Details of a Researcher - Saya, Hideyuki

Papers - Saya, Hideyuki

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A human homolog of Drosophila lethal(3)malignant brain tumor (l(3)mbt) protein associates with condensed mitotic chromosomes

Koga Hisashi, Matsui Shin Ichi, Hirota Toru, Takebayashi Shin Ichiro, Okumura Katsuzumi, Saya Hideyuki

Oncogene 18 ( 26 ) 3799 - 3809 1999.07

ISSN 0950-9232

The lethal(3)malignant brain tumor (D-l(3)mbt) gene is considered to be one of the tumor suppressor genes of Drosophila, and its recessive mutations are associated with malignant transformation of the neuroblasts in the larval brain. The structure of D-l(3)mbt protein is similar to Drosophila sex comb on midleg (Scm) protein which is a member of Polycomb group (PcG) proteins. We have isolated here the first human homolog of the D-l(3)mbt gene, designated h-l(3)mbt. Radiation hybrid mapping and fluorescence in situ hybridization (FISH) analysis localized the h-l(3)mbt gene to chromosome 20q12. The h-l(3)mbt transcript is expressed in most of the human adult normal tissues and cultured cell lines. However, some cancer cells markedly reduce the h-l(3)mbt protein expression. Immunocytochemical study revealed that the h-l(3)mbt protein shows a speckled and scattered distribution in interphase nuclei and completely associates with condensed chromosomes in mitotic cells. This subcellular localization has been shown to be different from that of Bmi1 protein which is a component of PcG complex. Furthermore, overexpression of h-l(3)mbt protein by using a Cre-mediated gene activation system leads to failures of proper chromosome segregation and cytokinesis, which result in formation of multinuclei in U251MG cells. These observations suggest that h-l(3)mbt protein has functions distinct from those of PcG proteins and may play a role in proper progression of cell division.

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Emerging therapeutic targets in schwannomas and meningiomas

Nakao Mitsuyoshi, Kimura Yoriyoshi, Saya Hideyuki

Expert Opinion on Therapeutic Targets 3 ( 2 ) 335 - 364 1999.06

ISSN 1472-8222

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Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD- 95/SAP90

Masuko Norio, Makino Keishi, Kuwahara Hiroaki, Fukunaga Kohji, Sudo Tamotsu, Araki Norie, Yamamoto Hideyuki, Yamada Yuji, Miyamoto Eishichi, Saya Hideyuki

Journal of Biological Chemistry 274 ( 9 ) 5782 - 5790 1999.02

ISSN 0021-9258

NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane- associated guanylate kinase family protein, is known to bind to C-terminal ends of N-methyl-D-aspartate receptor 2B (NR2B) through its PDZ (PSD- 95/Dlg/ZO-1) domains. NE-dlg/SAP102 and NR2B colocalize at synaptic sites in cultured rat hippocampal neurons, and their expressions increase in parallel with the onset of synaptogenesis. We have identified that NE-dlg/SAP102 interacts with calmodulin in a Ca²⁺-dependent manner. The binding site for calmodulin has been determined to lie at the putative basic α-helix region located around the src homology 3 (SH3) domain of NE-dlg/SAP102. Using a surface plasmon resonance measurement system, we detected specific binding of recombinant NE-dlg/SAP102 to the immobilized calmodulin with a K(d) value of 44 nM. However, the binding of Ca²⁺/calmodulin to NE-dlg/SAP102 did not modulate the interaction between PDZ domains of NE-dlg/SAP102 and the C- terminal end of rat NR2B. We have also identified that the region near the calmodulin binding site of NE-dlg/SAP102 interact with the GUK-like domain of PSD-95/SAP90 by two-hybrid screening. Pull down assay revealed that NE- dlg/SAP102 can interact with PSD-95/SAP90 in the presence of both Ca²⁺ and calmodulin. These findings suggest that the Ca²⁺/calmodulin modulates interaction of neuronal membrane-associated guanylate kinase proteins and regulates clustering of neurotransmitter receptors at central synapses.

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CD44 cleavage induced by a membrane-associated metalloprotease plays a critical role in tumor cell migration

Okamoto Isamu, Kawano Yoshiaki, Tsuiki Hiromasa, Sasaki Ji Ichiro, Nakao Mitsuyoshi, Matsumoto Mitsuhiro, Suga Moritaka, Ando Masayuki, Nakajima Motowo, Saya Hideyuki

Oncogene 18 ( 7 ) 1435 - 1446 1999.02

ISSN 0950-9232

CD44 is a cell surface receptor for hyaluronate, a component of the extracellular matrix (ECM). Although CD44 has been implicated in tumor invasion and metastasis, the molecular mechanisms remain to be elucidated. Here we find that CD44 expressed in cancer cells is cleaved at the membrane-proximal region of the ectodomain and the membrane-bound cleavage product can be detected using an antibody against the cytoplasmic domain of CD44. Furthermore, we report that CD44 cleavage is mediated by a membrane-associated metalloprotease expressed in cancer cells. A tissue inhibitor of metalloproteases-1 (TIMP-1), as well as metalloprotease inhibitors, inhibit CD44 cleavage in the cell-free assay. Contrary, serine protease inhibitors enhance CD44 cleavage, and the enhancement can be prevented by pretreatment with a metalloprotease inhibitor. Thus, CD44 cleavage is regulated by an intricate balance between some proteases and their inhibitors. Interestingly, treatment with the metalloprotease blocker 1,10-phenanthroline, which strongly prevent the CD44 cleavage, suppressed RERF-LC-OK lung cancer cell migration on a hyaluronate substrate, but not on several other substrates. These results suggest that CD44 cleavage plays a critical role in an efficient cell-detachment from a hyaluronate substrate during the cell migration and consequently promotes CD44-mediated cancer cell migration. Our present data indicate that CD44, not only ECM per se, is one of the targets of pericellular proteolysis involved in tumor invasion and metastasis.

Localization of the gene coding for ROCK II/Rho kinase on human chromosome 2p24

Takahashi N., Tuiki H., Saya H., Kaibuchi K.

Genomics 55 ( 2 ) 235 - 237 1999.01

ISSN 0888-7543

Serine/threonine kinase ROCK II/Rho kinase, which is an isozyme of ROCK I, is one of the targets for the small GTPase Rho. ROCK II regulates the formation of actin stress fibers and focal adhesions, cytokinesis, smooth muscle contraction, and the activation of c-fos serum response element. To elucidate the role of ROCK II in human disease, we have cloned a 4363-bp cDNA encoding human ROCK II. Sequencing analysis has shown that human ROCK II contains 1388 amino acid residues with a calculated molecular mass of approximately 161 kDa. Fluorescence in situ hybridization analysis showed that the human ROCK II gene is located on chromosome 2p24. Radiation hybrid mapping has shown that the human ROCK II gene is located very close to the highly polymorphic marker D2S359.

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Comparison of PCR results using scrape/exudate, syringe-sucked fluid and biopsy samples for diagnosis of cutaneous leishmaniasis in Ecuador

Matsumoto T., Hashiguchi Y., Gomez E. A., Calvopiña M. H., Nonaka S., Saya H., Mimori T.

Transactions of the Royal Society of Tropical Medicine and Hygiene 93 ( 6 ) 606 - 607 1999

ISSN 0035-9203

A novel human nucleoside diphosphate (NDP) kinase, Nm23-H6, localizes in mitochondria and affects cytokinesis

Tsuiki Hiromasa, Nitta Masayuki, Furuya Akiko, Hanai Nobuo, Fujiwara Toshiyoshi, Inagaki Masaki, Kochi Masato, Ushio Yukitaka, Saya Hideyuki, Nakamura Hideo

Journal of Cellular Biochemistry 76 ( 2 ) 254 - 269 1999

ISSN 0730-2312

Nucleoside diphosphate kinases (NDP kinases) are enzymes known to be conserved throughout evolution and have been shown to be involved in various biological events, in addition to the 'housekeeping' phosphotransferase activity. We present the molecular cloning of a novel human NDP kinase gene, termed Nm23- H6. Nm23-H6 gene has been mapped at chromosome 3p21.3 and is highly expressed in heart, placenta, skeletal muscle, and some of the cancer cell lines. Recombinant Nm23-H6 protein has been identified to exhibit functional NDP kinase activity. Immunolocalization studies showed that both endogenous and inducibly expressed Nm23-H6 proteins were present as short, filament-like, perinuclear radical arrays and that they colocalized with mitochondria. Cell fractionation study also demonstrated the presence of Nm23-H6 protein in a mitochondria- rich fraction. Moreover, induction of overexpression of Nm23-H6 in SAOS2 cells, using the Cre-loxP gene activation system, resulted in growth suppression and generation of multinucleated cells. Flow cytometric analysis also demonstrated that the proportion of cells with more than 4N DNA content increased to 28.1% after induction of Nm23-H6, coinciding with the appearance of multinucleated cells. These observations suggest that Nm23-H6, a new member of the NDP kinase family, resides in mitochondria and plays a role in regulation of cell growth and cell cycle progression.

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Cellular signal transduction via the neurofibromatosis type 2 tumor suppressor gene product; Merlin

Araki Norie, Saya Hideyuki

Seikagaku 71 ( 2 ) 128 - 134 1999

ISSN 0037-1017

The involvement of proteasome in myogenic differentiation of murine myocytes and human rhabdomyosarcoma cells

Mugita Norifumi, Honda Yoshiomi, Nakamura Hideo, Fujiwara Toshiyoshi, Tanaka Keiji, Omura Satoshi, Shimbara Naoki, Ogawa Michio, Saya Hideyuki, Nakao Mitsuyoshi

International Journal of Molecular Medicine 3 ( 2 ) 127 - 137 1999

ISSN 1107-3756

The murine C2C12 myocytes terminally differentiate to myotubes in the mitogen-depletion, and a portion of the cells undergo apoptosis. In this study, a specific proteasome inhibitor lactacystin induced cell cycle withdrawal and precocious expression of myosin in C2C12 cells in mitogen-enriched medium, but these cells did not fuse to form myotubes. Mitogen-starved myocytes could not differentiate to myotubes under the proteasome inhibition. The genes for p21, MyoD, Myogenin and RB were activated, and p27 gene was repressed under the proteasome inhibition, suggesting the transcriptional regulation of these genes linked to the proteasome activity. The induction of p21 prior to MyoD may contribute to the incomplete myogenesis in the presence of lactacystin. In addition, lactacystin-treated C2C12 cells did not undergo apoptosis, while proteasome accumulated in the nuclei of apoptotic cells but not in those of myotubes during mitogen-depleted differentiation. Further, lactacystin induced similarly incomplete differentiation in human RD embryonal rhabdomyosarcoma cells. Our findings demonstrated that proteasome has an essential role in myogenesis, especially in transcriptional control of myogenic and cell cycle regulators, cell fusion forming myotubes, and apoptosis.

Biological aspects of the neurofibromatosis type 2 gene product

Koga Hisashi, Takeshima Hideo, Araki Norie, Saya Hideyuki

Gann Monographs on Cancer Research 46 153 - 163 1999

ISSN 0072-0151

Neurofibromatosis 2 (NF2) is an inherited disorder characterized by a predisposition to multiple intracranial tumors. The protein encoded by the NF2 gene has striking similarities to ezrin, radixin and, moesin (ERM) proteins which link membrane proteins to the cytoskeleton. To elucidate the function of NF2 protein (merlin), we attempted to identify the merlin- binding proteins. The protein-binding assay detected five merlin-binding cellular proteins (MBPs). The entire ERM-homology domain of merlin was found to be essential for binding to all five proteins. Since most reported NF2 mutations were nonsense or frameshift mutations, we next performed a protein truncation test and found that 11 of 14 NF2 patients had truncational mutations (79%). Seven of the 11 patients (64%) had a splicing abnormality which leads to absence of exons in the ERM-homology domain. To examine the biological significance of the exon-missing mutations in the ERM-homology domain, we expressed the wild-type (wt-) and the various mutant (mu-) NF2s in a fibroblast cell line. The wt-NF2 showed intense punctate staining in the perinuclear cytoplasm in addition to overall staining of the submembranous area, whereas the mu-NF2s lacking exons in the ERM-homology domain showed granular staining at the perinuclear region without any accumulation at the submembrane region. Microinjection of wt-NF2 cDNA into the nucleus of fibroblasts revealed that wt-NF2 protein induced a progressive elongation of cell processes. Furthermore, cells that expressed mu-NF2 had decreased adhesion, which resulted in their detachment from the substratum. These findings suggest that the exon-missing mutations in the ERM-homology domain, through the loss of binding to MBPs, affect cell membrane-cytoskeleton signaling and consequently disrupt cell-to-cell or cell-to-matrix interaction.

Roles of Rho-associated kinase in cytokinesis; mutations in Rho- associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments

Yasui Yoshihiro, Amano Mutsuki, Nagata Koh Ichi, Inagaki Naoyuki, Nakamura Hideo, Saya Hideyuki, Kaibuchi Kozo, Inagaki Masaki

Journal of Cell Biology 143 ( 5 ) 1249 - 1258 1998.11

ISSN 0021-9525

Rho-associated kinase (Rho-kinase), which is activated by the small GTPase Rho, regulates formation of stress fibers and focal adhesions, myosin fiber organization, and neurite retraction through the phosphorylation of cytoskeletal proteins, including myosin light chain, the ERM family proteins (ezrin, radixin, and moesin) and adducin. Rho-kinase was found to phosphorylate a type III intermediate filament (IF) protein, glial fibrillary acidic protein (GFAP), exclusively at the cleavage furrow during cytokinesis. In the present study, we examined the roles of Rho-kinase in cytokinesis, in particular organization of glial filaments during cytokinesis. Expression of the dominant-negative form of Rho-kinase inhibited the cytokinesis of Xenopus embryo and mammalian cells, the result being production of multinuclei. We then constructed a series of mutant GFAPs, where Rho-kinase phosphorylation sites were variously mutated, and expressed them in type III IF-negative cells. The mutations induced impaired segregation of glial filament (GFAP filament) into postmitotic daughter cells. As a result, an unusually long bridge-like cytoplasmic structure formed between the unseparated daughter cells. Alteration of other sites, including the cdc2 kinase phosphorylation site, led to no remarkable defect in glial filament separation. These results suggest that Rho-kinase is essential not only for actomyosin regulation but also for segregation of glial filaments into daughter cells which in turn ensures correct cytokinetic processes.

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Multifocal renal cell carcinoma

Miyake Hideaki, Nakamura Hideo, Hara Isao, Gohji Kazuo, Arakawa Soichi, Kamidono Sadao, Saya Hideyuki

Clinical Cancer Research 4 ( 10 ) 2491 - 2494 1998.10

ISSN 1078-0432

The reported incidence of satellite tumor lesions in kidneys resected by radical nephrectomy for renal cell carcinoma (RCC) is 7-25%; however, genetic analyses of satellite tumors in comparison with those of main tumor lesions have not been performed well. In the present study, we investigated the incidence of loss of heterozygosity (LOH) at chromosome arms 3p, 6q, 8p, 9p, 9q, and 14q using 18 microsatellite markers in 10 nonpapillary RCCs of 50 mm or less in diameter and the accompanying satellite tumor lesions to evaluate the genetic alterations in main and satellite tumors. LOH was detected in 10, 3, 5, 3, 2, and 3 cases at chromosome arms 3p, 6q, 8p, 9p, 9q, and 14q, respectively. In addition, primary and satellite tumor lesions in 8 of 10 cases exhibited identical patterns of LOH on the 18 loci examined. In the remaining two cases, both main and satellite tumors demonstrated LOH on the common seven and three loci, respectively, whereas for another locus, LOH was observed only in the satellite tumor lesions. The similarity of LOH patterns detected in main and satellite tumor lesions indicates that the presence of satellite tumors might be the result of intrarenal metastasis from the main tumor lesion. These findings strongly suggest that even in case of small nonpapillary RCC, nephron-sparing surgery might carry the risk of failing to prevent postoperative local recurrence due to the incomplete resection of unrecognized satellite tumors with genetic alterations similar to those of the main tumor.

Impairment of cell adhesion by expression of the mutant neurofibromatosis type 2 (NF2) genes which lack exons in the ERM-homology domain

Koga Hisashi, Araki Norie, Takeshima Hideo, Nishi Toru, Hirota Toru, Kimura Yoriyoshi, Nakao Mitsuyoshi, Saya Hideyuki

Oncogene 17 ( 7 ) 801 - 810 1998.08

ISSN 0950-9232

Neurofibromatosis 2 (NF2) is an inherited disorder characterized by a predisposition to multiple intracranial tumors. The protein encoded by the NF2 gene has striking similarities to ezrin, radixin and moesin (ERM) proteins which link membrane proteins to the cytoskeleton. Therefore, it can be speculated that the disruption of cytoskeletal organization by alterations in the NF2 gene is involved in the development of tumors. It has been reported that the majority of NF2 mutations were nonsense or frameshift mutations that result in premature termination of translation. To facilitate the detection of these mutations, we performed protein truncation test and found that 11 of 14 NF2 patients had truncational mutations (79%). Seven of the 11 patients (64%) had a splicing abnormality which lead to absence of exons in the ERM homology domain. To examine the biological significance of the exon-missing mutations in the ERM homology domain, we expressed the wild-type (wt-NF2) and the various mutant NF2s (mu-NF2s) in a fibroblast cell line by using both liposome-mediated transfection and nuclear microinjection of the expression plasmids. The wt-NF2 showed intense punctate staining in the perinuclear cytoplasm in addition to overall staining of the submembranous area, whereas the mu-NF2s lacking exons in the ERM homology domain showed granular staining at the perinuclear region without any accumulation at the submembrane region. Microinjection of wt-NF2 cDNA into the nucleus of VA13 cells revealed that wt-NF2 protein induced a progressive elongation of cell processes. Furthermore, cells that expressed mu-NF2 had decreased adhesion, which resulted in detachment from the substratum. These findings suggested that the exon-missing mutations in the ERM-homology domain may affect cell membrane-cytoskeleton signaling and consequently disrupt cell-to-cell or cell-to-matrix interaction.

Identification of a novel human homolog of the Drosophila dlg, P-dlg, specifically expressed in the gland tissues and interacting with p55

Nakamura Hideo, Sudo Tamotsu, Tsuiki Hiromasa, Miyake Hideaki, Morisaki Tetsuro, Sasaki Ji Ichiro, Masuko Norio, Kochi Masato, Ushio Yukitaka, Saya Hideyuki

FEBS Letters 433 ( 1-2 ) 63 - 67 1998.08

ISSN 0014-5793

We have identified a novel human homolog of the Drosophila dlg tumor suppressor gene, termed P-dlg, which has been mapped at chromosome 10q23. Unlike other human dlg homologs, P-dlg is expressed in placenta and various gland tissues but not in brain. The P-dlg protein is localized at the plasma membrane and cytoplasm, and it is expressed in the gland epithelial cells in normal prostate tissue but not in prostate cancer cell lines. Furthermore, we identified interaction between P-dlg and p55 palmitoylated membrane protein by yeast two-hybrid screening. These findings suggest that P-dlg forms a complex with p55 at the plasma membrane and plays roles in maintaining the structure of epithelial cells and transmitting extracellular signals to the membrane and cytoskeleton, which may negatively regulate cell proliferation. Copyright (C) 1998 Federation of European Biochemical Societies.

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The involvement of calpain-dependent proteolysis of the tumor suppressor NF2 (merlin) in schwannomas and meningiomas

Kimurau Yoriyoshi, Koga Hisashi, Araki Norie, Mugita Norifumi, Fujita Naoyuki, Takeshima Hideo, Nishi Tohru, Yamashima Tetsumori, Saido Takaomi C., Yamasaki Toshiki, Moritake Kouzo, Saya Hideyuki, Nakao Mitsuyoshi

Nature Medicine 4 ( 8 ) 915 - 922 1998.08

ISSN 1078-8956

Neurofibromatosis type 2 (NF2) protein, also known as merlin or schwannomin, is a tumor suppressor, and NF2 is mutated in most schwannomas and meningiomas. Although these tumors are dependent on NF2, some lack detectable NF2 mutations, which indicates that alternative mechanisms exist for inactivating merlin. Here, we demonstrate cleavage of merlin by the ubiquitous protease calpain and considerable activation of the calpain system resulting in the loss of merlin expression in these tumors. Increased proteolysis of merlin by calpain in some schwannomas and meningiomas exemplifies tumorigenesis linked to the calpain-mediated proteolytic pathway.

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Significant correlation of nitric oxide synthase activity and p53 gene mutation in stage I lung adenocarcinoma

Fujimoto Hisao, Sasaki Ji Ichiro, Matsumoto Mitsuhiro, Suga Moritaka, Ando Yukio, Iggo Richard, Tada Mitsuhiro, Saya Hideyuki, Ando Masayuki

Japanese Journal of Cancer Research 89 ( 7 ) 696 - 702 1998.07

ISSN 0910-5050

Nitric oxide (NO) and its derivatives can directly cause DNA damage and mutation in vitro and may play a role in the multistage carcinogenic process. It has been reported that NO induces mutation in the p53 tumor suppressor gene; we therefore analyzed the relationship between NO synthase (NOS) activity and p53 gene status in early-stage lung adenocarcinoma. Surgical samples were classified into two categories: 14 lung adenocarcinomas with high NOS activity (> 25 pmol/min/g tissue, category A), and 16 with low NOS activity (< 25 pmol/min/g tissue, category B). A yeast functional assay for p53 mutations disclosed a red colony that corresponded to a mutation in the p53 gene in 8 cases (57.1%) in category A and 3 cases (18.8%) in category B, the frequency being significantly higher in the former (P < 0.05). A p53 DNA sequence analysis revealed that 5 of the 8 p53 mutation-positive samples in category A had a G:C-to-T:A transversion, which is reported to he a major target of NO. The mechanism of carcinogenesis of adenocarcinoma is not fully understood, but these results suggest that an excess of endogenously formed NO may induce a p53 gene mutation containing mainly G:C-to-T:A transversion in the early stage of lung adenocarcinoma. Our results suggest that NO has potential mutagenic and carcinogenic activity, and may play important roles in human lung adenocarcinoma.

Association of the myosin-binding subunit of myosin phosphatase and moesin

Fukata Yuko, Kimura Kazushi, Oshiro Noriko, Saya Hideyuki, Matsuura Yoshiharu, Kaibuchi Kozo

Journal of Cell Biology 141 ( 2 ) 409 - 418 1998.04

ISSN 0021-9525

The small GTPase Rho is believed to regulate the actin cytoskeleton and cell adhesion through its specific targets. We previously identified the Rho targets: protein kinase N, Rho-associated kinase (Rho-kinase), and the myosin-binding subunit (MBS) of myosin phosphatase. We found that in MDCK epithelial cells, MBS accumulated at the tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling area, where moesin, a member of the ERM (ezrin, radixin, and moesin) family, was localized. Neither membrane ruffling nor an accumulation of moesin and MBS at the free-end plasma membrane was induced when MDCK cells were stimulated with TPA after the microinjection of C3, which ADP-ribosylates and inactivates Rho. MBS was colocalized with moesin at the cell-cell contact sites in MDCK cells. We also found that moesin was coimmunoprecipitated with MBS from MDCK cells. Recombinant MBS interacted with the amino-terminal domains of moesin and ezrin. Myosin phosphatase composed of the catalytic subunit and MBS showed phosphatase activity toward moesin, which was phosphorylated by Rho-kinase. The phosphatase activity was inhibited when MBS was phosphorylated by Rho- kinase. These results suggest that MBS is recruited with moesin to the plasma membrane and that myosin phosphatase and Rho-kinase regulate the phosphorylation state of moesin downstream of Rho.

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Rapid identification of Leishmania species from formalin-fixed biopsy samples by polymorphism-specific polymerase chain reaction

Mimori Tatsuyuki, Sasaki Ji ichiro, Nakata Motomi, Gomez Eduardo A., Uezato Hiroshi, Nonaka Shigeo, Hashiguchi Yoshihisa, Furuya M. Masato, Saya Hideyuki

Gene 210 ( 2 ) 179 - 186 1998.04

ISSN 0378-1119

The precise identification and classification of Leishmania species is important for public health surveillance since different species cause different clinical features of the disease. A highly specific polymerase chain reaction (PCR) panel was developed to enable the identification of the five major Leishmania species that cause New World cutaneous leishmaniases. The primers used for this panel were designed to distinguish the polymorphism in sequences of commonly amplified DNA bands of the parasites produced by arbitrarily primed PCR. These polymorphism-specific PCR diagnoses were performed with formalin-fixed biopsy specimens of the leishmanial lesions from four patients in Ecuador and one hamster skin lesion, and these lesions were determined to be caused by Leishmania (Viannia) panamensis, L. (Leishmania) mexicana, and L. (L.) amazonensis. The PCR panel may offer an important and practical approach to the standardized identification of Leishmania species in field examinations.

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Neurosurgery and molecular biology

Nakamura Hideo, Saya Hideyuki

Neurological Surgery 26 ( 3 ) 200 - 206 1998.03

ISSN 0301-2603

Expression of CD44 splicing isoforms in lung cancers

Sasaki J. I Ichiro, Tanabe Kenneth K., Takahashi Kazuhisa, Okamoto Isamu, Fujimoto Hisao, Matsumoto Mitsuhiro, Suga Moritaka, Ando Masayuki, Saya Hideyuki

International Journal of Oncology 12 ( 3 ) 525 - 533 1998.03

ISSN 1019-6439

We examined CD44 isoform expression in 138 frozen tissue samples, which included primary lung carcinomas, adjacent non-tumorous lung tissues and benign lung diseases, by both reverse transcriptase polymerase chain reaction (RT-PCR) and immunohistochemical analyses. CD44v8-10 mRNA and protein were dominantly expressed in non-small cell lung carcinomas (NSCLC), while non-tumorous tissues principally expressed CD44s and small cell lung carcinomas (SCLC) expressed either CD44s or no detectable CD44. These results indicate that CD44v8-10 is the dominant splicing isoform in NSCLC and can be practically utilized as a diagnostic marker and therapeutical target in NSCLC.

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