Posttranslational processing of gastrin

1989 ◽  
Vol 69 (2) ◽  
pp. 482-502 ◽  
Author(s):  
D. Daugherty ◽  
T. Yamada
Keyword(s):  
Posttranslational Processing

Posttranslational processing and identification of a neutralization domain of the GP4 protein encoded by ORF4 of Lelystad virus.

1997 ◽  
Vol 71 (8) ◽  
pp. 6061-6067 ◽  
Author(s):  
J J Meulenberg ◽  
A P van Nieuwstadt ◽  
A van Essen-Zandbergen ◽  
J P Langeveld
Keyword(s):  
Posttranslational Processing ◽  
Lelystad Virus

Posttranslational Processing of Proteins

1993 ◽  
pp. 191-235
Author(s):  
Johannes M. F. G. Aerts ◽  
André W. Schram
Keyword(s):  
Posttranslational Processing

Cell-specific posttranslational processing of the surfactant-associated protein SP-B

1993 ◽  
Vol 264 (3) ◽  
pp. L290-L299 ◽  
Author(s):  
S. Hawgood ◽  
D. Latham ◽  
J. Borchelt ◽  
D. Damm ◽  
T. White ◽  
...  
Keyword(s):  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Cell Types ◽  
Specific Protein ◽  
Precursor Protein ◽  
Type Ii Cells ◽  
Posttranslational Processing ◽  
Type Ii ◽  
Clara Cells ◽  
Ovary Cells

Pulmonary surfactant-associated protein B (SP-B) is a 9-kDa lung-specific protein expressed in alveolar epithelial type II cells and Clara cells. The protein markedly increases the surface activity of phospholipids and is an active component in some surfactants in clinical use. SP-B is produced from a 43-kDa precursor protein by proteolytic cleavage of flanking regions from both the NH2- and COOH-terminal ends of the active protein. In this study we have compared the nature of the posttranslational processing of the SP-B precursor in type II cells and in a heterologous cell line transfected with the SP-B precursor. We found that isolated type II cells produce the 9-kDa form of SP-B from the precursor through a series of intermediates detectable in the cell lysates. In contrast Chinese hamster ovary cells stably transfected with the full-length human SP-B precursor produce the precursor and a 26-kDa intermediate but not the 9-kDa protein. The precursor protein in both cell types is glycosylated with NH2-linked sugars. Our results suggest there is cell specificity in the posttranslational processing of the SP-B precursor.

Effects of Monensin on Posttranslational Processing of Myelin Proteins

1983 ◽  
Vol 40 (5) ◽  
pp. 1333-1339 ◽  
Author(s):  
Laurace E. Townsend ◽  
Joyce A. Benjamins
Keyword(s):  
Myelin Proteins ◽  
Posttranslational Processing

Insulin modulates PC-1 processing and recruitment in cultured human cells

2003 ◽  
Vol 284 (3) ◽  
pp. E514-E520 ◽  
Author(s):  
C. Menzaghi ◽  
R. Di Paola ◽  
G. Baj ◽  
A. Funaro ◽  
A. Arnulfo ◽  
...  
Keyword(s):  
Gene Expression ◽  
Plasma Membrane ◽  
Intracellular Trafficking ◽  
Posttranslational Processing ◽  
Phosphatidylinositol 3 Kinase ◽  
S6 Kinase ◽  
Fourfold Increase ◽  
Membrane Recruitment ◽  
Insulin Receptor Signaling ◽  
Cultured Human Cells

We evaluated whether insulin signaling modulates plasma cell glycoprotein (PC-1) plasma membrane recruitment, posttranslational processing, and gene expression in human cultured cell lines. Insulin induced a fourfold increase ( P < 0.01) of membrane PC-1 expression by rapid and sensitive mechanism(s). This effect was reduced ( P < 0.05–0.01) by inhibition of phosphatidylinositol 3-kinase (200 nmol/l wortmannin) and S6 kinase (50 nmol/l rapamycin) activities and intracellular trafficking (50 μmol/l monensin) and was not accompanied by PC-1 gene expression changes. Moreover, at Western blot, insulin elicited the appearance, in both plasma membrane and cytosol, of a PC-1-related 146-kDa band (in addition to bands of 163, 117, 106, and 97 kDa observed also in absence of insulin) that was sensitive to endoglycosidase H. Finally, inhibition of PC-1 translocation to plasma membrane, by wortmannin pretreatment, increases insulin-stimulated receptor autophosphorylation. Our data indicate that insulin stimulates PC-1 posttranslational processing and translocation to the plasma membrane, which in turn impairs insulin receptor signaling. Bidirectional cross talk between insulin and PC-1, therefore, takes place, which may be part of the hormone self-desensitization mechanism.

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