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RISS 인기검색어
- 검색키워드
- 저자 : Kunapuli, Satya (검색결과 3 건)
- 무료
- 기관 내 무료
- 유료
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Expression of Enzymatically-active Phospholipase Cγ2 in E.coli
Ozdener, Fatih,Kunapuli, Satya P.,Daniel, James L. Korean Society for Biochemistry and Molecular Biol 2002 Journal of biochemistry and molecular biology Vol.35 No.5
Phospholipase C-gamma-2 ($PLC{\gamma}2$) activation is a key signaling event for many cell functions. In order to delineate the pathways that lead to $PLC{\gamma}2$ activation, we devised a quick method for obtaining sufficient $PLC{\gamma}2$. We obtained the full-length cDNA for human $PLC{\gamma}2$ and expressed it in E. coli using the expression vector pT5T. To enhance the protein expression, tandem AGG-AGG arginine codons at the amino acid positions 1204-1205 were replaced by CGG-CGG arginine codons. The protein expression was detected in a Western blot analysis by both anti-$PLC{\gamma}2$ antibodies and the antibodies that are raised against the tripeptide epitope (Glu-Glu-Phe) tag that are genetically-engineered to its carboxyl terminal. Crude lysates that were prepared from bacteria that express $PLC{\gamma}2$ were found to catalyze the hydrolysis of phosphatidylinositol 4,5 bisphosphate. Similar to previous reports on $PLC{\gamma}2$ that is isolated from mammalian tissue, the recombinant enzyme was $Ca^{2+}$ dependent with optimal activity at 1-10 uM $Ca^{2+}$.
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Expression of Enzymatically - active Phospholipase Cγ2 in E. coli
(Fatih Ozdener),(Satya P. Kunapuli),(James L. Daniel) 생화학분자생물학회 2002 BMB Reports Vol.35 No.5
Phospholipase C-gamma-2 (PLCγ2) activation is a key signaling event for many cell functions. In order to delineate the pathways that lead to PLCγ2 activation, we devised a quick method for obtaining sufficient PLCγ2. We obtained the full-length cDNA for human PLCγ2 and expressed it in E. coli using the expression vector pT5T. To enhance the protein expression, tandem AGG-AGG arginine codons at the amino acid positions 1204-1205 were replaced by CGG-CGG arginine codons. The protein expression was detected in a Western blot analysis by both anti-PLCγ2 antibodies and the antibodies that are raised against the tripeptide epitope (Glu-Glu-Phe) tag that are genetically-engineered to its carboxyl terminal. Crude lysates that were prepared from bacteria that express PLCγ2 were found to catalyze the hydrolysis of phosphatidylinositol 4,5 bisphosphate. Similar to previous reports on PLCγ2 that is isolated from mammalian tissue, the recombinant enzyme was Ca^2+ dependent with optimal activity at 1-10 uM Ca^2+.
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Role of ADP receptors on platelets in the growth of ovarian cancer
Cho, Min Soon,Noh, Kyunghee,Haemmerle, Monika,Li, Dan,Park, Hyun,Hu, Qianghua,Hisamatsu, Takeshi,Mitamura, Takashi,Mak, Sze Ling Celia,Kunapuli, Satya,Ma, Qing,Sood, Anil K.,Afshar-Kharghan, Vahid American Society of Hematology 2017 Blood Vol.130 No.10
<P>We investigated the effect of platelets on ovarian cancer and the role of adenosine diphosphate (ADP) receptors (P2Y12 and P2Y1) on platelets in the growth of primary ovarian cancer tumors. We showed that in murine models of ovarian cancer, a P2Y12 inhibitor (ticagrelor) reduced tumor growth by 60% compared with aspirin and by 75% compared with placebo. In P2Y12(-/-) mice, the growth of syngeneic ovarian cancer tumors was reduced by >85% compared with wild-type (WT) mice. In contrast, there was no difference in tumor growth between P2Y1(-/-) and WT mice. Reconstitution of hematopoiesis in irradiated P2Y12(-/-) mice by hematopoietic progenitor cells from WT mice (WT -> P2Y12(-/-)) restored tumor growth in P2Y12(-/-) mice. Finally, knockdown of ecto-apyrase (CD39) on ovarian cancer cells increased tumor growth in tumor-bearing mice. Although in the absence of platelets, ADP, the P2Y12 inhibitor, recombinant apyrase, or knockdown of CD39 did not affect cancer cell proliferation, in the presence of platelets, the P2Y12 inhibitor and recombinant apyrase reduced and knockdown of CD39 increased platelet-enhanced cancer cell proliferation. These results suggest that P2Y12 on platelets and ADP concentration at the interface between cancer cells and platelets affect the growth of primary ovarian cancer tumors in mice. If additional studies in mice and in pilot human trials confirm our results, inhibition of P2Y12 might be a new therapeutic option that can be used in adjuvant to the traditional surgery and chemotherapy in patients with ovarian cancer.</P>
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