WO1989002474A1 - Method for diagnosis of cancer diseases - Google Patents

Method for diagnosis of cancer diseases Download PDF

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Publication number
WO1989002474A1
WO1989002474A1 PCT/JP1988/000898 JP8800898W WO8902474A1 WO 1989002474 A1 WO1989002474 A1 WO 1989002474A1 JP 8800898 W JP8800898 W JP 8800898W WO 8902474 A1 WO8902474 A1 WO 8902474A1
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Prior art keywords
amount
liver
serum
acetylglucosamine
glycoprotein
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PCT/JP1988/000898
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English (en)
French (fr)
Inventor
Atusi Nisikawa
Naoyuki Taniguti
Isamu Takagahara
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Oriental Yeast Co., Ltd.
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Application filed by Oriental Yeast Co., Ltd. filed Critical Oriental Yeast Co., Ltd.
Priority to DE3853582T priority Critical patent/DE3853582T2/de
Priority to EP88907811A priority patent/EP0334962B1/en
Publication of WO1989002474A1 publication Critical patent/WO1989002474A1/ja
Priority to CA000597178A priority patent/CA1335071C/en

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    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/574—Immunoassay; Biospecific binding assay; Materials therefor for cancer
    • G01N33/57469—Immunoassay; Biospecific binding assay; Materials therefor for cancer involving tumor associated glycolinkage, i.e. TAG
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
    • A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
    • A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
    • A61K47/62—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being a protein, peptide or polyamino acid
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/48—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving transferase
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/574—Immunoassay; Biospecific binding assay; Materials therefor for cancer
    • G01N33/57407—Specifically defined cancers
    • G01N33/57438—Specifically defined cancers of liver, pancreas or kidney

Definitions

  • the present invention relates to a method for diagnosing a disease.
  • the present invention provides a method for increasing the amount of UDP-N-acetyl-glucosamme: glycoprotein N-acetylglucosaminyl-transierase (hereinafter, Gn- ⁇ - ⁇ ) in body fluids by increasing the amount of liver and the like.
  • the present invention relates to a method for diagnosing a disease.
  • the present invention is intended to more easily detect cancer diseases such as liver cancer (cirrhosis) by measuring the increase in the amount of Gn-II-II in body fluids (eg, serum, saliva, sewage, etc.).
  • body fluids eg, serum, saliva, sewage, etc.
  • liver function tests include many test items such as GOT, GPT, LDH, and ChE, and these are appropriately tested to diagnose liver function.
  • liver cancer tests are only for the purpose of detecting liver functions by comparing the degree of liver function, and cannot directly diagnose liver diseases, especially liver cancer. Furthermore, when diagnosing liver cancer, it is necessary to measure tumor markers such as AFP, CEA, etc., and the measurement has been performed. ⁇ However, the positive rate for conventional tumors was at most 60%, and it was almost impossible to diagnose early.
  • y-glutamino retranspeptidase has been attracting attention as a new tumor marker (particularly liver cancer). This is due to the fact that it has been known that patients with hepatic dystrophy appear in the blood with glycoproteins with different glycoproteins than normal subjects. However, this y-gluta mizoletolan transpita is not a better vagina than AFP, CEA, etc.
  • Gn-Tm activity is contained in a very small amount of about 2.0 ⁇ 0.5 nmol / m £ / h in the serum of normal subjects.
  • Serum of patients with liver cancer contains about 2-3 times the amount of Gn- ⁇ - ⁇ activity, and serum from patients with cirrhosis contains about 1.5 times the amount of Gn- ⁇ - ⁇ , and chronic hepatitis
  • For the first time it became clear that about 1.2 times the amount of Gn-T-DI was contained in the serum of these patients.
  • Gn-T- ⁇ is reacted with uridine diphospho N-acety 1-glucosamine (hereinafter referred to as UDP-GlcNAc) to convert N-acetylglucosamine into GnGnfe.
  • UDP-GlcNAc uridine diphospho N-acety 1-glucosamine
  • a fluorescent label is attached to the GnGn sugar chain and the obtained product is subjected to high-performance liquid chromatography, the fluorescence intensity of the chromatogram can be easily detected.
  • the GnGn sugar chain used in the present invention may be human transferrin.
  • GnGn sugar chains (fluorescent labeling) obtained from the obtained sugar chains by the method of Hase et al. (Hase, S. et al, Journal of Biochemistry 1984, 197-203) are shown in the formula (I). Is prepared). )
  • the portion of the compound of the formula (II) excluding 2-aminoviridine (fluorescent substance) is called GnGn sugar chain, and the compound in which fucose is bound to GlcNAc at position 1 of the GnGn sugar chain is also used. included.
  • reaction product 4GlcNAc ⁇ l-4GlcNAc-2-aminopyridine
  • the obtained reaction product was subjected to high-speed liquid chromatography to produce a chromatogram based on fluorescence intensity, and the amount of the reaction product was determined. It measures the enzymatic activity of Gn-T-III.
  • the amount of Gn- G- ⁇ can be measured not only by measuring the enzyme activity but also by an antigen-antibody reaction. (Effect)
  • the activity of Gn- ⁇ - ⁇ in serum was increased in liver disease, and the activity of Gn-T-DI was allowed to act on UDP-GlcNAc to convert N-acetylgucosamine into GnGn sugar.
  • the product was transferred to a chain, and the resulting product could be easily measured by high-speed liquid chromatography.
  • the present invention has an effect of easily diagnosing cancer diseases such as liver cancer, Next, examples of the present invention will be described.
  • Serum of primary liver asphyxia, serum of cirrhosis patient, serum of chronic hepatitis, serum of fatty liver, and serum of normal person in 50 containers each containing 50 ⁇ of the above reagent Then, the mixture was incubated at 37 ° C for 1 hour, and then the reaction was stopped by adding a 20 M solution of 0.2 M EDTA and 0.1 M sodium borate to each. 1 ⁇ H of each reaction solution was applied to a high-performance liquid chromatograph to prepare a chromatogram based on fluorescence intensity, and the specific activity of each Gn- ⁇ - ⁇ was measured.
  • Gn- ⁇ - ⁇ specific activity Serum from primary liver tumor 3.7 ⁇ 2.3 Serum from liver cirrhosis 3.3 ⁇ 1.8 Serum from invasive hepatitis 2.0 ⁇ 0.5 Fatty liver liver serum 2.0 ⁇ 0.5 Normal human serum 2.0 ⁇ 0.5

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
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  • Biotechnology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Oncology (AREA)
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Description

明 細 書 癌疾患の診断法
(産業上の利用分野）
本発明は瘙疾患の診断法に関するものである。
更に詳細には、 本発明は体液中の UDP-N-acetyl-gluco samme: glycoprotein N-acetylglucosaminyl- transierase (以下、 Gn-Τ-ΙΠ と レ、う） の量の増カロによつ て肝臓等の癀疾患を診断する方法に関するものである。
本発明は、 体液中 （例えば血清、 だ液、 屎等） の Gn- Τ-ΙΠの量の増加の測定によって、 よ り簡便に肝癌 （肝硬 変） 等の癌疾患を診新する こ と ができ るため、 医療界、 診断界に益する と ころ犬なるものがある。
(従来法及び発明が解決しょ う とする問題点）
一般に、 肝機能検査と しては、 GOT, GPT, LDH、 ChE など多く の検査事項があ り、 これ ら について適宜検査さ れ、 肝機能の診断が行なわれている。
しかし、 これらの検査事項は、 あ く までも肝機能の程 度を比較して検知する程度のものであっ て、 肝疾患、 特 に肝癌の.診断が直接できる という ものではなかつ た。 更に、 肝癌の診斬をする場合は、 AFP、 CEA等の腫瘍マー カーの測定も必要であ り 、 また、 行なわれるよ う にもな つてきた。 τ しかしながら、 従来の腫瘙マ一力一での陽性率はせい ぜぃ 6 0 %であ り、 かつ、 早期に診靳する ことは不可能 に近かった。
また、 最近、 新しい腫瘍マーカ一 （特に肝癌） と して y - グルタ ミノレトランスぺプチダーゼが注目されて来た。 これは、 肝瘙患者が、 正常人のものと比べて、 糖鎮搆造 の異なる糖蛋白質を血中に出現させる ことが知られたこ とによるものである。 しかし、 この y - グルタ ミゾレト ラ ンスぺプチタ"一ゼは AFP、 CEA 等よ り もすぐれた膣瘙 マ一力一とはなっていない。
(問題点を S決するための手段）
肝瘙患者における糖纘構造の変化を詳細に研究したと こ ろ、 ァスパラギン結合型糖鎮の ト リマン ノ シルコア部 分の β - 1,4 結合したマン ノースに Ν - ァセチルダルコ サミ ンが - 1,4 で結合したものである ことが分り、 本 発明者らは、 この ァセチルダルコサミ ンを転移結合 させる酵素の Gm-Τ-ΠΙの量が増加するのではないかと考 え、 鋭意研究した結果、 肝朦疾患、 特に肝癌の患者の血 清中に、 正常人の血清中と比較して、 Gn-T-mが有意に 高い活性を示すこ と を知り、 この Gn-Τ-ΠΙを筒易に測定 する方法を見出 し、 本発明を完成するに至っ たものであ る。
一般正常人の血清中に、 Gn-T-m活性は、 2.0±0.5 nm ol/m£/h 程度のごく微量含まれているものであるが、 肝 臓癌患者の血清中には約 2〜 3倍量の Gn-Τ-ΠΙ 活性が 含まれ、 肝硬変の患者の血清中には約 1.5倍量の Gn-Τ-ΠΙ が含まれ、 更に慢性肝炎の患者の血清中には約 1.2倍量 の Gn-T- DIが含まれているのが、 はじめて明らかとなつ たのである。
生化学会第 6 0 回大会予稿集 6 3 4頁に Gn-T- ffl の 活性測定に N-acetylglucosamine を GnGn糖鎖に転移さ せ、 得られた生成物を高速液体ク ロマ トグラ フィーによ つて測定する こ と が示されるが、 この方法を癌疾患の診 新に用いる こ とは全く知られていない。
本発明において、 Gn-Τ-ΙΠの量を測定するには、 Gn-T - ΠΙ を uridine diphospho N-acety 1- glucosamine (以下、 UDP— GlcNAcといラ）に作用させて N -acetylglucosamineを GnGnfe頻に？ s移させ、 得られた生 成物を高速液体ク ロマ 卜グラ フィ 一にかけて検出するの がよい。 この場合、 GnGn糖鎖に蛍光標識をつけておき、 得られた生成物を高速液体ク ロマ トグラ フィ 一にかけれ ば、 ク ロマ トグラムの蛍光強度をみて容易に検出する こ と ができる。 本発明で用いる GnGn糖鎖を、 まず、 ヒ ト ト ラ ンスフェ リ ンよ り得る.。 得られた糖鎖を長谷らの方 法 (Hase , S . et al , Journal of Biochemistry 1984， 197 - 203 ) によってピリ ジルア ミ ノィ匕 （蛍光標識） し た GnGn糖鎖 （式（ I )に示される）を調製する。 )
Figure imgf000006_0001
次いで、 この GnGn糖鎖に |8 -ガラク トシダーゼを作用 させて式（ II )で示される ピリ ジルアミ ノ化した GnGn糖鎖 を調製する。
5' '
Figure imgf000006_0002
本発明においては式 （ Π ) の化合物の 2 - ア ミ ノ ビリ ジン （蛍光物質） を除いた部分を GnGn糖鎖といい、 また この GnGn糖鎖の 1位の GlcNAcにフコースが結合したもの も含まれる。
本発明における Gn-T- mの反応式は次の式（ ΠΙ )に示さ れる。 蛍光標識した GnGn糖類
Figure imgf000007_0001
GlcNAc/31-2Hanal
6
GlcNAc β 1— 4 Man jS 1 __,
GlcNAc ^l-2Han a 1 3
匚 4GlcNAc β l-4GlcNAc-2-アミノピリジン こ こに得られた反応生成物を髙速液体ク ロマ ト グラ フ ィ 一にかけて、 蛍光強度によるク ロマ トグラムを作成し 反応生成物の量によっ て、 Gn-T-IIIの酵素活性を測定す るものである。
また、 Gn-Τ-ΠΙの量は酵素活性の測定以外にも、 抗原 抗体反応などによっても測定することができる。 (効 果）
本発明においては、 肝臓疾患で血清中の Gn-Τ-Πの活 性が増加する こ と を確認し、 その Gn-T-DIの活性を UDP- GlcNAcに作用させて N-acetylgucosamineを GnGn糖鎖に 転移させて、 得られた生成物を髙速液体ク ロマ トグラ フ ィ 一で容易に測定できたものである。 本発明は、 肝癌 等の癌疾患を簡便に診断できる効果を有するものである , 次に本発明の実施例を示す。
実旌树
(試薬）
250mM MES (2- (N-morpholino) ethane
sulfonic acid monohydrat e
(pH=6.25)
400mM GlcNAc (N-a6c /ety 1 lucosamine) 20mM MnCl2 40niM UDP-GlcNAc
1 , Q% Triton X - 100 150?H GnGn-糖類（蛍光標識).
上記試薬 50 ρβづっ入れた容器 50ケに、 原発性肝瘙息 者の血清、 肝硬変患者の血清、 慢性肝炎息者の血清、 脂 肪肝の息者の血清、 正常人の血清をそれぞれ 10検体づっ を 50 ί βづっ加え、 37°Cで 1時間インキュベー ト した後 それぞれに 20 A ϋの 0.2M EDTA、 0.1Mナ ト リ ウムボレー ト 溶液を加えて反応を停止した。 各反応液の 1 μ H を高速液体ク ロマ トグラ フィ ーにか けて、 蛍光強度によるク ロマ トグラムを作成し、 それぞ れの Gn-Τ-ΠΓの比活性を測定した。
その結果は次の表 1 に示される。 表 1
Gn-Τ-Π比活性 原発性肝瘙患者血清 3.7± 2.3 肝 硬 変 患 者 血 清 3·3± 1·8 侵 性 肝 炎 患 者 血 清 2.0 ± 0·5 脂 肪 肝 息 者 血 清 2.0± 0.5 正 常 人 血 清 2.0± 0.5

Claims

請求の範囲
(1 j 体液中 (Z)UDP-N-acetylglu cos amine: glycoprotein N-acetylglucosaminyltransf erase の量 ail定し、 そ の量の増加によって肝朦の疾息を診断するこ と を特徵と する瘙疾患の診新法。
(2) 量の測 73、 LlDP-N-ace ylglucosamine： glycoprotein N-acety lgluco samxny It ran sf erase を uridine■ dip - hospho N-acetylglucosamine に作 させて -acety lg- lucosamineを GnGn諳鎮に転移させ、 得られた 成物の量 を測定する ことを特墩とする特許請求の範囲第 1項記载 の瘙疾息の診断法。
PCT/JP1988/000898 1987-09-07 1988-09-06 Method for diagnosis of cancer diseases WO1989002474A1 (en)

Priority Applications (3)

Application Number Priority Date Filing Date Title
DE3853582T DE3853582T2 (de) 1987-09-07 1988-09-06 Verfahren zur diagnose von leberkrebs oder leberzirrhose.
EP88907811A EP0334962B1 (en) 1987-09-07 1988-09-06 Method for diagnosis of hepatic cancer or hepatocirrhosis
CA000597178A CA1335071C (en) 1988-09-06 1989-04-19 Diagnostic method of cirrhosis and hepatic cancer

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
JP62221992A JP2579497B2 (ja) 1987-09-07 1987-09-07 肝臓疾患診断剤
JP62/221992 1987-09-07

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WO1989002474A1 true WO1989002474A1 (en) 1989-03-23

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Title
Nihon Nogei Kagakukai-Hen (Nihon Nogei Kagakukai ABC Series (4) Koso-Biotechnology eno Shishin-I) 20 March 1985 (20. 03. 85) Asakura Shoten (Tokyo) p. 94-114 *
See also references of EP0334962A4 *
Seikagaku (The Sixtieth Times, Nippon Seikagakukai Taikai Shoroku-Go) Vol. 59, No. 8, August. 1987 (Tokyo) Fujii Shigeru, Nishikawa Atsushi, Taniguchi Naoyuki ('H-NMR Niyoru Ushi no IgG no Tosa Kozo no Kaiseki) p. 634 *

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4971905A (en) * 1987-08-11 1990-11-20 Pacific Northwest Research Foundation Diagnosis of cancerous or precancerous conditions in human secretory epithelia by enzyme activity of β-1-3N-acetylglucosaminyltransferase
US5403717A (en) * 1987-08-11 1995-04-04 Pacific Northwest Research Diagnosis of premalignant or malignant conditions of human secretory epithelia
US5032505A (en) * 1988-11-21 1991-07-16 Chembiomed, Ltd. Inhibitors for glycosaminosyl transferase V
US5206356A (en) * 1988-11-21 1993-04-27 Chembiomed, Ltd. Inhibitors for alpha-L-fucosyl transferase

Also Published As

Publication number Publication date
EP0334962B1 (en) 1995-04-12
JPS6465454A (en) 1989-03-10
EP0334962A4 (en) 1991-05-08
DE3853582D1 (de) 1995-05-18
US4994374A (en) 1991-02-19
DE3853582T2 (de) 1995-11-02
JP2579497B2 (ja) 1997-02-05
EP0334962A1 (en) 1989-10-04

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