Inhibition of RabSB expression attenuates Ca2+-dependent exocytosis in rat anterior pituitary cells

Lledo, Pierre−Marie; Verniert, Philippe; Vincent, Jean‐Didier; Mason, William T.; Zorec, Robert

doi:10.1038/364540a0

Cited by 201 publications

(123 citation statements)

References 34 publications

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“…rab3a) and facilitatory rab proteins (Frab) (e.g. rab3b and rab3d) [18,34,35]. Nevertheless, an explanation of how rab3AL would affect rab3a intracellular function and cause stimulation of exocytosis has been offered [23].…”

Section: Discussionmentioning

confidence: 99%

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites

Garde

Roldán

1996

FEBS Letters

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Aerosomal exocytosis triggered with A23187/Ca 2+ was enhanced by rab3AL, a synthetic peptide corresponding to the effector domain of the small GTP-binding protein rab3. Exocytosis was further enhanced when spermatozoa were also exposed to dihutyryl-cAMP, but was prevented when H-89, a protein kinase A (PKA) inhibitor, was included. The action of rab3AL was not on, or upstream of, phospholipase A2 (PLA2). Inhibition of exocytosis by the PLA2 inhibitor aristolochic acid was overcome by rab3AL when it was included together with lysophosphatidylcholine; this effect was prevented by H-89. These results suggest a functional coupling between rab3 protein, metabolites generated by PLA2, and cAMP-activated PKA, in the final steps leading to membrane fusion during acrosomal exocytosis.Key words: Exocytosis; rab3; Phospholipase Az; Lysophosphatidylcholine; cAMP; Spermatozoa that regulate docking and fusion of secretory granules with the plasma membrane [16][17][18][19].Synthetic peptides corresponding to a putative effector domain of rab3 proteins have been shown to stimulate exocytosis in permeabilized [20 23] and intact cells [24], and membrane fusion in a cell-free assay system [25]. We have therefore used a sperm model system, where cells are stimulated to undergo exocytosis with A23187/Ca 2+, to explore whether rab3 might be involved in the final steps of membrane fusion during acrosomal exocytosis. We present, for the first time, evidence suggesting that rab3 protein, together with PLA2-derived metabolites and the cAMP/PKA signalling pathway, play an important role during the final steps of acrosomal exocytosis in mammalian spermatozoa. Materials and methods

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Section: Discussionmentioning

confidence: 99%

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites

Garde

Roldán

1996

FEBS Letters

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“…The two forms of Rab protein are converted from one to the other by the action of GDP/GTP exchange factors and GTPase-activating proteins. While many Rab proteins are ubiquitously expressed, the Rab3 family proteins (Rab3A,Rab3B,Rab3C,and Rab3D) are enriched in the brain and secretory tissues, and have proven to be associated with Ca 2+ -regulated exocytosis in mammals (Lledo et al 1993;Fischer von Mollard et al 1994;Castillo et al 1997;Chen et al 2002). Rab3A, the best-characterized member of the Rab3 subfamily, is a predominant isotype present in neurons and amine/peptide-secreting endocrine cells, controlling calcium-dependent exocytosis as a positive or negative regulator (Holz et al 1994;Lledo et al 1994;Regazzi et al 1996;Takai et al 1996, Geppert andSudhöf 1998;Yaekura et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Cellular expression of Noc2, a Rab effector protein, in endocrine and exocrine tissues in the mouse

Teramae

Fujimoto

Seino

et al. 2006

Histochem Cell Biol

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Noc2 is a Rab effector which participates in regulated exocytosis. It is expressed abundantly in endocrine cells but at low levels in exocrine tissues. Noc2-deficient mice, however, exhibit marked accumulation of secretory granules in exocrine cells rather than endocrine cells. In the present study, we investigated localization of Noc2 immunohistochemically in various endocrine and exocrine tissues in normal mice.Western blotting detected a Noc2-immunoreactive band of 38 kDa in isolated pancreatic islets, the adrenal gland, pituitary gland, and thyroid gland. Immunostaining for Noc2 labeled endocrine cells in the adrenal medulla and adenohypophysis, pancreatic islet cells, thyroid parafollicular cells, and gut endocrine cells, supporting the notion that Noc2 is a Rab effector protein shared by amine/peptide-secreting endocrine cells.

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“…It has been shown that SNAP-25 is essential in the regulated release of adrenocorticotropin (ACTH) and prolactin (PRL) from AtT-20 and GH3 cell lines respectively , Masumoto et al 1997. In addition, different members of the Rab family are involved in secretory granule localization and calciuminduced exocytosis in anterior pituitary cells (Lledo et al 1993, Nsee et al 1993, Perez et al 1994.…”

Section: Introductionmentioning

confidence: 99%

Exocytotic protein components in rat pituitary gland after long-term estrogen administration

Majó

Lorenzo²,

Blasi³

et al. 1999

Journal of Endocrinology

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Recently, a set of proteins involved in the docking and fusion machinery of secretory organelles has been identified in anterior pituitary cells. In this study we analyzed, by Western blotting and immunocytochemistry, the expression of several proteins involved in exocytosis after long-term administration of 17 -estradiol (E 2 ) in Fischer 344 rats. No differences were observed in the amount of synaptosomal-associated protein of 25 kDa, synaptobrevin 2, syntaxin 1, synaptotagmin I and Rab3a in total brain homogenates from treated rats after E 2 administration. In striking contrast, the levels of all of these exocytotic proteins, including cellubrevin, were notably decreased in pituitary glands of E 2 -treated rats. In addition, no differences were observed in the in vitro basal and 8-Br-cAMPinduced prolactin (PRL) release between pituitary cells from control and E 2 -treated rats, whereas TRH-induced PRL release in anterior pituitary cells from E 2 -treated animals was higher than in control donors. In conclusion, this study shows that protein components of the exocytotic machinery are specifically down-regulated in the pituitary gland of E 2 -treated Fischer 344 rats.

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Inhibition of RabSB expression attenuates Ca2+-dependent exocytosis in rat anterior pituitary cells

Cited by 201 publications

References 34 publications

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites

Cellular expression of Noc2, a Rab effector protein, in endocrine and exocrine tissues in the mouse

Exocytotic protein components in rat pituitary gland after long-term estrogen administration

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Inhibition of RabSB expression attenuates Ca2+-dependent exocytosis in rat anterior pituitary cells

Cited by 201 publications

References 34 publications

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A2 metabolites

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A2 metabolites

Cellular expression of Noc2, a Rab effector protein, in endocrine and exocrine tissues in the mouse

Exocytotic protein components in rat pituitary gland after long-term estrogen administration

Contact Info

Product

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rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites