Improved processing of secretory proteins in Hansenula polymorpha by sequence variation near the processing site of the alpha mating factor prepro sequence

2013 ◽  
Vol 167 (2) ◽  
pp. 94-100 ◽  
Author(s):  
Eva Eilert ◽  
Theresa Rolf ◽  
Andreas Heumaier ◽  
Cornelis P. Hollenberg ◽  
Michael Piontek ◽  
...  
Keyword(s):  
Sequence Variation ◽  
Hansenula Polymorpha ◽  
Secretory Proteins ◽  
Processing Site ◽  
Mating Factor

Ultrastructural Aspects of Golgi Complex Function in Parathyroid Cells of Winter Frogs

1973 ◽  
Vol 31 ◽  
pp. 680-681
Author(s):  
William J. Dougherty
Keyword(s):  
Golgi Complex ◽  
Secretory Granules ◽  
Complex Function ◽  
Secretory Activity ◽  
Secretory Proteins ◽  
Perivascular Spaces ◽  
Pituitary Cells ◽  
Electron Microscopic ◽  
Ca Ions ◽  
Regulation Of Secretion

The regulation of secretion in exocrine and endocrine cells has long been of interest. Electron microscopic and other studies have demonstrated that secretory proteins synthesized on ribosomes are transported by the rough ER to the Golgi complex where they are concentrated into secretory granules. During active secretion, secretory granules fuse with the cell membrane, liberating and discharging their contents into the perivascular spaces. When secretory activity is suppressed in anterior pituitary cells, undischarged secretory granules may be degraded by lysosomes. In the parathyroid gland, evidence indicates that the level of blood Ca ions regulates both the production and release of parathormone. Thus, when serum Ca is low, synthesis and release of parathormone are both stimulated; when serum Ca is elevated, these processes are inhibited.

Fate of T Cells and their Secretory Proteins During the Progression of Leprosy

2018 ◽  
Vol 19 (9) ◽  
pp. 889-899 ◽  
Author(s):  
Mohd Tarique ◽  
Chaman Saini ◽  
Huma Naz ◽  
Raza Ali Naqvi ◽  
Faez Iqbal Khan ◽  
...  
Keyword(s):  
T Cells ◽  
Secretory Proteins
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