Secretory Protein Synthesis and Constitutive (Vesicular) Secretion by Salivary Glands

1998 ◽  
pp. 73-88 ◽  
Author(s):  
G.B. Proctor
Keyword(s):  
Protein Synthesis ◽  
Salivary Glands ◽  
Secretory Protein ◽  
Vesicular Secretion

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

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 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

scholarly journals The selective recruitment of mRNA to the ER and an increase in initiation are important for glucose-stimulated proinsulin synthesis in pancreatic β-cells

2005 ◽  
Vol 391 (2) ◽  
pp. 291-300 ◽  
Author(s):  
Isabel C. Greenman ◽  
Edith Gomez ◽  
Claire E. J. Moore ◽  
Terence P. Herbert
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Synthesis ◽  
Regulatory Mechanism ◽  
De Novo ◽  
Secretory Protein ◽  
Secretory Proteins ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Large Pool ◽  
Proinsulin Synthesis

Glucose acutely stimulates proinsulin synthesis in pancreatic β-cells through a poorly understood post-transcriptional mechanism. In the present study, we demonstrate in pancreatic β-cells that glucose stimulates the recruitment of ribosome-associated proinsulin mRNA, located in the cytoplasm, to the ER (endoplasmic reticulum), the site of proinsulin synthesis, and that this plays an important role in glucose-stimulated proinsulin synthesis. Interestingly, glucose has greater stimulatory effect on the recruitment of proinsulin mRNA to the ER compared with other mRNAs encoding secretory proteins. This, as far as we are aware, is the first example whereby mRNAs encoding secretory proteins are selectively recruited to the ER and provides a novel regulatory mechanism for secretory protein synthesis. Contrary to previous reports, and importantly in understanding the mechanism by which glucose stimulates proinsulin synthesis, we demonstrate that there is no large pool of ‘free’ proinsulin mRNA in the cytoplasm and that glucose does not increase the rate of de novo initiation on the proinsulin mRNA. However, we show that glucose does stimulate the rate of ribosome recruitment on to ribosome-associated proinsulin mRNA. In conclusion, our results provide evidence that the selective recruitment of proinsulin mRNA to the ER, together with increases in the rate of initiation are important mediators of glucose-stimulated proinsulin synthesis in pancreatic β-cells.

scholarly journals Regulation of lipoprotein lipase synthesis in 3T3-L1 adipocytes by cachectin Further proof for identity with tumour necrosis factor

1986 ◽  
Vol 240 (2) ◽  
pp. 601-604 ◽  
Author(s):  
S R Price ◽  
T Olivecrona ◽  
P H Pekala
Keyword(s):  
Protein Synthesis ◽  
Conditioned Medium ◽  
Tumour Necrosis Factor ◽  
Lipoprotein Lipase ◽  
Tumour Necrosis ◽  
Secretory Protein ◽  
Necrosis Factor ◽  
Precipitable Protein

We investigated the mechanism by which the endotoxin-induced macrophage secretory protein cachectin is able to suppress the activity of lipoprotein lipase in 3T3-L1 adipocytes. The loss in activity results from an effect on the synthesis of the enzyme, as determined by a decreased incorporation of [35S]methionine into immunoprecipitable lipoprotein lipase. The results were nearly identical whether crude conditioned medium or a highly purified preparation was utilized as a source of cachectin. [35S]Methionine incorporation into acid-precipitable protein was minimally affected by purified cachectin, suggesting that the suppression of the lipoprotein lipase was not due to a general suppression of protein synthesis. These results, taken together with our previous work, provide additional evidence that cachectin and tumour necrosis factor are functionally identical.

scholarly journals Transcriptomic Analysis of Salivary Glands of Ornithodoros brasiliensis Aragão, 1923, the Agent of a Neotropical Tick-Toxicosis Syndrome in Humans

2021 ◽  
Vol 12 ◽  
Author(s):  
Jose Reck ◽  
Anelise Webster ◽  
Bruno Dall’Agnol ◽  
Ronel Pienaar ◽  
Minique H. de Castro ◽  
...  
Keyword(s):  
Salivary Glands ◽  
Secretory Protein ◽  
Clinical Findings ◽  
Host Responses ◽  
Secretory Proteins ◽  
Major Protein ◽  
Host Interaction ◽  
Salivary Gland Protein ◽  
Duplication Events ◽  
Tick Salivary Glands

Tick salivary glands produce and secrete a variety of compounds that modulate host responses and ensure a successful blood meal. Despite great progress made in the identification of ticks salivary compounds in recent years, there is still a paucity of information concerning salivary molecules of Neotropical argasid ticks. Among this group of ticks, considering the number of human cases of parasitism, including severe syndromes and hospitalization, Ornithodoros brasiliensis can be considered one of the major Neotropical argasid species with impact in public health. Here, we describe the transcriptome analysis of O. brasiliensis salivary glands (ObSG). The transcriptome yielded ~14,957 putative contigs. A total of 368 contigs were attributed to secreted proteins (SP), which represent approximately 2.5% of transcripts but ~53% expression coverage transcripts per million. Lipocalins are the major protein family among the most expressed SP, accounting for ~16% of the secretory transcripts and 51% of secretory protein abundance. The most expressed transcript is an ortholog of TSGP4 (tick salivary gland protein 4), a lipocalin first identified in Ornithodoros kalahariensis that functions as a leukotriene C4 scavenger. A total of 55 lipocalin transcripts were identified in ObSG. Other transcripts potentially involved in tick-host interaction included as: basic/acid tail secretory proteins (second most abundant expressed group), serine protease inhibitors (including Kunitz inhibitors), 5' nucleotidases (tick apyrases), phospholipase A2, 7 disulfide bond domain, cystatins, and tick antimicrobial peptides. Another abundant group of proteins in ObSG is metalloproteases. Analysis of these major protein groups suggests that several duplication events after speciation were responsible for the abundance of redundant compounds in tick salivary glands. A full mitochondrial genome could be assembled from the transcriptome data and confirmed the close genetic identity of the tick strain sampled in the current study, to a tick strain previously implicated in tick toxicoses. This study provides novel information on the molecular composition of ObSG, a Brazilian endemic tick associated with several human cases of parasitism. These results could be helpful in the understanding of clinical findings observed in bitten patients, and also, could provide more information on the evolution of Neotropical argasids.

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