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Park, Jae Gahb,Ira Pastan,Shinn Liang Lai,Barnett S Kramer,Lori Goldstein,Adi Gazdar 한국유전학회 1988 Genes & Genomics Vol.10 No.4
170kDa glycoprotein (P-glycoprotein) product of mdrl gene has been found in plasma membrane of various multidrug-resist-tumor cells, and has long been considered as a transporter protein which pump out toxic drugs. Eleven human colorectal cell lines and four human gastric cell lines were established and characterized by us. In vitro chemosensitivity test was performed by MTT assay for 5-FU, doxorubicin, cisplatin and mitomycin-c. Slot blots containing l0㎍, 3㎍, 1㎍ and 0.3㎍ of total RNA were hybridized to nick-translated mdrl cDNA 5A. Comparable RNA loading was confirmed using a human gamma-actin probe. Each sample was compared with KB-8-5 RNA, which gave a reproducible and easily detectable signal, but the amount of mdrl RNA is expressed to drug-sensitive KB-3-1 for convenience. Three out of four gastric cell lines are sensitive to 5-FU while three out of eleven colorectal cell lines are sensitive to 5-FU. Three gastric lines sensitive to 5-FU are also sensitive to adriamycin, mitomycin and cisplatin. Reduced folates didn't increase the cytotoxicity of 5-FU in gastric cell lines. Interestingly in SNU-1 gastric cell line a clinically achievable level of leucovorin (20μM) increased the cytotoxicity of 5-FUdR but not of 5-FU. Leucovorin increased the cytotoxicity of 5-FUdR (2.4nM) in SNU-1 cell line from 0.01μM concentration but higher concentration up to 20μM showed more effect. The expression of the mdrl gene was low in all gastric lines while elevated levels of mdrl RNA were found in 5 colorectal lines.
Anoctamin and transmembrane channel-like proteins are evolutionarily related.
Hahn, Yoonsoo,Kim, Dong Seon,Pastan, Ira H,Lee, Byungkook D.A. Spandidos 2009 INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE Vol.24 No.1
<P>The anoctamin (ANO) family of proteins, consisting of 10 members in mammals, are transmembrane proteins that have Ca2+-activated Cl- channel activity. The transmembrane channel-like (TMC) family of proteins, consisting of 8 members in mammals, are also transmembrane proteins of which mutations are implicated in various human conditions, such as hearing loss and epidermodysplasia verruciformis. Here we show that ANO and TMC proteins share high sequence similarity and probably the same membrane topology, indicating that these proteins are evolutionarily related. We found many conserved amino acid residues between the two families of proteins, especially in regions spanning the transmembrane domains TM1, TM4-TM5, and TM6-TM7. These findings imply that these proteins form one large family, which we term ANO/TMC superfamily and that TMC proteins also function as channels for Cl- or other ions. The ANO/TMC superfamily proteins are present in almost all diverse groups of eukaryotic organisms, suggesting that the proteins function in important biological processes, such as ion homeostasis, in eukaryotic cells.</P>
Wang, S.,Shin, I.S.,Hancock, H.,Jang, B.s.,Kim, H.s.,Lee, S.M.,Zderic, V.,Frenkel, V.,Pastan, I.,Paik, C.H.,Dreher, M.R. Elsevier Science Publishers 2012 Journal of controlled release Vol.162 No.1
The success of radioimmunotherapy for solid tumors remains elusive due to poor biodistribution and insufficient tumor accumulation, in part, due to the unique tumor microenvironment resulting in heterogeneous tumor antibody distribution. Pulsed high intensity focused ultrasound (pulsed-HIFU) has previously been shown to increase the accumulation of <SUP>111</SUP>In labeled B3 antibody (recognizes Lewis<SUP>y</SUP> antigen). The objective of this study was to investigate the tumor penetration and therapeutic efficacy of pulsed-HIFU exposures combined with <SUP>90</SUP>Y labeled B3 mAb in an A431 solid tumor model. The ability of pulsed-HIFU (1MHz, spatial averaged temporal peak intensity=2685Wcm<SUP>-2</SUP>; pulse repetition frequency=1Hz; duty cycle=5%) to improve the tumor penetration and therapeutic efficacy of <SUP>90</SUP>Y labeled B3 mAb (<SUP>90</SUP>Y-B3) was evaluated in Le<SUP>y</SUP>-positive A431 tumors. Antibody penetration from the tumor surface and blood vessel surface was evaluated with fluorescently labeled B3, epi-fluorescent microscopy, and custom image analysis. Tumor size was monitored to determine treatment efficacy, indicated by survival, following various treatments with pulsed-HIFU and/or <SUP>90</SUP>Y-B3. The pulsed-HIFU exposures did not affect the vascular parameters including microvascular density, vascular size, and vascular architecture; although 1.6-fold more antibody was delivered to the solid tumors when combined with pulsed-HIFU. The distribution and penetration of the antibodies were significantly improved (p-value<0.05) when combined with pulsed-HIFU, only in the tumor periphery. Pretreatment with pulsed-HIFU significantly improved (p-value<0.05) survival over control treatments.