Relation of Rab26 to the amylase release from rat parotid acinar cells

Nashida, Tomoko; Imai, Akane; Shimomura, Hiromi

doi:10.1016/j.archoralbio.2005.06.005

Cited by 44 publications

(38 citation statements)

References 33 publications

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“…However, these earlier results were generated using antibody staining in fixed tissue sections and cell fractionation density gradient enrichment of granules (Nashida et al, 2006;Yoshie et al, 2000). In fact, secretory granules and lysosomes are not easily distinguishable by density gradient properties (Pasquali et al, 1999), and the mature secretory granule markers, syntaxin 6 and c-adaptin, used as markers of secretory granules in previous analyses of RAB26, are also involved in Golgi sorting to lysosomes and late endosomes (Ghosh et al, 2003;Robinson, 1990).…”

Section: Discussionmentioning

confidence: 99%

“…We had previously shown that interfering with RAB26 function inhibited MIST1-mediated granulogenesis (Tian et al, 2010) and hypothesized, based on the initial descriptive publications (Nashida et al, 2006;Wagner et al, 1995;Yoshie et al, 2000), that RAB26 would function somehow to traffic nascent or maturing secretory granules. To study RAB26-secretory-granule interactions, we induced a network of secretory granules by the transfecting secretory cargo RFPtagged Pepsinogen C, in cells stably expressing MIST1, a system we have previously described (Tian et al, 2010).…”

Section: Rab26 Localizes Specifically To Lamp1 Lysosomal Membraneassomentioning

confidence: 99%

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RAB26 coordinates lysosome traffic and mitochondrial localization

Jin

Mills

2014

Journal of Cell Science

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As they mature, professional secretory cells like pancreatic acinar and gastric chief cells induce the transcription factor MIST1 (also known as BHLHA15) to substantially scale up production of large secretory granules in a process that involves expansion of apical cytoplasm and redistribution of lysosomes and mitochondria. How a scaling factor like MIST1 rearranges cellular architecture simply by regulating expression levels of its transcriptional targets is unknown. RAB26 is a MIST1 target whose role in MIST1-mediated secretory cell maturation is also unknown. Here, we confirm that RAB26 expression, unlike most Rabs which are ubiquitously expressed, is tissue specific and largely confined to MIST1-expressing secretory tissues. Surprisingly, functional studies showed that RAB26 predominantly associated with LAMP1/cathepsin D lysosomes and not directly with secretory granules. Moreover, increasing RAB26 expression -by inducing differentiation of zymogensecreting cells or by direct transfection -caused lysosomes to coalesce in a central, perinuclear region. Lysosome clustering in turn caused redistribution of mitochondria into distinct subcellular neighborhoods. The data elucidate a novel function for RAB26 and suggest a mechanism for how cells could increase transcription of key effectors to reorganize subcellular compartments during differentiation.

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Section: Discussionmentioning

confidence: 99%

Section: Rab26 Localizes Specifically To Lamp1 Lysosomal Membraneassomentioning

confidence: 99%

RAB26 coordinates lysosome traffic and mitochondrial localization

Jin

Mills

2014

Journal of Cell Science

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“…The molecular mechanisms involved in fusion of exocytotic structures with the plasma membrane have been reviewed by Watson (1999), Gerber and Sudhof (2002), Wasle and Edwardson (2002), and Burgoyne and Morgan (2003). The presence of the spherule adjacent to the granule membrane might result in the selective adherence of a protein from the cytosol [such as ADP-ribosylation factor (Arf) , VAMP-2 (FujitaYoshigaki et al, 1998), rap1 (D'Silva et al, 1997), Rab3D (Ohnishi et al, 1996)] or Rab26 (Nashida et al, 2006), which ordinarily appear to be disposed over the entire granule surface and that could act as a docking protein. Another candidate is synexin or a synexin-like molecule, which has been proposed as a recognition protein that mediates fusion of chromaffin granules with the plasma membrane of cells in the adrenal medulla (Pollard et al, 1979).…”

Section: Discussionmentioning

confidence: 99%

Serous Cells in the Parotid Glands of Two Species of Tamarins: Polarized Secretory Granules

Tandler

2008

The Anatomical Record

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The parotid glands of two species of tamarins were examined by electron microscopy. Endpiece cells are typical in appearance, with an extensive rough endoplasmic reticulum, prominent Golgi apparatuses, and numerous serous granules. In the saddleback tamarin, the secretory granules contain a dense spherule pressed against the inner aspect of the limiting membrane, leading to a surface bulge. During the course of merocrine secretion (a form of exocytosis), such morphologically polarized granules approach the luminal plasma membranes with the bulge in the vanguard. It is these protuberances that fuse with the plasmalemma. In contrast, although serous granules in the cotton top tamarin contain a spherule, they lack surface bulges and their docking on luminal membranes seems to be a random event with respect to their surface morphology. Moreover, certain other types of cells in a taxonomically wide spectrum of species have granules with a less obvious structural polarity, as well as cells whose granules lack morphological polarity but have a functional polarity that comes into play during exocytosis of such secretory granules.

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“…These effects may be due to glandular denervation induced by inhibition of the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors involved in acetylcholine release at the neuroglandular junction and also inhibition of those involved in exocytosis of the granula of the acinar cells 15 . In this way, a temporary chemical denervation of the target organ is established 16,17 . This explanation is supported by Schneyer and Hall 18 and Ekstrom and Reinhold 19 , who found that parasympathetic denervation by sectioning of the chorda tympani in rats resulted a decrease in the weight of the submandibular gland, by between 15 and 30%, and caused the acinar cells to shrink.…”

Section: All Authors Contributed To Conception and Design Manuscriptmentioning

confidence: 99%

Untitled

2013

Annals of Oral and Maxillofacial Surgery

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Introduction Intraglandular injection of botulinum toxin A into the salivary glands is the effective treatment option for sialorrhoea in children with cerebral palsy or other neurological diseases without any severe side-effects. It results in transient denervation of the gland, which helps in reducing salivary secretion. The aim of this study was to evaluate histological changes in the rats' parotid glands after accidental or intended intraglandular injection of botulinum toxin A in patients with bruxism or sialorrhoea. Materials and methodsAfter 20 days of the botulinum toxin A injection, tissue specimens of the right parotid gland were obtained from 15 albino rats, while the specimens of left parotid gland were used as control. Ordinary light microscopy and electron microscopy were used to detect the morphological changes in the injected parotid glands. Results Morphological and ultrastructural analyses of the cell organelles and secretory granules showed a clear atrophy of the acini in glands injected with the botulinum toxin A. Acinar cells revealed significant morphologic variations in rough

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Relation of Rab26 to the amylase release from rat parotid acinar cells

Cited by 44 publications

References 33 publications

RAB26 coordinates lysosome traffic and mitochondrial localization

RAB26 coordinates lysosome traffic and mitochondrial localization

Serous Cells in the Parotid Glands of Two Species of Tamarins: Polarized Secretory Granules

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