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Journal of Biochemistry 2005 138(4):479-484; doi:10.1093/jb/mvi141
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© 2005 The Japanese Biochemical Society

Regular Paper

Interaction of N1,N12-Diacetylspermine with Polyamine Transport Systems of Polarized Porcine Renal Cell Line LLC-PK1

Toshiaki Miki1, Kyoko Hiramatsu2 and Masao Kawakita3,*

1 Department of Molecular Physiology and 2 Medical Research and Development Center, The Tokyo Metropolitan Institute of Medical Science, Bunkyo-ku, Tokyo 113-8613; and 3 Department of Applied Chemistry, Kogakuin University, Shinjuku-ku, Tokyo 163-8677

* To whom correspondence should be addressed. Tel: +81-3-3340-2731; Fax: +81-3-3340-0147; E-mail: bt13004{at}ns.kogakuin.ac.jp

LLC-PK1 cells grown on porous membrane filters were employed as a model system to explore the renal transport of polyamines. The polarity of LLC-PK1 monolayers was confirmed by the exclusive appearance of a Na+-dependent {alpha}-methylglucoside transport system on the apical surface. The uptake of free polyamines from the basolateral side of monolayers was consistent with the existence of a single class of transport system, while the existence of two kinetically distinct polyamine transport systems with higher and lower affinities on apical membranes was suggested. The results of competition studies indicated that each of these transporters was able to interact with putrescine, spermidine and spermine. LLC-PK1 cells incorporated monoacetylspermine from the apical surface of monolayers at about half the rate of spermine uptake. Monoacetylspermine inhibited spermidine uptake, indicating that free polyamine transport systems also recognized the monoacetylated derivative. In contrast, N1,N12-diacetylspermine did not inhibit spermidine uptake, nor was it incorporated into the cells, indicating the absence of transport systems that recognize N1,N12-diacetylspermine on the apical membranes of LLC-PK1 cells. These results may be relevant as to our previous observation that the content of diacetylpolyamines in urine is relatively constant, and may explain the excellence of N1,N12-diacetylspermine as a tumor marker.


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