scholarly journals Mammalian Expression Systems for Human Blood Coagulation Factors

1991 ◽  
Vol 2 (6) ◽  
pp. 546-549
Author(s):  
Tadashi MATSUSHITA ◽  
Nobuhiko EMI
Keyword(s):  
Blood Coagulation ◽  
Human Blood ◽  
Coagulation Factors ◽  
Expression Systems ◽  
Blood Coagulation Factors ◽  
Mammalian Expression ◽  
Human Blood Coagulation

High-level production of human blood coagulation factors VII and XI using a new mammalian expression vector

Gene ◽  
1994 ◽  
Vol 139 (2) ◽  
pp. 275-279 ◽  
Author(s):  
Geoffrey Kemball-Cook ◽  
Ian Garner ◽  
Yasufumi Imanaka ◽  
Takuya Nishimura ◽  
Donogh P. O'Brien ◽  
...  
Keyword(s):  
Blood Coagulation ◽  
Human Blood ◽  
Expression Vector ◽  
Coagulation Factors ◽  
Blood Coagulation Factors ◽  
Mammalian Expression ◽  
Mammalian Expression Vector ◽  
High Level ◽  
Level Production ◽  
Human Blood Coagulation

scholarly journals Purification and characterization of a heteromultimeric glycoprotein from Artocarpus heterophyllus latex with an inhibitory effect on human blood coagulation.

2011 ◽  
Vol 58 (4) ◽  
Author(s):  
Jaruwan Siritapetawee ◽  
Sompong Thammasirirak
Keyword(s):  
Blood Coagulation ◽  
Human Blood ◽  
Exchange Chromatography ◽  
Coagulation System ◽  
Thrombin Time ◽  
Blood Coagulation Factors ◽  
Artocarpus Heterophyllus ◽  
Blood Coagulation System ◽  
Peptide Mass ◽  
Human Blood Coagulation

Plant latex has many health benefits and has been used in folk medicine. In this study, the biological effect of Artocarpus heterophyllus (jackfruit) latex on human blood coagulation was investigated. By a combination of heat precipitation and ion-exchange chromatography, a heat stable heteromultimeric glycoprotein (HSGPL1) was purified from jackfruit milky latex. The apparent molecular masses of the monomeric proteins on SDS/PAGE were 33, 31 and 29 kDa. The isoelectric points (pIs) of the monomers were 6.63, 6.63 and 6.93, respectively. Glycosylation and deglycosylation tests confirmed that each subunit of HSGPL1 formed the native multimer by sugar-based interaction. Moreover, the multimer of HSGPL1 also resisted 2-mercaptoethanol action. Peptide mass fingerprint analysis indicated that HSGPL1 was a complex protein related to Hsps/chaperones. HSGPL1 has an effect on intrinsic pathways of the human blood coagulation system by significantly prolonging the activated partial thrombin time (APTT). In contrast, it has no effect on the human extrinsic blood coagulation system using the prothrombin time (PT) test. The prolonged APTT resulted from the serine protease inhibitor property of HSGPL1, since it reduced activity of human blood coagulation factors XI(a) and α-XII(a).

Natural Oestrogen in the Female Climacteric - Influence on Blood Coagulation and Fibrinolysis

1978 ◽  
Vol 40 (02) ◽  
pp. 532-541 ◽  
Author(s):  
Anders Lagrelius ◽  
Nils-Olov Lunell ◽  
Margareta Blombäck
Keyword(s):  
Blood Coagulation ◽  
Antithrombin Iii ◽  
Coagulation Factors ◽  
Control Group ◽  
Blood Coagulation Factors ◽  
Excessive Bleeding ◽  
Oestrone Sulphate ◽  
Menopausal Women ◽  
History Of ◽  
Coagulation And Fibrinolysis

SummaryThe aim of the present study was to investigate the effect on blood coagulation and fibrinolysis of a natural oestrogen preparation, piperazine oestrone sulphate, prospectively in menopausal women. Scopolamine was given to the control group.The women were investigated before and during treatment with regard to factors VIII, VII, X, V, fibrinopeptide A, antithrombin III, plasminogen, rapid antiplasmin and α1-antitrypsin. There was no significant change towards hypercoagulability or decreased fibrinolysis in any group. In the oestrogen group, however, a tendency towards an increased level of plasminogen and a decreased level of antiplasmin was demonstrated. In the scopolamine group there was an unexpected fall in factors X and V and also in plasminogen and α1,-antitrypsin. A low level of some blood coagulation factors in some of the women before treatment is somewhat astonishing; none of them had any history of excessive bleeding.

STEROIDSTRUKTUR UND LEBERTOXIZITÄT

1967 ◽  
Vol 54 (1) ◽  
pp. 73-84 ◽  
Author(s):  
H. L. Krüskemper ◽  
G. Noell
Keyword(s):  
Alkaline Phosphatase ◽  
Liver Function ◽  
Blood Coagulation ◽  
Electrophoretic Pattern ◽  
Coagulation Factors ◽  
Blood Coagulation Factors ◽  
Methyl Group ◽  
Liver Functions ◽  
Male Subjects ◽  
Androstane Derivatives

ABSTRACT In male subjects investigations have been carried out regarding the effect of C1- and C17-methylated androstane derivatives (20 mg per day, orally, two weeks) on liver functions (parameters: activities of GPT, GOT, alkaline phosphatase and cholinesterase in serum; electrophoretic pattern; blood coagulation factors V, VII, X and prothrombin; BSP-retention). In addition to the well known hepatotropic action of 17α-alkylated C-19-steroids a quasi-axial 1α-methyl configuration (in 1α-methylandrost-2-en-17β-ol) definitely increased BSP-retention and several coagulation factors. These steroid effects decreased gradually when a methyl group was introduced in C1 equatorially (1-methylandrost-1-en-17β-ol-3-one) or quasi-equatorially (1β-methylandrost-2-en-17β-ol), the latter compound completely lacking from any influence on parameters of liver function under investigation.

EXPRESSION IN ONTOGENESIS OF HUMAN BLOOD COAGULATION FACTORS

1987 ◽  
Author(s):  
H J Hassan ◽  
A Leonardi ◽  
C Chelucci ◽  
R Guerriero ◽  
P M Mannucci ◽  
...  
Keyword(s):  
Blood Coagulation ◽  
Protein C ◽  
Antithrombin Iii ◽  
Liver Homogenate ◽  
Coagulation Factor ◽  
Coagulation Factors ◽  
Factor Ix ◽  
Adult Liver ◽  
Blood Coagulation Factors ◽  
Guanidine Isothiocyanate

We have analyzed the expression of several blood coagulation factors (IX, VIII, X, fibrinogen chains) and inhibitors (antithrombin III, protein C) in human embryonic and fetal livers, obtained from legal abortions at 6-11 week post-conception. The age was established by morphologic staging and particularly crown-rump lenght measurement.Total cellular RNA was isolated from partially purified hepatocytes or total liver homogenate using the guanidine isothiocyanate method. Poly(A)+ RNA was selected by oligodT cellulose chromatography. The size and the number of the embryonic and fetal transcripts are equivalent to those observed in adult liver, as evaluated by Northern blot analysis of total or poly(A)+ RNA hybridized to human cDNA probes.The level of coagulation factor transcripts in embryonic and fetal liver was evaluated by dot hybridization of total RNA (0.5-10 ug), as compared to RNA extracted from normal adult liver biopsies. The expression of blood coagulation factors in embryos is generally reduced for all factors, but at a different degree. In 5-11 wk liver, the level of factor IX is 5-10% of that observed in adults, while fibrinogen, protein C, antithrombin III RNA level rises from 25 to 50% and factor X is expressed at a level comparable to that observed in adult liver.We conclude that during these stages of development blood coagulation factors are expressed according to three different time, curves, possibly due to the effect of different types of regulatory mechanisms.

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