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Gene Review

BP10  -  Blood pressure QTL 10

Homo sapiens

 
 
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Disease relevance of BP10

  • The recombinant BP10 has been overexpressed in Escherichia coli, its metalloenzyme nature has been confirmed, and its catalytic properties have been characterized through kinetic studies [1].
 

High impact information on BP10

  • Comparison of the size and orientation of the labelled territory in the late blastula with the fate map of the blastula stage embryo shows that the domain in which the BP10 gene is expressed corresponds to the presumptive ectoderm [2].
  • The BP10 protease is constructed with the same domains as the human bone morphogenetic protein BMP-1, a protease described as a factor involved in bone formation, and as the recently characterized product of the tolloid gene which is required for correct dorsal-ventral patterning of the Drosophila embryo [2].
  • Developing embryos treated with purified antibodies against the BP10 protein and with synthetic peptides derived from the EGF-like domain displayed perturbations in morphogenesis and were radialized to various degrees [2].
  • BP10 shows significant hydrolysis toward gelatin both in its native zinc-containing form and copper derivative [1].
  • Blastula protease 10 (BP10) is a metalloenzyme involved in sea urchin embryogenesis, which has been assigned to the astacin family of zinc-dependent endopeptidases [1].
 

Biological context of BP10

  • Sequence comparison and phylogeny analysis show that BP10 belongs to a sub-family of molecular proteins which all play a role during development [3].
  • Cell death, measured as release of prelabelled 3H-thymidine from cell layers, was increased after exposure to BP 10 micrograms/ml while DMBA 0.05-0.1 microgram/ml led to a significantly lesser cell death compared to controls in serum free media [4].
 

Associations of BP10 with chemical compounds

  • Calculation of pseudoisothermal retention indexes in both second dimensions was performed on low-polarity 5% phenyl equivalent polysilphenylene/siloxane (BPX5) and 14% cyanopropylphenyl/86% dimethylpolysiloxane (BP10) columns [5].
  • The propranolol hydrochloride dose was 20 to 160 mg four times a day, titrated to reduce resting pulse by 25% or systolic BP 10 mm Hg [6].
  • After derivatization with trifluoroacetic anhydride, the drugs were separated on a 25-m capillary column BP 10 and detected by selected ion monitoring [7].
  • In BP responders (decrease in systolic BP 10 mmHg or greater), enalapril and nifedipine-GITS caused clear decreases in LV mass by 12 to 16 g/m2, whereas felodipine-ER was less effective (decrease by only 6 g/m2, P<0.01 versus enalapril) [8].
 

Analytical, diagnostic and therapeutic context of BP10

  • By in situ hybridization with digoxygenin-labelled RNA probes, the BP10 transcripts were only detected in a limited area of the blastula, showing that the transcription of the BP10 gene is also spatially controlled [2].
  • From exercise tests, a group (ER) of healthy young males who were normotensive at rest (BP less than or equal to 140/90) but showed an exaggerated BP response to exercise (systolic BP greater than or equal to 200 mm Hg and/or diastolic BP 10 mm Hg to greater than 90 mm Hg) were selected [9].
  • The fall in systolic BP 10 min after induction of anesthesia was 22 +/- 18 in the ICU-group versus 41 +/- 17 mm Hg in the control group (p = 0.004) [10].

References

  1. Overexpression and mechanistic characterization of blastula protease 10, a metalloprotease involved in sea urchin embryogenesis and development. da Silva, G.F., Reuille, R.L., Ming, L.J., Livingston, B.T. J. Biol. Chem. (2006) [Pubmed]
  2. Spatial and temporal expression pattern during sea urchin embryogenesis of a gene coding for a protease homologous to the human protein BMP-1 and to the product of the Drosophila dorsal-ventral patterning gene tolloid. Lepage, T., Ghiglione, C., Gache, C. Development (1992) [Pubmed]
  3. Structure of the gene encoding the sea urchin blastula protease 10 (BP10), a member of the astacin family of Zn2+-metalloproteases. Lhomond, G., Ghiglione, C., Lepage, T., Gache, C. Eur. J. Biochem. (1996) [Pubmed]
  4. Effects of polycyclic aromatic hydrocarbons on proliferation, collagen secretion and viability of arterial smooth muscle cells in culture. Stavenow, L., Pessah-Rasmussen, H. Artery (1988) [Pubmed]
  5. Generating Multiple Independent Retention Index Data in Dual-secondary Column Comprehensive Two-dimensional Gas Chromatography. Bieri, S., Marriott, P.J. Anal. Chem. (2006) [Pubmed]
  6. Propranolol in the treatment of cirrhotic ascites. Rector, W.G., Reynolds, T.B. Arch. Intern. Med. (1984) [Pubmed]
  7. Identification by GC/MS of 6-monoacetylmorphine as an indicator of heroin abuse. Kintz, P., Mangin, P., Lugnier, A.A., Chaumont, A.J. Eur. J. Clin. Pharmacol. (1989) [Pubmed]
  8. Differential effects of once-daily antihypertensive drugs on blood pressure, left ventricular mass and sympathetic activity: Nifedipine-GITS versus felodipine-ER versus enalapril. Leenen, F.H., Myers, M.G., Joyner, C.D., Toal, C.B. The Canadian journal of cardiology. (2002) [Pubmed]
  9. Follow-up of normotensive men with exaggerated blood pressure response to exercise. Dlin, R.A., Hanne, N., Silverberg, D.S., Bar-Or, O. Am. Heart J. (1983) [Pubmed]
  10. Prevention of hypotension after induction of anesthesia after preoperative tune-up. A preliminary report of the Groningen Tune-up Study. Girbes, A.R., Ligtenberg, J.J., Sonneveld, J.P., Wierda, J.M. The Netherlands journal of medicine. (1999) [Pubmed]
 
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