scholarly journals Targeting of the "insulin-responsive" glucose transporter (GLUT4) to the regulated secretory pathway in PC12 cells [published erratum appears in J Cell Biol 1993 Sep;122(5):following 1143]

1993 ◽  
Vol 122 (3) ◽  
pp. 579-588 ◽  
Author(s):  
A. W. Hudson
Keyword(s):  
Pc12 Cells ◽  
Secretory Pathway ◽  
Glucose Transporter ◽  
Cell Biol ◽  
Regulated Secretory Pathway ◽  
Glucose Transporter Glut4

Release of interleukin-6 via the regulated secretory pathway in PC12 cells

2006 ◽  
Vol 400 (1-2) ◽  
pp. 75-79 ◽  
Author(s):  
Jens Carsten Möller ◽  
Alex Krüttgen ◽  
Rosi Burmester ◽  
Joachim Weis ◽  
Wolfgang H. Oertel ◽  
...  
Keyword(s):  
Pc12 Cells ◽  
Interleukin 6 ◽  
Secretory Pathway ◽  
Regulated Secretory Pathway

scholarly journals The glucose transporter GLUT4 and the aminopeptidase vp165 colocalise in tubulo-vesicular elements in adipocytes and cardiomyocytes

1997 ◽  
Vol 110 (18) ◽  
pp. 2281-2291 ◽  
Author(s):  
S. Martin ◽  
J.E. Rice ◽  
G.W. Gould ◽  
S.R. Keller ◽  
J.W. Slot ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Secretory Pathway ◽  
Glucose Transporter ◽  
Secretory Granules ◽  
Intact Cells ◽  
Atrial Cardiomyocytes ◽  
Immuno Electron Microscopy ◽  
Double Label ◽  
Regulated Secretory Pathway ◽  
High Degree

The aminopeptidase vp165 is one of the major polypeptides enriched in GLUT4-containing vesicles immuno-isolated from adipocytes. In the present study we have confirmed and quantified the high degree of colocalisation between GLUT4 and vp165 using double label immuno-electron microscopy on vesicles isolated from adipocytes and heart. The percentage of vp165-containing vesicles that also contained GLUT4 was 91%, 76%, and 86% in rat adipocytes, 3T3-L1 adipocytes, and rat heart, respectively. Internalisation of a transferrin/HRP (Tf/HRP) conjugate by 3T3-L1 adipocytes, followed by diaminobenzidine treatment in intact cells, resulted in ablation of only 41% and 45% of GLUT4 and vp165, respectively, whereas endosomal markers are almost quantitatively ablated. Using immuno-electron microscopy on cryosections it was determined that in atrial cardiomyocytes GLUT4 and vp165 colocalised in a population of tubulo-vesicular (T-V) elements that were often found close to the plasma membrane. Double label immunocytochemistry indicated a high degree of overlap in these T-V elements between GLUT4 and vp165. However, in atrial cardiomyocytes a large proportion of GLUT4 was also present in secretory granules containing atrial natriuretic factor (ANF). In contrast, very little vp165 was detected in ANF granules. These data indicate that GLUT4 and vp165 are colocalised in an intracellular, post-endocytic, tubulo-vesicular compartment in adipocytes and cardiomyocytes suggesting that both proteins are sorted in a similar manner in these cells. However, GLUT4 but not vp165 is additionally localised in the regulated secretory pathway in atrial cardiomyocytes.

The Golgi-associated long coiled-coil protein NECC1 participates in the control of the regulated secretory pathway in PC12 cells

2012 ◽  
Vol 443 (2) ◽  
pp. 387-396 ◽  
Author(s):  
David Cruz-García ◽  
Alberto Díaz-Ruiz ◽  
Yoana Rabanal-Ruiz ◽  
Juan R. Peinado ◽  
Francisco Gracia-Navarro ◽  
...  
Keyword(s):  
Golgi Apparatus ◽  
Pc12 Cells ◽  
Secretory Pathway ◽  
Hormone Secretion ◽  
Coiled Coil ◽  
Neuroendocrine Cells ◽  
Peripheral Membrane Protein ◽  
Regulated Secretory Pathway ◽  
Regulated Trafficking ◽  
Golgi Matrix

Golgi-associated long coiled-coil proteins, often referred to as golgins, are involved in the maintenance of the structural organization of the Golgi apparatus and the regulation of membrane traffic events occurring in this organelle. Little information is available on the contribution of golgins to Golgi function in cells specialized in secretion such as endocrine cells or neurons. In the present study, we characterize the intracellular distribution as well as the biochemical and functional properties of a novel long coiled-coil protein present in neuroendocrine tissues, NECC1 (neuroendocrine long coiled-coil protein 1). The present study shows that NECC1 is a peripheral membrane protein displaying high stability to detergent extraction, which distributes across the Golgi apparatus in neuroendocrine cells. In addition, NECC1 partially localizes to post-Golgi carriers containing secretory cargo in PC12 cells. Overexpression of NECC1 resulted in the formation of juxtanuclear aggregates together with a slight fragmentation of the Golgi and a decrease in K+-stimulated hormone release. In contrast, NECC1 silencing did not alter Golgi architecture, but enhanced K+-stimulated hormone secretion in PC12 cells. In all, the results of the present study identify NECC1 as a novel component of the Golgi matrix and support a role for this protein as a negative modulator of the regulated trafficking of secretory cargo in neuroendocrine cells.

scholarly journals Glucose Transporter (GLUT-4) Is Targeted to Secretory Granules in Rat Atrial Cardiomyocytes

1997 ◽  
Vol 137 (6) ◽  
pp. 1243-1254 ◽  
Author(s):  
Jan W. Slot ◽  
Gabriella Garruti ◽  
Sally Martin ◽  
Viola Oorschot ◽  
George Posthuma ◽  
...  
Keyword(s):  
Secretory Pathway ◽  
Glucose Transporter ◽  
Secretory Granules ◽  
Fat Cells ◽  
Atrial Cardiomyocytes ◽  
Glut 4 ◽  
Regulated Secretory Pathway ◽  
The Relationship ◽  
Atrial Cell ◽  
Vesicular Compartment

The insulin-responsive glucose transporter GLUT-4 is found in muscle and fat cells in the transGolgi reticulum (TGR) and in an intracellular tubulovesicular compartment, from where it undergoes insulindependent movement to the cell surface. To examine the relationship between these GLUT-4–containing compartments and the regulated secretory pathway we have localized GLUT-4 in atrial cardiomyocytes. This cell type secretes an antihypertensive hormone, referred to as the atrial natriuretic factor (ANF), in response to elevated blood pressure. We show that GLUT-4 is targeted in the atrial cell to the TGR and a tubulo-vesicular compartment, which is morphologically and functionally indistinguishable from the intracellular GLUT-4 compartment found in other types of myocytes and in fat cells, and in addition to the ANF secretory granules. Forming ANF granules are present throughout all Golgi cisternae but only become GLUT4 positive in the TGR. The inability of cyclohexamide treatment to effect the TGR localization of GLUT-4 indicates that GLUT-4 enters the ANF secretory granules at the TGR via the recycling pathway and not via the biosynthetic pathway. These data suggest that a large proportion of GLUT-4 must recycle via the TGR in insulin-sensitive cells. It will be important to determine if this is the pathway by which the insulin-regulatable tubulo-vesicular compartment is formed.

scholarly journals PC5-A-mediated Processing of Pro-neurotensin in Early Compartments of the Regulated Secretory Pathway of PC5-transfected PC12 Cells

1998 ◽  
Vol 273 (39) ◽  
pp. 25339-25346 ◽  
Author(s):  
Pierre Barbero ◽  
Carole Rovère ◽  
Isabelle De Bie ◽  
Nabil Seidah ◽  
Alain Beaudet ◽  
...  
Keyword(s):  
Pc12 Cells ◽  
Secretory Pathway ◽  
Regulated Secretory Pathway

scholarly journals Transport via the regulated secretory pathway in semi-intact PC12 cells: role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II.

1994 ◽  
Vol 127 (3) ◽  
pp. 693-705 ◽  
Author(s):  
L Carnell ◽  
H P Moore
Keyword(s):  
Pc12 Cells ◽  
Secretory Pathway ◽  
Secretory Granules ◽  
Ph Gradients ◽  
Secretogranin Ii ◽  
Prohormone Processing ◽  
Endoproteolytic Cleavage ◽  
Regulated Secretory Pathway ◽  
Gamma S

To gain insight into the mechanisms governing protein sorting, we have developed a system that reconstitutes both the formation of immature secretory granules and their fusion with the plasma membrane. Semi-intact PC12 cells were incubated with ATP and cytosol for 15 min to allow immature granules to form, and then in a buffer containing 30 microM [Ca2+]free to induce exocytosis. Transport via the regulated pathway, as assayed by the release of secretogranin II (SgII) labeled in the TGN, was inhibited by depletion of ATP, or by the inclusion of 100 microM GTP gamma S, 50 microM AlF3-5 or 5 micrograms/ml BFA. When added after immature granules had formed, GTP gamma S stimulated rather than inhibited exocytosis. Thus, exocytosis of immature granules in this system resembles the characteristics of fully matured granules. Transport of SgII via the regulated pathway occurred at a fourfold higher efficiency than glycosaminoglycan chains, indicating that SgII is sorted to some extent upon exit from the TGN. Addition of A23187 to release Ca2+ from the TGN had no significant effect on sorting of SgII into immature granules. In contrast, depletion of lumenal calcium inhibited the endoproteolytic cleavage of POMC and proinsulin. These results establish the importance of intra-cisternal Ca2+ in prohormone processing, but raise the question whether lumenal calcium is required for proper sorting of SgII into immature granules. Disruption of organelle pH gradients with an ionophore or a weak base resulted in the inhibition of transport via both the constitutive and the regulated pathways.

scholarly journals Somatostatin is targeted to the regulated secretory pathway of gonadotrophs in transgenic mice expressing a metallothionein-somatostatin gene.

1986 ◽  
Vol 261 (34) ◽  
pp. 16260-16263
Author(s):  
M J Low ◽  
P J Stork ◽  
R E Hammer ◽  
R L Brinster ◽  
M J Warhol ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Secretory Pathway ◽  
Regulated Secretory Pathway
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