Golgi Apparatus, Gerl, and Lysosomes of Neurons in Rat Dorsal Root Ganglia, Studied by Thick Section and Thin Section Cytochemistry

Novikoff, Phyllis M.; Novikoff, Alex B.; Quintana, Nelson; Hauw, Jean‐Jacques

doi:10.1083/jcb.50.3.859

Cited by 556 publications

(240 citation statements)

References 50 publications

Supporting

Mentioning

219

Contrasting

Unclassified

Order By: Relevance

“…These observations confirm and extend older work by P. M. Novikoff, A. B. Novikoff, and colleagues who proposed a direct interface between the trans-part of the Golgi and smooth ER continuous with the rough ER based on stained thick sections (Novikoff et al, 1971). This observation led to the well-known Golgi endoplasmic reticulum lysosome hypothesis postulating a direct anterograde route from the ER to outer Golgi membrane elements.…”

Section: Rab6supporting

confidence: 90%

Regulation of Microtubule-dependent Recycling at theTrans-Golgi Network by Rab6A and Rab6A'

Young

Stauber

Nery

et al. 2005

MBoC

105

126

View full text Add to dashboard Cite

The small GTPase rab6A but not the isoform rab6A has previously been identified as a regulator of the COPIindependent recycling route that carries Golgi-resident proteins and certain toxins from the Golgi to the endoplasmic reticulum (ER). The isoform rab6A has been implicated in Golgi-to-endosomal recycling. Because rab6A but not A , binds rabkinesin6, this motor protein is proposed to mediate COPI-independent recycling. We show here that both rab6A and rab6A GTP-restricted mutants promote, with similar efficiency, a microtubule-dependent recycling of Golgi resident glycosylation enzymes upon overexpression. Moreover, we used small interfering RNA mediated down-regulation of rab6A and A' expression and found that reduced levels of rab6 perturbs organization of the Golgi apparatus and delays Golgi-to-ER recycling. Rab6-directed Golgi-to-ER recycling seems to require functional dynactin, as overexpression of p50/dynamitin, or a C-terminal fragment of Bicaudal-D, both known to interact with dynactin inhibit recycling. We further present evidence that rab6-mediated recycling seems to be initiated from the trans-Golgi network. Together, this suggests that a recycling pathway operates at the level of the trans-Golgi linking directly to the ER. This pathway would be the preferred route for both toxins and resident Golgi proteins. INTRODUCTIONAnterograde flow of material through the exocytic pathway is offset by the constant recycling of both proteins and lipids. This recycling helps to ensure that steady-state distributions of resident proteins are maintained within the pathway at the same time as keeping a lipid balance. Besides intra-Golgi recycling between cisternae (Hoe et al., 1995;Love et al., 1998;Lanoix et al., 1999;Lin et al., 1999), Golgi glycosylation enzymes also can recycle directly to the endoplasmic reticulum (ER). It is estimated that at least 5% of Golgi resident enzymes reside in the ER, at steady state (Pelletier et al., 2000). This pool constitutes recycled material originating from the Golgi apparatus (Cole et al., 1998;Storrie et al., 1998).The extent of ER recycling of Golgi resident membrane proteins is sufficient to allow for complete assembly of functional Golgi stacks. Thus, upon addition of nocodazole to depolymerize microtubules, the central and juxtanuclear Golgi apparatus relocates to the 100 or so peripheral ER exit sites scattered throughout the cell. This microtubule-independent relocation occurs in the absence of any detectable elements tracking outwards from the central Golgi apparatus. Rather, the Golgi apparatus undergoes a molecular deconstruction in the trans-to-cis-direction, i.e., resident glycosylation enzymes of the trans-cisternae/trans-Golgi network (TGN) relocate with faster kinetics than do enzymes of the medial-cisternae (Yang and Storrie, 1998). Enzymes seemingly enter the ER close to the microtubule organizing center (MTOC), diffuse through the ER, and then reemerge at peripheral ER exit sites. Here, Golgi stacks are then reassembled into discrete, yet fully functiona...

show abstract

Section: Rab6supporting

confidence: 90%

Regulation of Microtubule-dependent Recycling at theTrans-Golgi Network by Rab6A and Rab6A'

Young

Stauber

Nery

et al. 2005

MBoC

105

126

View full text Add to dashboard Cite

show abstract

“…The reaction products, localized in Golgi apparatus, were found also in tissue incubated in the presence of 20 mm 3-amino-1,2,4, triazole) (Fig. 3d), thus indicating that the staining is not due to peroxidatic activity of catalase (20). No reaction products were detected in the nucleus, nucleolus, or ribosomes as reported by others (22,24).…”

Section: Methodssupporting

confidence: 60%

Cell Wall and Protoplast Isoperoxidases in Tobacco Plants in Relation to Mechanical Injury and Infection with Tobacco Mosaic Virus

Birecka¹,

Catalfamo²,

Urban³

1975

Plant Physiol.

View full text Add to dashboard Cite

Leaves and pith of Turkish, Wisconsin 38, and Samsun NN tobacco (Nicotiana tabacum) varieties, which differ in their sensitivity to tobacco mosaic virus, showed the same qualitative isoperoxidase patterns and a similar distribution of distinctive isoperoxidases between the cell protoplast and wall-free, ionically, and covalently bound fractions. No changes in the qualitative isoenzyme spectrum were found in relation to age, mechanical injury, or leaf infection with tobacco mosaic virus. The distinctive isoperoxidases which reacted to infection were the same as those responsive to mechanical injury, confirming that the enzyme reaction to infection results from a nonspecific response to injury. The increase in peroxidase activity in response to infection or mechanical injury, or both, was greater in young tissue than in the older ones. The great increase in Samsun NN leaves and no increase in those of the two other varieties in response to infection may be due to differences in the degree to which the pathogen affected processes controlling the nonspecific peroxidase reaction to injury. Peroxidase development in the infected Samsun NN leaves was due to isoenzymes which form the wall-bound fraction in very young tissues, and to those which increase in activity with aging in the protoplast and wall-free fractions. In mechanically injured tissue, only the first group of isoenzymes increased in activity. In Samsun NN plants, the increased peroxidase activity in upper intact leaves above the infected ones was only due to isoenzymes whose activity increases with both normal and virus-accelerated senescence. Peroxidase reaction to challenge inoculation in these leaves was the same whether the lower ones were intact, infected and/or mechanically injured. Thus, the induced systemic resistance to tobacco mosaic virus may be due to other than peroxidase factors.In infected tissues, peroxidase was detected in the endoplas. mic reticulum, Golgi apparatus, vacuole, cell wall, and intercellular spaces. The Golgi vesicles were often localized near the tonoplast and plasmalemma, fusing with membranes and secreting their contents. The possible "rejuvenating" effects of injury on synthesis and transport of distinctive isoperoxidases are discussed.eases. Systemic-induced resistance to TMV' in the hypersensitive Samsun NN tobacco plants (9) has been also related to peroxidase; increased peroxidase activity leading to production of toxic compounds causes early killing of infected cells and early formation of a barrier to viral spread (30, 31). Increases in the activity of peroxidase in infected organs, usually referred to the soluble fraction of this enzyme, are assumed by many to result from a nonspecific host response (2,11,18,27,32,34), although new soluble isoperoxidases are claimed to appear in some infected tissues (2,8,10,11,26).Previous study on Wisconsin 38 tobacco plant pith has shown a great increase of peroxidase activity, not only in its protoplast fraction, but also in the wall-bound fraction in response to cuttin...

show abstract

“…As in earlier studies from our laboratory (10,11), two phosphatase markers are used to distinguish the Golgi apparatus from GERL. The trans (12) element of the Golgi apparatus shows thiamine pyrophosphatase (TPPase) activity whereas GERL does not.…”

mentioning

confidence: 99%

“…On the other hand, GERL shows activity for acid phosphatase [orthophosphoric-monoester phosphohydrolase ( 7.4 and 0.25% CaCl2 (13) and fixed for 3 hr. Further processing for morphological study by electron microscopy has been described elsewhere (10). Electron microscopic localizations of TPPase and AcPase activities were determined as previously described (10,11) except that in the present experiments the nonfrozen "chopper" sections were 20,um thick.…”

mentioning

confidence: 99%

Cytochemical study of secretory process in transplantable insulinoma of syrian golden hamster.

Novikoff¹,

Yam²,

Novikoff³

1975

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Concerning the intracellular localization of this conversion, Steiner et al. (2) have suggested that this conversion "probably begins when the polypeptide reaches the Golgi apparatus and continues for several hours after new secretory granules have formed within the lamellae of the Golgi apparatus." It was of interest to study the roles, if any, of GERL* and of the ER outside of the Golgi zone in such secretory granule packaging.

show abstract

Golgi Apparatus, Gerl, and Lysosomes of Neurons in Rat Dorsal Root Ganglia, Studied by Thick Section and Thin Section Cytochemistry

Cited by 556 publications

References 50 publications

Regulation of Microtubule-dependent Recycling at theTrans-Golgi Network by Rab6A and Rab6A'

Regulation of Microtubule-dependent Recycling at theTrans-Golgi Network by Rab6A and Rab6A'

Cell Wall and Protoplast Isoperoxidases in Tobacco Plants in Relation to Mechanical Injury and Infection with Tobacco Mosaic Virus

Cytochemical study of secretory process in transplantable insulinoma of syrian golden hamster.

Contact Info

Product

Resources

About