http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : 김형로 ( Jung Soo Kim (검색결과 2 건)
- 무료
- 기관 내 무료
- 유료
-
백일해 독소에 의한 중성 백혈구 chemotaxis 의 억제에 관한 연구
김정수,김우현,노혜원,김종석,박진우,김형로 ( Jung Soo Kim,Uh Hyun Kim,Hye Won Rho,Jong Suk Kim,Jin Woo Park,Hyung Rho Kim ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.2
It has been suggested that pertussis toxin (PT) inhibits the chemotaxis of neutrophil by modifying signal transduction system coupled to phospholipase C. The PT substrate, probably the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase (Gi) or an analogous protein, is hence proposed to mediate N-formyl-methionyl-leucyl-phenylalanine (fMLP) receptor-linked activation of the phospholipase C. The aim of this investigation was to determine whether the role played by PT in this system, is dependent upon the ability of the A-protomer of the toxin to ADP-ribosylate Gi or secondary to the binding of the B-oligomer of the toxin to the surface of target cells. PT and methylated PT (mPT) were employed in parallel to assess the involvement of two distinct biologic activities of the toxin in the inhibition of chemotaxis and its related events. Our preparation of mPT retained its ability to ADP-ribosylate Gi, but the pretreatment of mPT to neutrophils did show the inhibition of the chemotaxis as well as the other events related to the phospholipase C, indicating that the involvement of PT is not solely dependent on its capacity to ADP-ribosylate Gi, but rather related to the role of B-oligomer of the toxin.
-
The Inhibition of Neutrophil Chemotaxis by Pertussis Toxin
김정수,김우현,노혜원,김종석,박진우,김형로,Kim, Jung-Soo,Kim, Uh-Hyun,Rho, Hye-Won,Kim, Jong-Suk,Park, Jin-Woo,Kim, Hyung-Rho 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.2
백일해 독소(PT)는 phospholipase C와 연결된 신호전달 체계를 변형시켜 중성 백혈구의 chemotaxis를 억제한다고 알려져 왔다. fMLP 수용체에 연결되어 phospholipase C가 활성화 되는데는 adenylate cyclase 체계를 억제하는 guanine nucleotide의 결합 조절 단백질(Gi 단백질) 또는 상동성 단백질이 신호전달을 중계할 것이라고 생각되고 있다. 본 연구에서는 이 체계에 대한 PT의 역할이 A-protomer의 ADP-ribosyltransferase 작용에 의한 Gi 단백질의 변형 때문인지 또는 B-oligomer의 세포 표면 결합에 의한 이차적인 효과인지를 구명하였다. PT와 메틸화 PT(mPT)는 chemotaxis 억제 및 관련된 현상들에 서로 다른 생물학적 활성을 가진 독소의 두 부분중 어느 부분이 관여하는지를 알기 위하여 이용하였다. 조제한 mPT는 ADP-ribosyltransferase 활성을 유지하고 있음을 확인하였고 이 mPT는 chemotaxis 억제능력이 없음을 관찰함과 동시에 그에 수반되는 생화학적 사건들에서도 일관성 있는 결과를 얻었기에 PT에 의한 chemotaxis의 억제는 A-protomer보다는 B-oligomer의 역할과 관계되리라 사료된다. It has been suggested that pertussis toxin (PT) inhibits the chemotaxis of neutrophil by modifying signal transduction system coupled to phospholipase C. The PT substrate, probably the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase (Gi) or an analogous protein, is hence proposed to mediate N-formyl-methionyl-leucyl-phenylalanine (fMLP) receptor-linked activation of the phospholipase C. The aim of this investigation was to determine whether the role played by PT in this system, is dependent upon the ability of the A-protomer of the toxin to ADP-ribosylate Gi or secondary to the binding of the B-oligomer of the toxin to the surface of target cells. PT and methylated PT (mPT) were employed in parallel to assess the involvement of two distinct biologic activities of the toxin in the inhibition of chemotaxis and its related events. Our preparation of mPT retained its ability to ADP-ribosylate Gi, but the pretreatment of mPT to neutrophils did show the inhibition of the chemotaxis as well as the other events related to the phospholipase C, indicating that the involvement of PT is not solely dependent on its capacity to ADP-ribosylate Gi, but rather related to the role of B-oligomer of the toxin.
연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
