Effect of day of the oestrous cycle, side of the reproductive tract and heat shock on in-vitro protein secretion by bovine endometrium

Reproduction ◽  
1988 ◽  
Vol 84 (2) ◽  
pp. 567-578 ◽  
Author(s):  
J. R. Malayer ◽  
P. J. Hansen ◽  
W. C. Buhi
Keyword(s):  
Heat Shock ◽  
Protein Secretion ◽  
Reproductive Tract ◽  
Oestrous Cycle ◽  
Vitro Protein

Effects of oestradiol, the oestrous cycle and pregnancy on weight, metabolism and cytosol receptors in the uterus of the brush-tail possum (Trichosurus vulpecula)

1986 ◽  
Vol 108 (2) ◽  
pp. 201-210 ◽  
Author(s):  
J. D. Curlewis ◽  
G. M. Stone
Keyword(s):  
Protein Synthesis ◽  
Protein Content ◽  
Corpus Luteum ◽  
Metabolic Activity ◽  
Weight Ratio ◽  
Oestrous Cycle ◽  
Uterine Weight ◽  
In Vitro Protein Synthesis ◽  
Vitro Protein

ABSTRACT Uterine weight, RNA, DNA, protein content, in-vitro rate of protein synthesis, cytosol oestrogen and progesterone receptors were examined after administration of oestradiol to ovariectomized animals and on days 0, 5, 9 and 13 of the non-pregnant cycle and day 13 of pregnancy. In ovariectomized animals, oestradiol increased uterine weight, RNA: DNA and protein: DNA ratios and the concentration of cytosol receptors for oestradiol and progesterone. During the oestrous cycle there was a linear increase in uterine weight and a significant effect of the corpus luteum on the weight of the ipsilateral uterus. Changes in RNA, DNA and protein content between days 0 and 5 were not observed, but between days 5 and 13 RNA: DNA and protein: DNA ratios increased and the DNA: tissue weight ratio decreased. Thus, cellular hypertrophy and/or increased metabolic activity rather than hyperplasia occur over this period, which is coincident with the known rise in plasma progesterone levels. The rate of in-vitro protein synthesis (per unit tissue protein) during the non-pregnant cycle was greatest at day 0. These changes in uterine metabolic activity were associated with alterations in cytosol receptor concentrations for both steroids. Cytosol progesterone receptor concentrations were highest at day 0 after which they declined to a minimum at day 13. Cytosol oestradiol receptor concentrations, however, rose between days 0 and 5 and then declined. Although lutectomy on day 8 of the cycle does not interfere with the development of a histologically normal luteal phase, high peripheral progesterone levels which occur after day 8 in intact animals are associated with major increases in uterine metabolic activity. The unilateral effect of the corpus luteum on uterine weight was associated with a decrease in DNA: g tissue ratio and an increase in rate of in-vitro protein synthesis indicating hypertrophy and/or extracellular accumulation of secreted material as well as enhanced metabolic activity. There was a significant effect of pregnancy on uterine weight at day 13 and this was associated with an increase in DNA content of both uteri. There was a unilateral effect of pregnancy on RNA: DNA ratio and in-vitro rate of protein synthesis, but not on uterine weight. J. Endocr. (1986) 108, 201–210

The Interleukin 1-β Exonic (+3953) Polymorphism Does Not Alter in Vitro Protein Secretion

2002 ◽  
Vol 73 (2) ◽  
pp. 139-141 ◽  
Author(s):  
Roberto Dominici ◽  
Giulia Malferrari ◽  
Claudio Mariani ◽  
Luigi M.E. Grimaldi ◽  
Ida Biunno
Keyword(s):  
Protein Secretion ◽  
Interleukin 1 ◽  
Vitro Protein

Applicability of Instability Index for In vitro Protein Stability Prediction

2019 ◽  
Vol 26 (5) ◽  
pp. 339-347 ◽  
Author(s):  
Dilani G. Gamage ◽  
Ajith Gunaratne ◽  
Gopal R. Periyannan ◽  
Timothy G. Russell
Keyword(s):  
Protein Stability ◽  
Caulobacter Crescentus ◽  
Effect Of Temperature ◽  
Instability Index ◽  
Dipeptide Composition ◽  
Experimental Conditions ◽  
The Stability ◽  
Vitro Protein

Background: The dipeptide composition-based Instability Index (II) is one of the protein primary structure-dependent methods available for in vivo protein stability predictions. As per this method, proteins with II value below 40 are stable proteins. Intracellular protein stability principles guided the original development of the II method. However, the use of the II method for in vitro protein stability predictions raises questions about the validity of applying the II method under experimental conditions that are different from the in vivo setting. Objective: The aim of this study is to experimentally test the validity of the use of II as an in vitro protein stability predictor. Methods: A representative protein CCM (CCM - Caulobacter crescentus metalloprotein) that rapidly degrades under in vitro conditions was used to probe the dipeptide sequence-dependent degradation properties of CCM by generating CCM mutants to represent stable and unstable II values. A comparative degradation analysis was carried out under in vitro conditions using wildtype CCM, CCM mutants and two other candidate proteins: metallo-β-lactamase L1 and α -S1- casein representing stable, borderline stable/unstable, and unstable proteins as per the II predictions. The effect of temperature and a protein stabilizing agent on CCM degradation was also tested. Results: Data support the dipeptide composition-dependent protein stability/instability in wt-CCM and mutants as predicted by the II method under in vitro conditions. However, the II failed to accurately represent the stability of other tested proteins. Data indicate the influence of protein environmental factors on the autoproteolysis of proteins. Conclusion: Broader application of the II method for the prediction of protein stability under in vitro conditions is questionable as the stability of the protein may be dependent not only on the intrinsic nature of the protein but also on the conditions of the protein milieu.

In Vitro Holdase Activity of E. coli Small Heat-Shock Proteins IbpA, IbpB and IbpAB: A Biophysical Study with Some Unconventional Techniques

2014 ◽  
Vol 21 (6) ◽  
pp. 564-571 ◽  
Author(s):  
Sourav Roy ◽  
Monobesh Patra ◽  
Suman Nandy ◽  
Milon Banik ◽  
Rakhi Dasgupta ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
E Coli ◽  
Biophysical Study ◽  
Shock Proteins

scholarly journals Heat shock cognate 70 protein secretion as a new growth arrest signal for cancer cells

Oncogene ◽  
2009 ◽  
Vol 29 (1) ◽  
pp. 117-127 ◽  
Author(s):  
P Nirdé ◽  
D Derocq ◽  
M Maynadier ◽  
M Chambon ◽  
I Basile ◽  
...  
Keyword(s):  
Heat Shock ◽  
Cancer Cells ◽  
Protein Secretion ◽  
Growth Arrest ◽  
Heat Shock Cognate 70

scholarly journals Contrasting effects of heat shock during in vitro maturation on development of in vitro‐fertilized and parthenogenetic bovine embryos

2019 ◽  
Vol 54 (10) ◽  
pp. 1357-1365
Author(s):  
Luiz Sergio Almeida Camargo ◽  
Fernanda Queiros Costa ◽  
Michele Munk ◽  
Sabine Wohlres‐Viana ◽  
Raquel Varela Serapião ◽  
...  
Keyword(s):  
Heat Shock ◽  
In Vitro Maturation ◽  
Bovine Embryos
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