scholarly journals Both male and female gametogenesis require a fully functional protein S‐ acyl transferase 21 in Arabidopsis thaliana

2019 ◽  
Vol 100 (4) ◽  
pp. 754-767 ◽  
Author(s):  
Yaxiao Li ◽  
Hong‐Ju Li ◽  
Chris Morgan ◽  
Kirsten Bomblies ◽  
Weicai Yang ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein S ◽  
Acyl Transferase ◽  
Functional Protein ◽  
Male And Female ◽  
Female Gametogenesis

scholarly journals Biosynthesis and secretion of functional protein S by a human megakaryoblastic cell line (MEG-01)

Blood ◽  
1987 ◽  
Vol 70 (1) ◽  
pp. 301-306
Author(s):  
M Ogura ◽  
N Tanabe ◽  
J Nishioka ◽  
K Suzuki ◽  
H Saito
Keyword(s):  
Cell Line ◽  
Plasma Protein ◽  
Culture Medium ◽  
De Novo ◽  
Specific Activity ◽  
Calf Serum ◽  
Protein S ◽  
Immunoblot Analysis ◽  
Functional Assay ◽  
Functional Protein

A human megakaryoblastic cell line (MEG-01) was investigated for the presence of protein S in culture medium and cell lysates using a specific enzyme-linked immunoassay (ELISA) and a functional assay. When 5 X 10(5) MEG-01 cells/mL was subcultured in RPMI 1640 medium with 10% fetal calf serum (FCS), the concentration of protein S antigen in the culture medium increased progressively with time from less than 8 ng/mL on day 0 to 105.6 +/- 6.0 ng/mL on day 13. Vitamin K2(1 microgram/mL) increased the production of functional protein S, whereas warfarin (1 microgram/mL) profoundly decreased the quantity and the specific activity of secreted protein S. By an indirect immunofluorescent technique, protein S antigen was detected in both MEG-01 cells and human bone marrow megakaryocytes. Immunoblot analysis of culture medium revealed two distinct bands (mol wt 84,000 and 78,000) that are identical to the doublets of purified plasma protein S. De novo synthesis of protein S was demonstrated by the presence of specific immunoprecipitable radioactivity in the medium after 5 hours of labeling of the cells with [35S]-methionine as a 84,000 mol wt protein. Plasma protein S levels of nine patients with severe aplastic anemia were not significantly different from those of normal controls. These results suggest that megakaryocytes produce functional protein S and contain the enzymes required for the carboxylation of selected glutamic acid residues, and that protein S synthesized by megakaryocytes does not represent a main source of plasma protein S.

Drosophila melanogaster Importin α1 and α3 Can Replace Importin α2 During Spermatogenesis but Not Oogenesis

Genetics ◽  
2002 ◽  
Vol 161 (1) ◽  
pp. 157-170 ◽  
Author(s):  
D Adam Mason ◽  
Robert J Fleming ◽  
David S Goldfarb
Keyword(s):  
Drosophila Melanogaster ◽  
Female Sterility ◽  
Degenerate Pcr ◽  
Male And Female ◽  
Importin Α ◽  
Localization Signal ◽  
Male And Female Sterility ◽  
A Site ◽  
Female Gametogenesis

Abstract Importin α’s mediate the nuclear transport of many classical nuclear localization signal (cNLS)-containing proteins. Multicellular animals contain multiple importin α genes, most of which fall into three conventional phylogenetic clades, here designated α1, α2, and α3. Using degenerate PCR we cloned Drosophila melanogaster importin α1, α2, and α3 genes, demonstrating that the complete conventional importin α gene family arose prior to the split between invertebrates and vertebrates. We have begun to analyze the genetic interactions among conventional importin α genes by studying their capacity to rescue the male and female sterility of importin α2 null flies. The sterility of α2 null males was rescued to similar extents by importin α1, α2, and α3 transgenes, suggesting that all three conventional importin α’s are capable of performing the important role of importin α2 during spermatogenesis. In contrast, sterility of α2 null females was rescued only by importin α2 transgenes, suggesting that it plays a paralog-specific role in oogenesis. Female infertility was also rescued by a mutant importin α2 transgene lacking a site that is normally phosphorylated in ovaries. These rescue experiments suggest that male and female gametogenesis have distinct requirements for importin α2.

PROTEIN C, PROTEIN S AND THE FIBRINOLYTIC SYSTEM IN PATIENTS WITH A HISTORY OF THROMBOSIS

1987 ◽  
Author(s):  
J Malm ◽  
M Laurell ◽  
I M Nilsson ◽  
B Dahlbäck
Keyword(s):  
Plasminogen Activator ◽  
Fibrinolytic Activity ◽  
Protein C ◽  
Protein S ◽  
Protein S Deficiency ◽  
Functional Protein ◽  
Protein C Deficiency ◽  
S Deficiency ◽  
Tissue Plasminogen ◽  
History Of

Consecutive patients with a history of thrombo-embolic disease (n = 241, 109 males, 132 females, mean age 46 y), referred to the Coagulation Laboratory during an 18 month period, were analysed for defects in their coagulation and fibrinolytic systems. The diagnosis of thrombosis had been verified with phlebography and that of pulmonary embolus with scintigraphy or angiography. Retinal venous thrombosis was found in 15 of the patients. In 15 cases the thrombotic episodes occurred postoperatively, in 15 during pregnancy, in 12 during the postpartum period and in 20 during use of oral contraceptives. In the remaining cases no clinical riskfactors were identified.The concentration of protein C zymogen was measured with an immunoradiometric assay. Functional protein C was determined with a clotting inhibition assay. Protein C deficiency was found in 8 cases. Two of these had a functional protein C deficiency with normal zymogen levels. The concentration of total, as well as free (not in complex with C4b-binding protein), protein S was determined with a radioimmunoassay. Two cases of protein S deficiency were detected. Three patients with antithrombin III deficiency and two with plasminogen deficiency were found.The fibrinolytic activity after venous occlusion was analysed in 216 patients. Decreased levels were found in 32 %. The concentration of tissue plasminogen activator inhibitor (PAI) was measured in 110 patients and found to be increased in 65 % of the cases. In 99 patients both the fibrinolytic activity and the PAI concentration were measured. A combination of decreased fibrinolytic activity and increased levels of PAI was found in 44 cases. The concentration of tissue plasminogen activator antigen was decreased in 22 % of 105 cases analysed.Thus, in this material of patients with thrombo-embolic disease, abnormalities were found in 47 %. Defects in the fibrinolytic system were the most common findings. Protein C or protein S deficiency was diagnosed in less than 5 % of the cases.

A simple functional protein S assay using PROTAC®

1990 ◽  
Vol 12 (2) ◽  
pp. 201-208 ◽  
Author(s):  
P. HAN ◽  
M. PRADHAM
Keyword(s):  
Protein S ◽  
Functional Protein

scholarly journals Twenty putative palmitoyl-acyl transferase genes with distinct expression patterns in Arabidopsis thaliana

2011 ◽  
Vol 10 (52) ◽  
pp. 10575-10584 ◽  
Author(s):  
Wang Qian ◽  
Sun Jianli ◽  
Bao Li ◽  
Lian Jinpan ◽  
Zhao Huixian
Keyword(s):  
Arabidopsis Thaliana ◽  
Expression Patterns ◽  
Acyl Transferase

scholarly journals CHR11, a chromatin-remodeling factor essential for nuclear proliferation during female gametogenesis in Arabidopsis thaliana

2005 ◽  
Vol 102 (47) ◽  
pp. 17231-17236 ◽  
Author(s):  
W. Huanca-Mamani ◽  
M. Garcia-Aguilar ◽  
G. Leon-Martinez ◽  
U. Grossniklaus ◽  
J.-P. Vielle-Calzada
Keyword(s):  
Arabidopsis Thaliana ◽  
Chromatin Remodeling ◽  
Nuclear Proliferation ◽  
Female Gametogenesis

scholarly journals Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification

2018 ◽  
Vol 19 (8) ◽  
pp. 2292 ◽  
Author(s):  
Stanislav Bondarev ◽  
Kirill Antonets ◽  
Andrey Kajava ◽  
Anton Nizhnikov ◽  
Galina Zhouravleva
Keyword(s):  
Binding Site ◽  
Molecular Mechanisms ◽  
Amyloid Fibrils ◽  
Specific Binding ◽  
Protein S ◽  
Functional Protein ◽  
Functional Roles ◽  
Protein Fibrils ◽  
Protein Functions ◽  
Functional Amyloids

Amyloids are unbranched protein fibrils with a characteristic spatial structure. Although the amyloids were first described as protein deposits that are associated with the diseases, today it is becoming clear that these protein fibrils play multiple biological roles that are essential for different organisms, from archaea and bacteria to humans. The appearance of amyloid, first of all, causes changes in the intracellular quantity of the corresponding soluble protein(s), and at the same time the aggregate can include other proteins due to different molecular mechanisms. The co-aggregation may have different consequences even though usually this process leads to the depletion of a functional protein that may be associated with different diseases. The protein co-aggregation that is related to functional amyloids may mediate important biological processes and change of protein functions. In this review, we survey the known examples of the amyloid-related co-aggregation of proteins, discuss their pathogenic and functional roles, and analyze methods of their studies from bacteria and yeast to mammals. Such analysis allow for us to propose the following co-aggregation classes: (i) titration: deposition of soluble proteins on the amyloids formed by their functional partners, with such interactions mediated by a specific binding site; (ii) sequestration: interaction of amyloids with certain proteins lacking a specific binding site; (iii) axial co-aggregation of different proteins within the same amyloid fibril; and, (iv) lateral co-aggregation of amyloid fibrils, each formed by different proteins.

scholarly journals Familial protein S deficiency with a variant protein S molecule in plasma and platelets

Blood ◽  
1989 ◽  
Vol 74 (1) ◽  
pp. 213-221 ◽  
Author(s):  
HP Schwarz ◽  
MJ Heeb ◽  
R Lottenberg ◽  
H Roberts ◽  
JH Griffin
Keyword(s):  
Gene Expression ◽  
Family Member ◽  
Anticoagulant Activity ◽  
Oral Anticoagulants ◽  
Protein S ◽  
The Other ◽  
Protein S Deficiency ◽  
Functional Protein ◽  
S Deficiency ◽  
Variant Protein

Abstract A protein S deficient family presenting a variant protein S molecule in plasma and platelets is described. The propositus, age 20, and two brothers suffered from venous thrombotic disease. The propositus, the only family member studied while taking oral anticoagulants, had a protein S antigen (ag) level of 17% and undetectable activity. As demonstrated by immunoblotting both the propositus and one clinically affected brother (42% ag, 7% activity) presented variant protein S molecules of 65,000 molecular weight (mol wt) while the other clinically affected brother (64% ag, 11% activity) had only protein S with normal electrophoretic mobility of 70,000 mol wt. The mother had normal protein S levels (93% ag, 100% activity) but had both normal and variant protein S molecules and based on her functional protein S data a normal anticoagulant activity of the variant molecule is suggested. One asymptomatic but protein S deficient sister (68% ag, 9% activity) as well as the asymptomatic protein S deficient father (59% ag, 10% activity) had only protein S molecules of 70,000 mol wt. The variant protein S bound to C4b-binding protein in plasma, and differed from normal protein S in carbohydrate content. Platelets of each family member contained the same immunoblotting pattern of normal and variant protein S forms as found in plasma, consistent with the hypothesis that protein S gene expression involves codominant expression of two alleles that is similar in cells that control the synthesis of both platelet and plasma forms of protein S.

scholarly journals Boule-like genes regulate male and female gametogenesis in the flatworm Macrostomum lignano

2011 ◽  
Vol 357 (1) ◽  
pp. 117-132 ◽  
Author(s):  
Georg Kuales ◽  
Katrien De Mulder ◽  
Jade Glashauser ◽  
Willi Salvenmoser ◽  
Shigeo Takashima ◽  
...  
Keyword(s):  
Male And Female ◽  
Macrostomum Lignano ◽  
Female Gametogenesis
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