinshead M, Lu X, van Kuppeveld FJ, Smith GL (2007). "A new inhibitor of apoptosis from vaccinia virus and eukaryotes". PLoS Pathog. 3 (2): e17. doi:10.1371/journal.ppat.0030017. PMC 1803007. PMID 17319741.
^ Glick BS, Malhotra V (December 1998). "The curious status of the Golgi apparatus". Cell 95 (7): 883–9. doi:10.1016/S0092-8674(00)81713-4. PMID 9875843.
^ Pelham HR, Rothman JE (2000). "The debate about transport in the Golgi—two sides of the same coin?". Cell 102 (6): 713–9. doi:10.1016/S0092-8674(00)00060-X. PMID 11030615.
^ Glick BS (2000). "Organization of the Golgi apparatus". Curr. Opin. Cell Biol. 12 (4): 450–6. doi:10.1016/S0955-0674(00)00116-2. PMID 10873826.
^ Kimball JW (2009-12-09). "The Golgi Apparatus". Kimball's Biology Pages. Retrieved 2010-09-20.

UpToDate Contents

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1. 抗核抗体染色パターンおよび関連自己抗体の臨床的意義 clinical significance of antinuclear antibody staining patterns and associated autoantibodies
2. 先天性代謝異常：分類 inborn errors of metabolism classification
3. 小児における先天性中枢性低換気症候群および睡眠関連低換気症のその他の原因 congenital central hypoventilation syndrome and other causes of sleep related hypoventilation in children
4. Sequelae of mild traumatic brain injury
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English Journal

The effect of RNAi silencing of p62 using an osmotic polysorbitol transporter on autophagy and tumorigenesis in lungs of K-ras(LA1) mice.

Islam MA1, Shin JY2, Yun CH1, Cho CS3, Seo HW2, Chae C2, Cho MH4.Author information 1Department of Agricultural Biotechnology, Seoul National University, Seoul 151-921, Republic of Korea; Research Institute for Agriculture and Life Sciences, Seoul National University, Seoul 151-921, Republic of Korea; Center for Food and Bioconvergence, Seoul National University, Seoul 151-742, South Korea.2Laboratory of Pathology, College of Veterinary Medicine, Seoul National University, Seoul 151-742, Republic of Korea.3Department of Agricultural Biotechnology, Seoul National University, Seoul 151-921, Republic of Korea; Research Institute for Agriculture and Life Sciences, Seoul National University, Seoul 151-921, Republic of Korea. Electronic address: chocs@snu.ac.kr.4Laboratory of Toxicology, College of Veterinary Medicine, Seoul National University, Seoul 151-742, Republic of Korea; Graduate School of Convergence Science and Technology, Suwon 443-270, Republic of Korea; Graduate Group of Tumor Biology, Seoul National University, Seoul 151-742, Republic of Korea; Advanced Institute of Convergence Technology, Seoul National University, Suwon 443-270, Republic of Korea. Electronic address: mchotox@snu.ac.kr.AbstractTreating cancer patients by conventional chemotherapy to achieve prolonged survival still remains complicated. Autophagy is a topic of considerable interest in recent times, as it may contribute greatly to tumor suppression. Recent studies indicate that autophagy-deficient cells accumulate high levels of p62, an ubiquitin-binding scaffold protein, involved greatly in tumorigenesis. Here, we synthesized an osmotically active polysorbitol-mediated transporter (PSMT) to downregulate p62 using an RNAi strategy and described the mechanism of how p62 silencing using PSMT/siRNA p62 system activates autophagy and contributes to tumor suppression in the lungs of K-ras(LA1) mice. Downregulation of p62 by PSMT/siRNA p62 activated autophagy confirmed by the formation of autophagosomes and swelling of Golgi apparatus with a decreasing level of GM130, a cis-Golgi matrix protein. Activation of osmotic PSMT-mediated autophagy remarkably reduced the size and number of tumors by suppressing proliferative cell nuclear antigen, cluster of differentiation 31, and vascular endothelial growth factor levels. Furthermore, an increase in apoptosis was observed in the lungs of PSMT/siRNA p62-delivered K-ras(LA1) mice.
Biomaterials.Biomaterials.2014 Feb;35(5):1584-96. doi: 10.1016/j.biomaterials.2013.11.010. Epub 2013 Nov 22.
Treating cancer patients by conventional chemotherapy to achieve prolonged survival still remains complicated. Autophagy is a topic of considerable interest in recent times, as it may contribute greatly to tumor suppression. Recent studies indicate that autophagy-deficient cells accumulate high leve
PMID 24269155

DIRECT EVIDENCE OF INTRACRINE ANGIOTENSIN II SIGNALING IN NEURONS.

Deliu E, Brailoiu GC, Eguchi S, Hoffman NE, Rabinowitz JE, Tilley DG, Madesh M, Koch WJ, Brailoiu E.Author information Temple University School of Medicine.AbstractThe existence of a local renin-angiotensin system (RAS) in neurons was first postulated forty years ago. Further studies indicated intraneuronal generation of angiotensin II (ANG II). However, the function and signaling mechanisms of intraneuronal ANG II remained elusive. Since angiotensin II type 1 receptor, AT1, is the major type of receptor mediating the effects of ANG II, we used intracellular microinjection and concurrent calcium and voltage imaging to examine the functionality of intracellular AT1 receptor in neurons. We show here that intracellular administration of ANG II produces a dose-dependent elevation in cytosolic Ca2+ concentration, [Ca2+]i, in hypothalamic neurons, that is sensitive to AT1 receptor antagonism. Endo-lysosomal, but not Golgi apparatus disruption, prevents the effect of microinjected ANG II on [Ca2+]i. Additionally, the ANG II-induced Ca2+ response is dependent on microautophagy and sensitive to inhibition of phospholipase C or antagonism of inositol 1,4,5-trisphosphate receptors. Furthermore, intracellular application of ANG II produces AT1-mediated depolarization of hypothalamic neurons, which was dependent on [Ca2+]i increase and on cation influx via transient receptor potential canonical channels. In summary, in the present study we provide evidence that intracellular ANG II activates endo-lysosomal AT1 receptors in hypothalamic neurons. Our results point to the functionality of a novel intraneuronal angiotensinergic pathway extending the current understanding of intracrine angiotensin II signaling.
American journal of physiology. Cell physiology.Am J Physiol Cell Physiol.2014 Jan 8. [Epub ahead of print]
The existence of a local renin-angiotensin system (RAS) in neurons was first postulated forty years ago. Further studies indicated intraneuronal generation of angiotensin II (ANG II). However, the function and signaling mechanisms of intraneuronal ANG II remained elusive. Since angiotensin II type 1
PMID 24401846

Study of GOLPH3: a Potential Stress-Inducible Protein from Golgi Apparatus.

Li T, You H, Zhang J, Mo X, He W, Chen Y, Tang X, Jiang Z, Tu R, Zeng L, Lu W, Hu Z.Author information Department of Neurology, The Second Xiangya Hospital, Central South University, Changsha, 410011, People's Republic of China, lilisten2011@163.com.AbstractAlthough the Golgi apparatus has been studied extensively for over 100 years, the complex structure-function relationships have yet to be elucidated. It is well known that the Golgi complex plays an important role in the transport, processing, sorting, and targeting of numerous proteins and lipids destined for secretion, plasma membrane, and lysosomes. Increasing evidence suggests that the Golgi apparatus is a sensor and common downstream effector of stress signals in cell death pathways. It undergoes disassembly and fragmentation in several neurological disorders. Recent studies indicate that Golgi phosphoprotein 3 (GOLPH3 also known as GPP34/GMx33/MIDAS), a peripheral membrane protein of trans-Golgi network, represents an exciting new class of oncoproteins involved in cell signal transduction and is potentially mobilized by stress. In this review, we focus on the importance of GOLPH3 in vesicular trafficking, Golgi architecture maintenance, receptor sorting, protein glycosylation, and further discuss its potential in signal sensing in stress response.
Molecular neurobiology.Mol Neurobiol.2014 Jan 7. [Epub ahead of print]
Although the Golgi apparatus has been studied extensively for over 100 years, the complex structure-function relationships have yet to be elucidated. It is well known that the Golgi complex plays an important role in the transport, processing, sorting, and targeting of numerous proteins and lipids
PMID 24395131

Japanese Journal

JB Review : Regulatory mechanisms and cellular functions of non-centrosomal microtubules

The journal of biochemistry 162(1), 1-10, 2017-07
NAID 40021274572

Proteasome impairment in neural cells derived from HMSN-P patient iPSCs

Molecular Brain 10(7), 2017-02-15
NAID 120005971847

ゴルジ体の糖鎖修飾酵素は小胞体とゴルジ体の間を循環するのか？

Ｔｒｅｎｄｓ　ｉｎ　Ｇｌｙｃｏｓｃｉｅｎｃｅ　ａｎｄ　Ｇｌｙｃｏｔｅｃｈｎｏｌｏｇｙ 29(167), J39-J40, 2017
NAID 130005679583

Related Pictures

★リンクテーブル★

リンク元	「ゴルジ装置」「ゴルジ体」
関連記事	「apparatus」

「ゴルジ装置」

　　[★]

英: Golgi apparatus, Golgi complex
ラ: complexus golgiensis
同: 内網装置、ゴルジ複合体、ゴルジ小胞、ゴルジ体 Golgi body、ゴルジ内網装置 Golgi internal reticulum、ディクチオソーム dictyosome
関

機能

1. Distribution center of proteins and lipids from ER to the plasma membrane, lysosomes, and

secretory vesicles

2. Modifies N-oligosaccharides on asparagine
3. Adds O-oligosaccharides to serine and threonine residues
4. Addition of mannose-6-phosphate to specific lysosomal proteins, which targets the protein

to the lysosome

5. Proteoglycan assembly from proteoglycan core proteins
6. Sulfation of sugars in proteoglycans and of selected tyrosine on proteins

臨床関連

I細胞病ムコ脂質症II型

リソソームに行くタンパク質(リソソーム酵素)にマンノース6-リン酸を付加できないため、リソソーム酵素が細胞外に分泌されて症状を起こす疾患。症状は粗い顔貌や関節運動障害(関節の運動が制限される)

「ゴルジ体」

　　[★] ゴルジ装置

同: Golgi apparatus

「apparatus」

　　[★]

n.

装置、器具

関: device、instrument、machine

[isbn3-211-76309-0-1] Pavelk M, Mironov AA (2008). The Golgi Apparatus: State of the art 110 years after Camillo Golgi's discovery. Berlin: Springer. ISBN 3-211-76309-0. ^{[page needed]}

[pmid9865849-2] Fabene PF, Bentivoglio M (1998). "1898–1998: Camillo Golgi and "the Golgi": one hundred years of terminological clones". Brain Res. Bull. 47 (3): 195–8. doi:10.1016/S0361-9230(98)00079-3. PMID 9865849.

[url_molexpress-3] Davidson MW (2004-12-13). "The Golgi Apparatus". Molecular Expressions. Florida State University. Retrieved 2010-09-20.

[url_Dictyosome-4] "Dictyosome". Dictionary.com. Retrieved 2010-09-20.

[wolfe-5] Wolfe SA (1993). Molecular and Cellular Biology. Belmont, CA: Wadsworth Pub. Co. p. 828. ISBN 0-534-12408-9.

[pmid18385516-6] Duran JM, Kinseth M, Bossard C, Rose DW, Polishchuk R, Wu CC, Yates J, Zimmerman T, Malhotra V (2008). "The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis". Mol. Biol. Cell 19 (6): 2579–87. doi:10.1091/mbc.E07-10-0998. PMC 2397314. PMID 18385516.

[becker-7] Becker, Kleinsmith, Hardin, Bertoni (2009). the World of the Cell. San Francisco, CA: Pearson Benjamin Cummings. pp. 333, 339. ISBN 0-321-55418-3.

[lodish-8] Krieger M, Scott MP, Matsudaira PT, Lodish HF, Darnell JE. Lawrence Z, Kaiser C, Arnold B (2004). Molecular cell biology (5th edn ed.). New York: W.H. Freeman and CO. ISBN 0-7167-4366-3.

[9] Chiu, Chi-Fang; Ghanekar, Yashoda; Frost, Laura; Diao, Aipo; Morrison, Daniel; McKenzie, Eddie; Lowe, Martin (2008). "ZFPL1, a novel ring finger protein required for cis-Golgi integrity and efficient ER-to-Golgi transport". The EMBO Journal 27 (7): 934–47. doi:10.1038/emboj.2008.40. PMC 2323254. PMID 18323775.

[10] "Regulated Secretion (Golgi): The Movie". North Dakota State University. Retrieved 2010-11-14.

[Campbell-11] Campbell, Neil A (1996). Biology (4 ed.). Menlo Park, CA: Benjamin/Cummings. pp. 122, 123. ISBN 0-8053-1957-3.

[Flynne2008-12] William G. Flynne (2008). Biotechnology and Bioengineering. Nova Publishers. pp. 45–. ISBN 978-1-60456-067-1. Retrieved 13 November 2010.

[Alberts-13] Alberts, Bruce; et al.. Molecular Biology of the Cell. Garland Publishing. ISBN 978-0-8153-1619-0. Cite uses deprecated parameters (help)

[pmid10633071-14] Prydz K, Dalen KT (January 2000). "Synthesis and sorting of proteoglycans". J. Cell. Sci. 113 Pt 2: 193–205. PMID 10633071.

[pmid2925690-15] Capasso JM, Keenan TW, Abeijon C, Hirschberg CB (1989). "Mechanism of phosphorylation in the lumen of the Golgi apparatus. Translocation of adenosine 5'-triphosphate into Golgi vesicles from rat liver and mammary gland". J. Biol. Chem. 264 (9): 5233–40. PMID 2925690.

[pmid8940163-16] Swift LL (1996). "Role of the Golgi apparatus in the phosphorylation of apolipoprotein B". J. Biol. Chem. 271 (49): 31491–5. doi:10.1074/jbc.271.49.31491. PMID 8940163.

[pmid17319741-17] Gubser C, Bergamaschi D, Hollinshead M, Lu X, van Kuppeveld FJ, Smith GL (2007). "A new inhibitor of apoptosis from vaccinia virus and eukaryotes". PLoS Pathog. 3 (2): e17. doi:10.1371/journal.ppat.0030017. PMC 1803007. PMID 17319741.

[pmid9875843-18] Glick BS, Malhotra V (December 1998). "The curious status of the Golgi apparatus". Cell 95 (7): 883–9. doi:10.1016/S0092-8674(00)81713-4. PMID 9875843.

[pmid11030615-19] Pelham HR, Rothman JE (2000). "The debate about transport in the Golgi—two sides of the same coin?". Cell 102 (6): 713–9. doi:10.1016/S0092-8674(00)00060-X. PMID 11030615.

[pmid10873826-20] Glick BS (2000). "Organization of the Golgi apparatus". Curr. Opin. Cell Biol. 12 (4): 450–6. doi:10.1016/S0955-0674(00)00116-2. PMID 10873826.

[urlThe_Golgi_Apparatus-21] Kimball JW (2009-12-09). "The Golgi Apparatus". Kimball's Biology Pages. Retrieved 2010-09-20.

匿名

検索

案内

案内

Golgi apparatus