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Volume 132 (2002)
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Volume 132, Issue 3
Displaying 1-18 of 18 articles from this issue
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Takashi Muramatsu2002 Volume 132 Issue 3 Pages 359-371
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSMidkine (MK) and pleiotrophin (PTN) are low molecular weight proteins with closely related structures. They are mainly composed of two domains held by disulfide bridges, and there are three antiparallel β-sheets in each domain. MK and PTN promote the growth, survival, and migration of various cells, and play roles in neurogenesis and epithelial mesenchymal interactions during organogenesis. A chondroitin sulfate proteoglycan, protein-tyrosine phosphatase ζ (PTPζ), is a receptor for MK and PTN. The downstream signaling system includes ERK and PI3 kinase. MK binds to the chondroitin sulfate portion of PTPζ with high affinity. Among the various chondroitin sulfate structures, the E unit, which has 4, 6-disulfated N-acetylgalactosamine, provides the strongest binding site. The expression of MK and PTN is increased in various human tumors, making them promising as tumor markers and as targets for tumor therapy. MK and PTN expression also increases upon ischemic injury. MK enhances the migration of inflammatory cells, and is involved in neointima formation and renal injury following ischemia. MK is also interesting from the viewpoints of the treatment of neurodegenerative diseases, increasing the efficiency of in vitro development, and the prevention of HIV infection.View full abstractDownload PDF (4897K) -
Yuhong He, Jing Chen, Jianguo Ren, Guochun Wang, Guoping Cai2002 Volume 132 Issue 3 Pages 373-379
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSThe extracellular matrix (ECM) plays an important role in cell differentiation and apoptosis. Collagen is the major component of ECM. Here, an ESR signal of the hydroxyl radicals (_??_OH) generated via Fe2+-mediated Fenton reaction was found to be significantly inhibited by type I collagen. Further study showed that type I collagen also inhibited cell apoptosis induced by _??_OH, as evidenced by morphological criteria (DAPI and annexin V staining) and quantitive assays for apoptotic cells (MTT and flow-cytometric assay for subG1 cells). By addition of type I collagen in HeLa cells, the lipid peroxidation caused by _??_OH was inhibited and the cellular GSH was protected. In comparison with type I collagen, BSA and the denatured collagen, gelatin, lacked such antioxidative and antiapoptotic effects. Together, the results suggest that type I collagen can uniquely prevent _??_OH-mediated apoptosis by scavenging free radicals.View full abstractDownload PDF (1497K) -
Akiko Shiratsuchi, Tomoe Mori, Yoshinobu Nakanishi2002 Volume 132 Issue 3 Pages 381-386
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSPlasma membrane blebs are observed in many types of apoptotic cells, but their physiological roles remain to be clarified. We examined whether there is a causative connection between membrane blebbing and other apoptotic changes in Jurkat cells induced to undergo apoptosis by doxorubicin in the presence or absence of Y-27632, an inhibitor of the Rho kinase ROCK-I. The inclusion of the drug made most membrane blebs disappear, while other changes, such as chromatin condensation, inactivation of mitochondrial enzymes, externalization of the membrane phospholipid phosphatidylserine, and removal of cell surface sialic acid, remained unaffected. Furthermore, these apoptotic cells were phagocytosed by macrophages as efficiently as normally apoptosing cells. These results indicate that blebbing of the plasma membrane occurs independently from other apoptotic changes and is not involved in the recognition and engulfinent of apoptotic cells by macrophages.View full abstractDownload PDF (2822K) -
Michiko Sekine, Yoshiaki Kikkawa, Sumiyo Takahama, Kaoru Tsuda, Hiromi ...2002 Volume 132 Issue 3 Pages 387-393
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSIn our previous study, we identified a mouse gene, Gsl 5, that controls the expression of a glycolipid, GL-Y [Gal β1-4 (Fucα1-3) GlcNAcβ1-6 (Galβ1-3) GalNAcβ1-3 Galα1-4 Galβ1-4 Glcβ1-Cer], and the core 2 structure of O-linked glycans of glycoproteins, GlcNAcβ1-6 (Galβ1-3) GalNAcα-Ser/Thr, in a kidney tubular cell-specific manner through the regulation of UDP-GlcNAc β-1, 6-GlcNAc transferase (GNT). Regulation by the Gsl 5 gene occurs at the level of GNT mRNA and the recessive allele of Gsl 5 is rare and carried by DBA/2 and its related strains. Here, we report a sequence comparison of the 5'flanking region of the GNT gene among 5 laboratory strains and 10 wild-derived strains, demonstrating that the DBA/2 allele sequence is similar to the sequence carried by Asian Mus m. musculus and differs substantially from the East European M. m. musculus. These results suggest that the DBA/2 allele of Gsl 5 was introduced into laboratory mouse strains by Asian wild-derived mice. Phylogenetic comparison of the 5'flanking region sequences between the recessive and dominant Gsl 5 alleles indicates that mutations to create a functional Gsl 5 gene occurred approximately one million years ago during the subspeciation of M. musculus, and provides a case for studies on the creation of functional genes involved in tissue-specific transcriptional regulation.View full abstractDownload PDF (1874K) -
Atsuhiro Miyazaki, Tadashi Koieyama, Yukio Shimada, Takashi Kikuchi, H ...2002 Volume 132 Issue 3 Pages 395-400
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSIn experimental animals and humans, the concentration of serum mevalonate (MVA), a direct product of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, is considered to reflect the activity of whole-body sterol synthesis. The relationship between the concentration of serum MVA and the activity of sterol synthesis in tissues, however, has not been fully clarified. In the present study, we examined MVA metabolism by using pravastatin, a liver-selective inhibitor of HMG-CoA reductase, and common marmosets, a good model animal for studying lipid metabolism. In the time course study, the maximal reduction in the concentration of serum MVA was observed 2h after a single oral administration of 30mg/kg pravastatin to common marmosets. We, therefore, examined the relationship between the concentrations of serum and hepatic MVA, and sterol synthesis in some tissues at this time point. Sterol synthesis was determined ex vivo in tissue slices by measuring the incorporation of [14C] acetate into digitonin-precipitable [14C] sterols. Pravastatin at 0.03-30mg/kg reduced dose-dependently the activity of hepatic sterol synthesis, whereas no significant reduction of sterol synthesis was observed in other tissues such as intestine, kidney, testis and spleen, even with the highest dose (30mg/kg). The liver-specific inhibition of sterol synthesis caused parallel reductions in the concentrations of both serum and liver MVA. In addition, there were good correlations between the concentration of either serum or hepatic MVA and the activity of hepatic sterol synthesis. These data indicate that the major origin of serum MVA is the liver, and that the concentration of serum MVA reflects the concentration of hepatic MVA and the activity of hepatic sterol synthesis 2h after a single oral administration of pravastatin in common marmosets.View full abstractDownload PDF (712K) -
Tomohisa Horibe, Chieko Yosho, Satoshi Okada, Masami Tsukamoto, Hiroak ...2002 Volume 132 Issue 3 Pages 401-407
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSTo elucidate the function of protein disulfide isomerase (PDI), we screened for PDI-binding proteins in a bovine liver extract using affinity column chromatography. One of the binding proteins was identified by SDS-PAGE and N-terminal amino acid sequence analysis to be cyclophilin B (Cyp B). Use of the BIACORE system revealed that purified bovine Cyp B bound specifically to bovine PDI with a KD value of 1.19×10-5M. Interestingly, the binding affinity between PDI and Cyp B was strengthened by preincubation of the Cyp B with cyclosporin A (CsA), yielding a KD value of 3.67×10-6M. Although the interaction between PDI and Cyp B affected neither the isomerase activity of PDI nor the peptidyl-prolyl cis-trans isomerase activity of Cyp B, Cyp B increased the chaperone activity of PDI. However, the complex of Cyp B and CsA completely inhibited the chaperone activity of PDI. Thus, PDI and Cyp B appear to cooperate with each other to regulate the functional expression of proteins in vivo.View full abstractDownload PDF (1775K) -
Ayako Sakaguchi, Mitsuko Miyaike, Kazufumi Kuroda, Naohito Nozaki, Mas ...2002 Volume 132 Issue 3 Pages 409-416
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSThe epitopes of about 100 monoclonal antibodies against human type II DNA topoisomerase were mapped along the enzyme molecules. Although they were randomly and independently established, epitope sites were unevenly distributed the toward N-terminal or C-terminal region. We suggest that the central catalytic domain is hidden inside the molecule and inaccessible to the antigen recognition sites. Using antibodies, we demonstrate the distinct localization of isoforms of Topo II in cultured cells. Some particularly useful antibodies are listed.View full abstractDownload PDF (4342K) -
Shinichiro Hori, Makoto Yamada, Sachiko Ohtani, Chiyo Hori, Tadahiro Y ...2002 Volume 132 Issue 3 Pages 417-425
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSA novel chymotrypsin-like proteinase termed myonase was previously purified from MDX-mouse skeletal muscle [Hori et al. (1998) J. Biochem. 123, 650-658]. Western blots and immunohistochemical analyses showed that myonase was present within myocytes of both MDX-mouse and control mouse, and subcellular fractionation showed that it was associated with myofibrils. No significant difference was observed on Western blots between the amounts of myonase in myofibrils of MDX-mouse and control mouse, but the amount of myonase recoverable as a pure protein was 5-10-fold more when MDX-mouse was the source of the skeletal muscle. Myofibrils also possessed an endogenous inhibitor of myonase, whose inhibitory activity at physiological pH (pH 7.4) depended on salt concentration, stronger inhibition being observed at a low salt concentration. Inhibition at alkaline pH (pH 9) was weak and independent of salt concentration. Myonase in myofibrils was partially released at neutral pH by a high salt concentration (>0.6M NaCl). However, even at 4M NaCl, more than 80% of myonase remained within the myofibrils. Under alkaline conditions, release of myonase from myofibril was more extensive. At pH 12, myonase was almost completely present in the soluble fraction. Release of myonase under these conditions coincided with the solubilization of other myofibrillar proteins.View full abstractDownload PDF (6386K) -
Hideto Hoshino, Kazuhiko Igarashi2002 Volume 132 Issue 3 Pages 427-431
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSBach 2 is an oxidative stress-regulated transcription factor and functions as a repressor of gene expression directed by the TPA-response element, the Maf recognition element, and the antioxidant responsive element. To investigate the possibility that these enhancers are regulated in a tissue-specific manner, we analyzed expression of Bach 2 during differentiation of neural cells. Bach 2 was induced upon neuronal differentiation of P 19 embryonic carcinoma cells, while its related factor Bachl did not show significant change. By using affinity-purified anti-Bach 2 antibodies, expression of Bach 2 in mouse embryos was determined. High levels of Bach 2 antigen were found in differentiating neuronal and lens cells in day 12.5 embryos. Consistent with the fact that subcellular localization of Bach 2 is regulated by nuclear export in cultured cells, extensive Bach 2-staining was found in the cytoplasmic regions of developing neuronal and lens cells. These results suggest that Bach 2 regulates AP-1- and Maf-dependent gene expression during development of neuronal and lens cells and that its activity may be regulated by nuclear export in these cells.View full abstractDownload PDF (3741K) -
María Teresa Olmo, Francisca Sánchez-Jiménez, Mig ...2002 Volume 132 Issue 3 Pages 433-439
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSMammalian histidine decarboxylases have not been characterized well owing to their low amounts in tissues and instability. We describe here the first spectroscopic characterization of a mammalian histidine decarboxylase, i.e. a recombinant version of the rat enzyme purified from transformed Escherichia coli cultures, with similar kinetic constants to those reported for mammalian histidine decarboxylases purified from native sources. We analyzed the absorption, fluorescence and circular dichroism spectra of the enzyme and its complexes with the substrate and substrate analogues. The pyridoxal-5'-phosphate-enzyme internal Schiff base is mainly in an enolimine tautomeric form, suggesting an apolar environment around the coenzyme. Michaelis complex formation leads to a polarized, ketoenamine form of the Schiff base. After transaldimination, the coenzyme-substrate Schiff base exists mainly as an unprotonated aldimine, like that observed for dopa decarboxylase. However, the coenzyme-substrate Schiff base suffers greater torsion than that observed in other L-amino acid decarboxylases, which may explain the relatively low catalytic efficiency of this enzyme. The active center is more resistant to the formation of substituted aldamines than the prokaryotic homologous enzyme and other L-amino acid decarboxylases. Characterization of the similarities and differences of mammalian histidine decarboxylase with respect to other homol-ogous enzymes would open new perspectives for the development of new and more specific inhibitors with pharmacological potential.View full abstractDownload PDF (1846K) -
Tadashi Tamura, Tatsuya Oda, Tsuyoshi Muramatsu2002 Volume 132 Issue 3 Pages 441-449
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSWe have found that a brefeldin A (BFA)-resistant mutant cell line derived from Vero cells (BER-40) is highly resistant to ricin-induced apoptosis as compared with parental Vero cells. In BER-40 cells, all apoptotic events caused by ricin including cytolysis, nuclear morphological changes, and DNA fragmentation occur to a lesser extent than in Vero cells, even though both cell lines show similar sensitivities to ricin-mediated inhibition of protein synthesis. Furthermore, no significant apoptotic signaling events, such as increases in caspase-3 and -9-like activities, release of cytochrome c from mitochondria, or the cleavage of PARP, were observed in BER-40 cells under the conditions at which these changes were evident in Vero cells. Intracellular biochemical changes associated with ricin-induced apoptosis, such as the depletion of glutathione and an increase in free Zn2+, were also less apparent in BER-40 cells than in Vero cells. BER-40 cells were also found to be highly resistant to apoptosis induced by other toxins with different intoxication mechanisms such as diphtheria toxin, modeccin, and anisomycin. These results suggest that the entire apoptotic signal transduction mechanism in BER-40 cells, which may be triggered after the inhibition of protein synthesis by toxins, becomes resistant. Since MDCK cells, a naturally BFA resistant cell line, are highly sensitive to ricin-induced apoptosis, it seems likely that the BFA resistance phenotype may not necessarily lead to resistance to apoptotic cell death. Probably the underlaying BFA-resistance mechanism in BER-40 cells is distinct from that in MDCK cells, and the resistance to ricin-induced apoptosis of BER-40 cells maybe a unique phenotype acquired concomitantly with BFA-resistance.View full abstractDownload PDF (3653K) -
Masakazu Kikuchi, Eisuke Doi, Ikuo Tsujimoto, Tomohisa Horibe, Yoshiyu ...2002 Volume 132 Issue 3 Pages 451-455
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSHuman P5 (hP5) was expressed in the Escherichia coli pET system and purifie by sequential Ni2+-chelating resin column chromatography. Characterization of purified hP5 indicated that it has both isomerase and chaperone activities, but both activities are lower than those of human protein disulfide isomerase (PDI). Moreover, hP5 was observed to have peptide-binding ability, and its chaperone activity was confirmed with rhodanese and citrate synthase as substrates, but not with D-glyceraldehyde-3-phosphate dehydrogenase, showing that hP5 has substrate specificity with respect to chaperone activity. Mutation of two thioredoxin-related motifs in hP 5 revealed that the first motif is more important than the second for isomerase activity and that the first cysteine in each motif is necessary for isomerase activity. Since thioredoxin motif mutants lacking isomerase activity retain chaperone activity with the substrate citrate synthase, the isomerase and chaperone activities of hP5 are probably independent, as was shown for PDI.View full abstractDownload PDF (1450K) -
Faye Xu, Masahito Suiko, Yoichi Sakakibara, T. Govind Pai, Ming-Cheh L ...2002 Volume 132 Issue 3 Pages 457-462
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSCytosolic sulfotransferases (STs), traditionally viewed as Phase II drug-metabolizing or detoxifying enzymes, are increasingly being implicated in the metabolism of endogenous biologically-active molecules. Except for studies on changes in their levels of expression and activity in the early stage of development in mammals, very little is known about how these enzymes are regulated. In this study, the regulatory effects of divalent metal cations on the activity of human cytosolic STs were quantitatively evaluated. Results obtained indicate that all nine human cytosolic STs examined are partially or completely inhibited/stimulated by the ten divalent metal cations tested at 10mM concentration. Compared with the other metal cations, the inhibitory or stimulatory effect of Mg2+ and Ca2+ on the activities of the human cytosolic STs appeared to be relatively smaller. Concentration-dependent effects of the divalent metal cations were further examined. The IC50 or EC50 values determined for different divalent metal cations were mostly above their normal physiological concentration ranges. In a few cases, however, IC50 values close to the physiological concentrations of certain divalent metal cations were observed. Using the monoamine (M)-form phenol ST (PST) as a model, it was demonstrated that the Km for dopamine changed only slightly with increasing concentrations of Cd2+, whereas the Vmax was dramatically decreased.View full abstractDownload PDF (745K) -
Koji Nakamura, Kan Tanoue, Takeshi Satoh, Mutsuhiro Takekawa, Masahiko ...2002 Volume 132 Issue 3 Pages 463-470
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSWe have identified a novel dual-specificity phosphatase (DSP), called LDP-2 (low-molecular-mass DSP-2), composed of 220 amino acid residues showing high sequence homology to VHR and LDP-1/TAMP, which belong to a family of DSPs with low molecular masses. The LDP-2 gene is ubiquitously expressed, and LDP-2 is localized in the cytoplasm. The main structural feature of LDP-2 is that the serine-156 residue located in the common active site sequence motif, HCXXGXXRS, for DSP is naturally substituted with an alanine residue. The recombinant LDP-2 protein showed extremely low phosphatase activity towards p-nitrophenyl phosphate (pNPP). Back-mutation of Ala-156 in LDP-2 to a serine (A 156 S mutation) conferred significant phosphatase activity towards pNPP. However, both LDP-2 and LDP-2 (A 156 S) exhibited substantial phosphatase activities towards both phospho-seryl/threonyl and -tyrosyl residues of myelin basic protein, with similar specific activities. Ala-156 of LDP-2 might be crucially involved in the recognition of a physiological substrate. We analyzed the effect of VHR and LDP-2 on mitogenactivated protein kinases (MAPKs) in vivo. We first found that VHR inhibits the activation of p 38 as well as ERK and JNK, with similar efficiency. Under the conditions ussed, LDP-2 specifically suppressed JNK activation.View full abstractDownload PDF (3894K) -
Yoshiaki Mizukura, Shinsaku Maruta2002 Volume 132 Issue 3 Pages 471-482
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSIn order to elucidate the molecular basis of energy transduction by myosin as a molecular motor, a fluorescent ribose-modified ATP analog 2'(3')-O-[6-(N-(7-nitrobenz-2-oxa-1, 3-diazol-4-yl) amino) hexanoyl]-ATP (NBD-ATP), was utilized to study the conformational change of the myosin motor domain during ATP hydrolysis using the fluorescence resonance energy transfer (FRET) method. The FRET efficiency from the fluorescent probe, BD- or AD-labeled at the reactive cysteine residues, SH 1 (Cys 707) or SH 2 (Cys 697), respectively, to the NBD fluorophore in the ATP binding site was measured for several transient intermediates in the ATPase cycle. The FRET efficiency was greater than that using NBD-ADP. The FRETs for the myosin•ADP•AlF4- and myosin•ADP•BeFn ternary complexes, which mimic the M*•ADP•Pi state and M*•ATP state in the ATPase cycle, respectively, were similar to that of NBD-ATP. This suggests that both the SH 1 and SH 2 regions change their localized conformations to move closer to the ATPase site in the M*•ATP state and M**ADP•Pi state than in the M*•ADP state. Furthermore, we measured energy transfer from BD in the essential light chain to NBD in the active site. Assuming the efficiency at different states, myosin adopts a conformation such that the light chain moves closer to the active site by approximately 9 Å during the hydrolysis of ATP.View full abstractDownload PDF (2885K) -
Norihiro Nakamura, Yoshihide Miyake, Masafumi Matsushita, Shingo Tanak ...2002 Volume 132 Issue 3 Pages 483-491
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSKinesin family proteins are microtubule-dependent molecular motors involved in the intracellular motile process. Using a Ca2+-binding protein, CHP (calcineurin B homologous protein), as a bait for yeast two hybrid screening, we identified a novel kinesinrelated protein, KIF1Bβ2. KIHF1Bβ2 is a member of the KIF 1 subfamily of kinesin-related proteins, and consists of an amino terminal KIF 1 B-type motor domain followed by a tail region highly similar to that of KIF1A. CHP binds to regions adjacent to the motor domains of KIF1Bβ2 and KIF1B, but not to those of the other KIF 1 family members, KIF1A and KIF1C. Immunostaining of neuronal cells showed that a significant portion of KIF1Bβ2 is co-localized with synaptophysin, a marker protein for synaptic vesicles, but not with a mitochondria-staining dye. Subcellular fractionation analysis indicated the co-localization of KIF1Bβ2 with synaptophysin. These results suggest that KIF1Bβ2, a novel CHP-interacting molecular motor, mediates the transport of synaptic vesicles in neuronal cells.View full abstractDownload PDF (5058K) -
Jian Liu, Takayuki Tsukuba, Kuniaki Okamoto, Masamichi Ohishi, Kenji Y ...2002 Volume 132 Issue 3 Pages 493-499
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSCathepsin E, an intracellular aspartic proteinase of the pepsin family, is composed of two homologous domains, each containing the catalytic Asp residue in a consensus DTG motif. Here we examine the significance of residues in the motifs of rat cathepsin E by substitution of Asp 98, Asp 283, and Thr 284 with other residues using site-directed mutagenesis. Each of the mutant proenzymes, as well as the wild-type protein, was found in culture media and cell extracts when heterologously expressed in human embryonic kidney 293T cells. The single mutants D98A, D283A, and D283E, and the double mutants D98A/D283 A and D 98E/D283E showed neither autocatalytic processing nor enzymatic activities under acidic conditions. However, the D98E and T284S mutants retained the ability to transform into the mature forms, although they exhibited only about 13 and 40% of the activity of the wild-type enzyme, respectively. The Km values of these two mutants were similar to those of the wild-type enzyme, but their kcat values were greatly decreased. The Ki values for pepstatin and the Ascaris pepsin inhibitor of the mutants and the wild-type enzyme were almost the same. The circular dichroism spectra of the two mutants were essentially the same as those of the wild-type enzyme at various pH values. These results indicate that (i) Asp 98, Asp 283, and Thr 284 are indeed critical for catalysis, and (ii) the decrease in the catalytic activity of D98E and T284S mutants is brought about by an effect on the kinetic process from the enzyme-substrate complex to the release of the product.View full abstractDownload PDF (2959K) -
Masahiko Sugiki, Sayuri Omura, Etsuo Yoshida, Hiroshi Itoh, Hiroaki Ka ...2002 Volume 132 Issue 3 Pages 501-508
Published: 2002
Released on J-STAGE: November 14, 2008
JOURNAL FREE ACCESSUrokinase-type and tissue-type plasminogen activators (uPA, tPA) are key enzymes for starting the plasminogen system, which plays important roles in various physiological and pathological conditions. In order to examine the gene regulation in rabbit pathophysiological models we attempted to clone full-length cDNAs encoding uPA and tPA from kidney extracts of rabbit (Oryctolagus cuniculus) by reverse transcription-polymerase chain reaction and rapid amplification of cDNA ends. The cloned rabbit uPA and tPA eDNAs were 2, 350 and 2, 561 by in length, respectively, and the basic molecular structures predicted from the cDNAs were well-conserved compared with human uPA and tPA. In a rabbit model of renal ischemia/reperfusion (1/R), the expression of uPA and tPA mRNAs was down-regulated and that of their physiological inhibitor, type 1 plasminogen activator inhibitor, mRNA was up-regulated in ischemic kidney compared to nonischemic kidney. In addition, fibrinolytic activity in ischemic kidney was lower than that in non-ischemic kidney. It is suggested that repression of fibrinolysis in the kidneys in rabbit I/R may contribute to the progression of renal damage in the model.View full abstractDownload PDF (1923K)
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