Correlated changes of Balbiani ring expansion and secretory protein synthesis in larval salivary glands ofChironomus tentans

Chromosoma ◽  
1976 ◽  
Vol 58 (2) ◽  
pp. 137-153 ◽  
Author(s):  
Walter Pankow ◽  
Markus Lezzi ◽  
Ingrid Holderegger-M�hling
Keyword(s):  
Protein Synthesis ◽  
Salivary Glands ◽  
Ring Expansion ◽  
Secretory Protein ◽  
Balbiani Ring

Concomitant induction of a Balbiani ring and a giant secretory protein in Chironomus salivary glands

Chromosoma ◽  
1980 ◽  
Vol 81 (1) ◽  
pp. 115-124 ◽  
Author(s):  
J. -E. Edstr�m ◽  
L. Rydlander ◽  
C. Francke
Keyword(s):  
Salivary Glands ◽  
Secretory Protein ◽  
Balbiani Ring

scholarly journals A novel giant secretion polypeptide in Chironomus salivary glands: implications for another Balbiani ring gene.

1985 ◽  
Vol 101 (3) ◽  
pp. 1044-1051 ◽  
Author(s):  
W Y Kao ◽  
S T Case
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Salivary Glands ◽  
Cyanogen Bromide ◽  
Tryptic Peptide ◽  
Amino Acid Sequences ◽  
The Other ◽  
Balbiani Ring ◽  
Sequence Organization ◽  
Peptide Maps

Chironomus salivary glands contain a family of high Mr (approximately 1,000 X 10(3)) secretion polypeptides thought to consist of three components: sp-Ia, sp-Ib, and sp-Ic. The use of a new extraction protocol revealed a novel high Mr component, sp-Id. Results of a survey of individual salivary glands indicated that sp-Id was widespread in more than a dozen strains of C. tentans and C. pallidivittatus. Sp-Id was phosphorylated at Ser residues, and a comparison of cyanogen bromide and tryptic peptide maps of 32P-labeled polypeptides suggested that sp-Ia, sp-Ib, and sp-Id are comprised of similar but nonidentical tandemly repeated amino acid sequences. We concluded that sp-Id is encoded by an mRNA whose size and nucleotide sequence organization are similar to Balbiani ring (BR) mRNAs that code for the other sp-I components. Furthermore, parallel repression of sp-Ib and sp-Id synthesis by galactose led us to hypothesize that both of their genes exist within Balbiani ring 2.

Effects of calcium on synthesis and secretion of parathyroid hormone and secretory protein I

1988 ◽  
Vol 255 (3) ◽  
pp. E299-E305
Author(s):  
R. R. MacGregor ◽  
D. A. Hinton ◽  
R. D. Ridgeway
Keyword(s):  
Protein Synthesis ◽  
Steady State ◽  
Parathyroid Hormone ◽  
Total Protein ◽  
Secretory Protein ◽  
Hormone Synthesis ◽  
Synthesis And Degradation

Bovine parathyroid organoids were cultured for up to 3 wk in medium containing 1.4 or 1.8 mM calcium. Steady-state secretion of parathyroid hormone and secretory protein I was two- to fourfold greater at 1.4 mM. At the end of culture, organoids were incubated 3.5 h in 1 or 2 mM calcium to examine maximum and minimum acute secretory rates. Relative to organoids cultured at 1.8 mM calcium, culture at 1.4 mM induced a hypersecretory state, i.e., both the maximum and minimum acute secretory rates of organoids previously cultured at 1.4 mM calcium were up to threefold greater than those of organoids previously at 1.8 mM calcium. Proparathyroid hormone synthesis was up to 50% greater in organoids cultured at 1.4 mM calcium, whereas secretory protein I and total protein synthesis were unaltered. The results showed that parathyroid hypersecretion can be induced by chronic hypocalcemic conditions in vitro. We conclude that the secretory adaptation to chronic hypocalcemia in vitro involves alterations in both synthesis and degradation of parathyroid hormone.

scholarly journals Nuclear localization of a DNA-binding C-terminal domain from Balbiani ring coded secretory protein.

1988 ◽  
Vol 7 (12) ◽  
pp. 3881-3888 ◽  
Author(s):  
L. Botella ◽  
C. Grond ◽  
H. Saiga ◽  
J. E. Edström
Keyword(s):  
Dna Binding ◽  
Nuclear Localization ◽  
Secretory Protein ◽  
Balbiani Ring ◽  
Terminal Domain

scholarly journals Antiribophorin antibodies inhibit the targeting to the ER membrane of ribosomes containing nascent secretory polypeptides.

1990 ◽  
Vol 111 (4) ◽  
pp. 1335-1342 ◽  
Author(s):  
Y H Yu ◽  
D D Sabatini ◽  
G Kreibich
Keyword(s):  
Protein Synthesis ◽  
Polyclonal Antibodies ◽  
Liver Microsomes ◽  
Inhibitory Effect ◽  
Secretory Protein ◽  
Rat Liver Microsomes ◽  
Membrane Glycoproteins ◽  
Site Specific ◽  
Dog Pancreas ◽  
Er Membrane

Polyclonal antibodies directed against ribophorins I and II, two membrane glycoproteins characteristic of the rough endoplasmic reticulum, inhibit the cotranslational translocation of a secretory protein growth hormone into the lumen of dog pancreas or rat liver microsomes. As expected, site-specific antibodies to epitopes located within the cytoplasmic domain of ribophorin I, but not antibodies to epitopes in the luminal domain of this protein, were effective in inhibiting translocation. Since monovalent Fab fragments were as inhibitory as intact IgG molecules, ribophorins must be closely associated with the translocation site and, therefore, are likely to function at some stage in the translocation process. In all cases, the antibodies that inhibited translocation also caused a significant reduction in total protein synthesis and treatments that neutralized their capacity to inhibit translocation also prevented their inhibitory effect on protein synthesis. This would be expected if the antibodies blocked the membrane-mediated relief of the SRP-induced arrest of polypeptide elongation. The antibodies were effective only when added before translocation was allowed to begin. In this case, they prevented the targeting of active ribosomes containing mRNA and nascent chains to the ER membrane. Thus, ribophorins must either directly participate in targeting or be so close to the targeting site that the antibodies sterically blocked this early phase of the translocation process.

Androgen-regulated expression of secretory protein synthesis in mouse ventral prostate

1987 ◽  
Vol 53 (1-2) ◽  
pp. 111-118 ◽  
Author(s):  
John S. Mills ◽  
Maurice Needham ◽  
Timothy C. Thompson ◽  
Malcolm G. Parker
Keyword(s):  
Protein Synthesis ◽  
Secretory Protein ◽  
Ventral Prostate ◽  
Regulated Expression
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