scholarly journals cDNA Cloning and Expression of Biologically Active Platelet Activating Factor-Acetylhydrolase (PAF-AH) from Bovine Mammary Gland

2005 ◽  
Vol 28 (4) ◽  
pp. 580-583 ◽  
Author(s):  
Eunkyung Lee ◽  
Su Jeong Lee ◽  
Tae Yoon Lee ◽  
Hyeun Wook Chang
2006 ◽  
Vol 30 (3) ◽  
pp. 239-246 ◽  
Author(s):  
Daisuke Yamaji ◽  
Kazuhiro Kimura ◽  
Atsushi Watanabe ◽  
Yasuhiro Kon ◽  
Toshihiko Iwanaga ◽  
...  

2013 ◽  
Vol 45 (15) ◽  
pp. 645-652 ◽  
Author(s):  
Emmanuelle Koch ◽  
Cathy Hue-Beauvais ◽  
Laurent Galio ◽  
Gili Solomon ◽  
Arieh Gertler ◽  
...  

Leptin is known as a cytokine mostly produced by fat cells and implicated in regulation of energy metabolism and food intake but has also been shown to be involved in many physiological mechanisms such as tissue metabolism and cell differentiation and proliferation. In particular, leptin influences the development of mammary gland. Although leptin expression in mammary gland has been studied in several species, no data are available in the rabbit. Leptin transcripts in this species have been described as being encoded by only two exons rather than three as in other species. Our focus was to clone and sequence the rabbit leptin cDNA and to prepare the recombinant biologically active protein for validation of the proper sequence and then to describe leptin expression in rabbit mammary gland during different stages of pregnancy and lactation. The leptin sequence obtained was compared with those of other species, and genome alignment demonstrated that the rabbit leptin gene is also encoded by three exons. Additionally, we analyzed the expression of leptin during pregnancy and lactation. Leptin mRNA was weakly expressed throughout pregnancy, whereas mRNA levels were higher during lactation, with a significant increase between days 3 and 16. Leptin transcripts and protein were localized in luminal epithelial cells, thus indicating that leptin synthesis occurs in this compartment. Therefore, mammary synthesized leptin may constitute a major regulator of mammary gland development by acting locally as an autocrine and/or paracrine factor. Furthermore, our results support the possible physiological role of leptin in newborns through consumption of milk.


1995 ◽  
Vol 270 (52) ◽  
pp. 31345-31352 ◽  
Author(s):  
Mitsuharu Hattori ◽  
Hideki Adachi ◽  
Junken Aoki ◽  
Masafumi Tsujimoto ◽  
Hiroyuki Arai ◽  
...  

1999 ◽  
Vol 338 (2) ◽  
pp. 479-487 ◽  
Author(s):  
Colin H. MACPHEE ◽  
Kitty E. MOORES ◽  
Helen F. BOYD ◽  
Dash DHANAK ◽  
Robert J. IFE ◽  
...  

A novel and potent azetidinone inhibitor of the lipoprotein-associated phospholipase A2 (Lp-PLA2), i.e. platelet-activating factor acetylhydrolase, is described for the first time. This inhibitor, SB-222657 (Ki = 40±3 nM, kobs/[I] = 6.6×105 M-1·s-1), is inactive against paraoxonase, is a poor inhibitor of lecithin:cholesterol acyltransferase and has been used to investigate the role of Lp-PLA2 in the oxidative modification of lipoproteins. Although pretreatment with SB-222657 did not affect the kinetics of low-density lipoprotein (LDL) oxidation by Cu2+ or an azo free-radical generator as determined by assay of lipid hydroperoxides (LOOHs), conjugated dienes and thiobarbituric acid-reacting substances, in both cases it inhibited the elevation in lysophosphatidylcholine content. Moreover, the significantly increased monocyte chemoattractant activity found in a non-esterified fatty acid fraction from LDL oxidized by Cu2+ was also prevented by pretreatment with SB-222657, with an IC50 value of 5.0±0.4 nM. The less potent diastereoisomer of SB-222657, SB-223777 (Ki = 6.3±0.5 µM, kobs/[I] = 1.6×104 M-1·s-1), was found to be significantly less active in both assays. Thus, in addition to generating lysophosphatidylcholine, a known biologically active lipid, these results demonstrate that Lp-PLA2 is capable of generating oxidized non-esterified fatty acid moieties that are also bioactive. These findings are consistent with our proposal that Lp-PLA2 has a predominantly pro-inflammatory role in atherogenesis. Finally, similar studies have demonstrated that a different situation exists during the oxidation of high-density lipoprotein, with enzyme(s) other than Lp-PLA2 apparently being responsible for generating lysophosphatidylcholine.


1996 ◽  
Vol 271 (51) ◽  
pp. 33032-33038 ◽  
Author(s):  
Kenji Hattori ◽  
Hideki Adachi ◽  
Atsushi Matsuzawa ◽  
Kazuo Yamamoto ◽  
Masafumi Tsujimoto ◽  
...  

2000 ◽  
Vol 12 (12) ◽  
pp. 4318-4330 ◽  
Author(s):  
Nathalie Moragues ◽  
Philippe Ciofi ◽  
Pierrette Lafon ◽  
Marie-Francoise Odessa ◽  
Gerard Tramu ◽  
...  

1998 ◽  
Vol 80 (09) ◽  
pp. 372-375 ◽  
Author(s):  
Hidemi Yoshida ◽  
Tadaatsu Imaizumi ◽  
Koji Fujimoto ◽  
Hiroyuki Itaya ◽  
Makoto Hiramoto ◽  
...  

SummaryPlatelet-activating factor (PAF) acetylhydrolase is an enzyme that inactivates PAF. Deficiency of this enzyme is caused by a missense mutation in the gene. We previously found a higher prevalence of this mutation in patients with ischemic stroke. This fact suggests that the mutation might enhance the risk for stroke through its association with hypertension. We have addressed this hypothesis by analyzing the prevalence of the mutation in hypertension. We studied 138 patients with essential hypertension, 99 patients with brain hemorrhage, and 270 healthy controls. Genomic DNA was analyzed for the mutant allele by the polymerase-chain reaction. The prevalence of the mutation was 29.3% (27.4% heterozygotes and 1.9% homozygotes) in controls and 36.2% in hypertensives and the difference was not significant. The prevalence in patients with brain hemorrhage was significantly higher than the control: 32.6% heterozygotes and 6.1% homozygotes (p <0.05). PAF acetylhydrolase deficiency may be a genetic risk factor for vascular diseases.


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