研究者詳細 - 佐藤　ちひろ

論文 - 佐藤　ちひろ

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Co-localization of receptor and transducer proteins in the glycosphingolipid-enriched, low density, detergent-insoluble membrane fraction of sea urchin sperm

Ohta K., Sato C., Matsuda T., Toriyama M., Vacquier V., Lennarz W., Kitajima K.

Glycoconjugate Journal 17 巻 ( 3-4 ) 頁： 205 - 214 2000年12月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：Glycoconjugate Journal

The low density, detergent-insoluble membrane fraction (LD-DIM), where gangliosides are likely to be highly enriched, was prepared from sperm of two sea urchin species, Hemicentrotus pulcherrimus and Strongylocentrotus purpuratus. Immunoblotting showed the presence in the LD-DIM of two receptors for egg ligands, a glycosylphosphatidylinositol (GPI)-anchored protein, and four proteins which may be involved in signal transduction. Co-immunoprecipitation revealed that at least three proteins, the speract receptor, the 63kDa GPI-anchored protein and the α subunit of a heterotrimeric Gs protein, are localized in the LD-DIM. This suggests that the LD-DIM fraction may be a membrane microdomain for speract-speract receptor interaction, as well as the subsequent signal transduction pathway involved in induction of sperm respiration, motility and possibly the acrosome reaction.

DOI： 10.1023/A:1026589223811

Frequent occurrence of pre-existing α2→8-linked disialic and oligosialic acids with chain lengths up to 7 Sia residues in mammalian brain glycoproteins. Prevalence revealed by highly sensitive chemical methods and anti-di-, oligo-, and poly-Sia antibodies specific for defined chain lengths Open Access

Sato C., Fukuoka H., Ohta K., Matsuda T., Koshino R., Kobayashi K., Troy F.A., Kitajima K.

Journal of Biological Chemistry 275 巻 ( 20 ) 頁： 15422 - 15431 2000年5月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：Journal of Biological Chemistry

The pre-existence of α2→8-linked disialic acid (di-Sia) and oligosialic acid (oligo-Sia) structures with up to 7 Sia residues was shown to occur on a large number of brain glycoproteins, including neural cell adhesion molecules (N-CAMs), by two highly sensitive chemical methods (Sato, C., Inoue, S., Matsuda, T., and Kitajima, K. (1998) Anal. Biochem. 261, 191- 197; Sato, C., Inoue, S., Matsuda, T., and Kitajima, K. (1999) Anal Biochem. 266, 102-109). This unexpected finding was also confirmed using a newly developed antibody prepared using a copolymer of α2→8-linked N- acetylneuraminyl p-vinylbenzylamide and acrylamide as an immunogen and known antibodies whose immunospecificities were determined to be di- and oligo-Sia residues with defined chain lengths. The major significance of the new finding that di- and oligo-Sia chains exist on a large number of brain glycoproteins is 2-fold. First, it reveals a surprising diversity in the number and M(r) of proteins distinct from N-CAM that are covalently modified by these short sialyl glycotopes. Second, it suggests that synthesis of di- and/or oligo-Sia units may be catalyzed by α2→8-sialyltransferase(s) that are distinct from the known polysialyltransferases, STX and PST, which are partially responsible for polysialylation of N-CAM.

DOI： 10.1074/jbc.275.20.15422

Lipid raft on gametic cells as a functional domain for sperm-egg interaction coupled with signal transduction

Ohta K., Sato C., Matsuda T., Toriyama M., Vacquier V.D., Hirohashi N., Lennarz W.J., Kitajima K.

Zygote 8 巻 ( SUPPL. ) 頁： . 2000年

Ｏ‐アセチル化シアル酸　　その検出，生物学的意義，および病気における変化 Open Access

佐藤ちひろ

Ｔｒｅｎｄｓ　ｉｎ　Ｇｌｙｃｏｓｃｉｅｎｃｅ　ａｎｄ　Ｇｌｙｃｏｔｅｃｈｎｏｌｏｇｙ 12 巻 ( 63 ) 頁： 17 - 33 2000年

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：FCCA(Forum: Carbohydrates Coming of Age)

シアル酸はカルボン酸をもつ酸性9炭糖であり、一般に、細胞膜局在あるいは分泌性の複合糖質の糖鎖の最も外側に位置している。この配位は、多くの細胞間および分子間相互作用の制御に関与しやすい点で好都合である。シアル酸は構造多様性をもつが、中でも最も多く見出されるのはC-<sub>4、7、9</sub>位の<i>O</i>-アセチル化体である。<i>O</i>-アセチル化シアル酸 (<i>O</i>-AcSA) における構造多様性は、それを担っている糖鎖の結合様式、<i>O</i>-アセチル化される炭素の位置、および結合している複合糖質の性状に起因する。分析手法が改善されてきたことによって、いくつかの病気における<i>O</i>-AcSA誘導体の同定が可能になったことから、興味の中心はこの修飾反応の生物学的重要性の理解へと方向変換してきた。この総説では、様々な病理生理学的状態に伴って変化する<i>O</i>-アセチル化体の検出法やそれらの生物学的関連性に関する最新の情報を扱っている。特に、9-<i>O</i>-アセチル化シアル酸含有複合糖質 (9-<i>O</i>AcSA) がその病気の診断マーカーとして有用である二つの全く異なる病気である、急性リンパ球性白血病 (ALL) と内臓リーシュマニア症 (VL) に注目している。

DOI： 10.4052/tigg.12.17

Lipid raft on gametic cells as a functional domain for sperm-egg interaction coupled with signal transduction

Ohta K, Sato C, Matsuda T, Toriyama M, Vacquier VD, Hirohashi N, Lennarz WJ, Kitajima K

ZYGOTE 8 巻頁： S63 - S63 2000年

Lipid raft on gametic cells as a functional domain for sperm-egg interaction coupled with signal transduction.

Ohta K, Sato C, Matsuda T, Toriyama M, Vacquier VD, Hirohashi N, Lennarz WJ, Kitajima K

Zygote (Cambridge, England) 8 Suppl 1 巻頁： S63 2000年

Glycobiology of Di- and Oligosialyl Glycotopes Open Access

Sato C., Kitajima K.

Trends in Glycoscience and Glycotechnology 11 巻 ( 62 ) 頁： 371 - 390 1999年11月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：Trends in Glycoscience and Glycotechnology

α2→8-Linked di- and oligosialic acid (diSia and oligoSia) chains with DP 2,3 Sia residues are known to be common structural units of gangliosides, and to be involved in various biological processes, such as cell adhesion, cell differentiation, signal transduction, and surface expression of stage specific antigen. In contrast, little attention has been paid to the occurrence and functions of such short sialyl oligomers on glycoproteins. However, it has recently been shown that glycoproteins containing di- and oligoSia groups occur in nature more frequently than was ever recognized, as analytical methods to detect di- and oligoSia structures have improved. It is thus hypothesized that these di- and oligoSia moieties on glycoproteins may have similar important functions in common with those proposed for the gangliosides. In this review, we describe the recent advances in the study of di- and oligoSia residues on glycoproteins, including analytical methods, occurrence, functions, and biosynthetic pathways.

DOI： 10.4052/tigg.11.371

Cholesterol-dependent localization of NAP-22 on a neuronal membrane microdomain (Raft) Open Access

Maekawa S., Sato C., Kitajima K., Funatsu N., Kumanogoh H., Sokawa Y.

Journal of Biological Chemistry 274 巻 ( 30 ) 頁： 21369 - 21374 1999年7月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：Journal of Biological Chemistry

A membrane microdomain called raft has been under extensive study since the assembly of various signal-transducing molecules into this region has been envisaged. This domain is isolated as a low buoyant membrane fraction after the extraction with a nonionic detergent such as Triton X-100. The characteristic low density of this fraction is ascribed to the enrichment of several lipids including cholesterol. To clear the molecular mechanism of raft formation, several extraction methods were applied to solubilize raft components. Cholesterol extraction using methyl-β-cyclodextrin was found to be effective to solubilize NAP-22, a neuron-enriched Ca2+-dependent calmodulin-binding protein as well as one of the main protein components of brain raft. Purified NAP-22 bound to the liposomes that were made from phosphatidylcholine and cholesterol. This binding was dependent on the amount of cholesterol in liposomes. Calmodulin inhibited this binding in a dose- dependent manner. These results suggest that the presence of a calcium- dependent regulatory mechanism works on the assembly of raft within the neuron.

DOI： 10.1074/jbc.274.30.21369

Isolation and characterization of low density detergent-insoluble membrane (LD-DIM) fraction from sea urchin sperm

Ohta K., Sato C., Matsuda T., Toriyama M., Lennarz W., Kitajima K.

Biochemical and Biophysical Research Communications 258 巻 ( 3 ) 頁： 616 - 623 1999年5月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：Biochemical and Biophysical Research Communications

The low density detergent-insoluble membrane (LD-DIM) fraction was obtained by a sucrose-density gradient centrifugation from sperm of three sea urchin species, Hemicentrotus pulcherrimus, Strongylocentrotus purpuratus, and Anthocidaris crassispina. These LD-DIM preparations were characterized by enriched glycosphingolipids (GSL) including gangliosides and sulfatide (SLF), having more than 50% of the total amount of GSL present in these sperm. Interestingly, a minor component of H. pulcherrimus sperm (HO3S→8Neu5Acα2→8Neu5Acα2→6Glcβ1→Cer) was shown to be even more enriched in the LD-DIM as revealed by using monoclonal antibody (mAb.3G9) specific to this ganglioside. In addition to the GSL, phosphatidylserine (PS) and diacylglycerol (DG) were enriched in the LD-DIM. On the other hand, cholesterol (CL) and sphingomyelin (SM) were not so enriched, which contrasted with the LD-DIM from Madin-Darby canine kidney (MDCK) cells, where CL and SM were reported to be abundant. Because mammalian somatic cell-derived DIMs have been proposed to be associated with functional signal transduction, it seems possible that the ganglioside-enriched LD-DIM in sea urchin sperm can participate in binding to eggs and the subsequent egg activation process. To our knowledge this is the first chemical characterization of the LD-DIM fraction of a gametic cell.

DOI： 10.1006/bbrc.1999.0686

A 42-kDa glycoprotein from chicken egg-envelope, an avian homolog of the ZPC family glycoproteins in mammalian zona pellucida. Its first identification, cDNA cloning and granulosa cell-specific expression Open Access

Takeuchi Y., Nishimura K., Aoki N., Adachi T., Sato C., Kitajima K., Matsuda T.

European Journal of Biochemistry 260 巻 ( 3 ) 頁： 736 - 742 1999年3月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：European Journal of Biochemistry

A glycoprotein with molecular mass of 42 kDa was identified as the major component of the chicken egg-envelope, the filamentous, extracellular matrix known as the perivitelline layer. By using a DNA probe amplified with degenerative primers derived from the protein's partial amino acid sequences, a cDNA clone encoding the egg-envelope 42-kDa glycoprotein (gp42) was isolated from a hen's ovary cDNA library. The gp42 open reading frame encoded 435 amino acid residues, including a putative signal peptide of 20 amino acids. The deduced amino acid sequence of gp42 showed significant similarity to egg-envelope glycoproteins of the ZPC family of several other vertebrate species, including human ZP3, mouse ZP3, Xenopus laevis gp43 and medaka (Oryzias latipes) ZI3 (LS-F), which play important roles for sperm-egg interaction. A single N-glycosylation site present in chicken gp42 is conserved among all five of these proteins: carbohydrate analysis of gp42 revealed the presence of a complex type glycan chain at this site. N-terminal sequence analysis of the mature polypeptide suggests that C-terminal processing of the pro-protein occurs during synthesis and secretion. The 1.4- kb gp42 transcript was detected only in follicles, and was found to be accumulated in granulosa cells in a manner dependent on ovarian follicular development. Furthermore, a metabolically radio-labeled gp42 was immunoprecipitated from both cell lysate and culture supernatant of the granulosa cells with specific anti-gp42 antibody, suggesting granulosa cell- specific synthesis and secretion of the glycoprotein.

DOI： 10.1046/j.1432-1327.1999.00203.x

Fluorescent-assisted detection of oligosialyl units in glycoconjugates

Sato C., Inoue S., Matsuda T., Kitajima K.

Analytical Biochemistry 266 巻 ( 1 ) 頁： 102 - 109 1999年1月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：Analytical Biochemistry

A highly sensitive chemical method to detect various types of oligo/polysialic acid (oligo/polySia) units in glycoconjugates, i.e., α2 → 8-linked homooligo/polySia [N-acetylneuraminic acid (Neu5Ac), N- glcolylneuraminic acid (Neu5Gc), or 2-keto-3-deoxy-D-glycero-D-galacto- nononic acid], α2 → 8-linked heterodimers of Neu5Ac and Neu5Gc, α2 → 9- linked homooligo/polyNeu5Ac, and α2 → 5-O(glycolyl)-linked homooligo/polyNeu5Gc, was developed with an α-keto acid-reactive fluorescent labeling reagent, 1,2-diamino-4,5-methylenedioxybenzene (DMB). Fluorescent labeled di- or oligoSia was separated and quantitated by fluorometric anion- exchange high-performance liquid chromatography (HPLC). As little as 13 fmol of Neu5Acα2 → 8Neu5Ac was detectable by this method. When α2 → 8-linked oligo/polyNeu5Ac with on average eight Neu5Ac residues was labeled with DMB, DMB derivatives of oligomers with only lower degrees of polymerization of 2 to 7, were detected, due to concomitant partial depolymerization of oligo/polySia chain with the derivatization. For glycoproteins and glycolipids, mild acid hydrolysis was performed to release oligoSia prior to DMB derivatization. The mild acid hydrolysis/fluorometric HPLC method was also applicable to glycoprotein samples blotted on the membrane.

DOI： 10.1006/abio.1998.2921

Development of a highly sensitive chemical method for detecting α2→8- linked oligo/polysialic acid residues in glycoproteins blotted on the membrane

Sato C., Inoue S., Matsuda T., Kitajima K.

Analytical Biochemistry 261 巻 ( 2 ) 頁： 191 - 197 1998年8月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：Analytical Biochemistry

A highly sensitive chemical method for detecting α2→8-linked oligo/polysialic acid (oligo/polySia) chains was developed, including (i) periodate oxidation, reduction with sodium borohydride, and subsequent acid hydrolysis, giving rise to C7 analogues and intact C9 compounds from nonreducing terminal and internal sialic acid residues, respectively; (ii) fluorescent labeling of these C7 and C9 compounds with 1,2-diamino-4,5- methylenedioxybenzene (DMB); and (iii) quantitation of these DMB derivatives on fluorometric high-performance liquid chromatography. As little as 1 ng of internal sialic acid residues of oligo/polySia chains, the existence of which indicates the presence of oligo/polySia structure, was detectable by this method. This fluorometric C7/C9 analysis was successfully applied to glycoproteins blotted onto a slit of polyvinylidene fluoride membranes and suggested the presence of some novel oligoSia-containing glycoproteins in pig embryonic brains.

DOI： 10.1006/abio.1998.2718

Identification of oligo-N-glycolylneuraminic acid residues in mammal- derived glycoproteins by a newly developed immunochemical reagent and biochemical methods Open Access

Sato C., Kitajima K., Inoue S., Inoue Y.

Journal of Biological Chemistry 273 巻 ( 5 ) 頁： 2575 - 2582 1998年1月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：Journal of Biological Chemistry

The occurrence of the α2→8-linked oligomeric form of N- glycolylneuraminic acid (oligo-Neu5Gc) residues in mammalian glycoproteins was unequivocally demonstrated using a newly developed anti-oligo/poly- Neu5Gc monoclonal antibody as well as by chemical and biochemical methods. First, the antibody, designated mAb.2-4B, which specifically recognized oligo/poly-Neu5Gc with a degree of polymerization of >2, was developed by establishing a hybridoma cell line from P3U1 myeloma cells fused with splenocytes from an MRL autoimmune mouse immunized with dipalmitoylphosphatidylethanolamine-conjugated oligo/poly-Neu5Gc. Second, oligo-Neu5Gc was shown to occur in glycoproteins derived from pig spleen by Western blot analysis using mAb.2-4B, which was also confirmed by fluorometric high performance liquid chromatographic analysis of the product of periodate oxidation/reduction/acid hydrolysis of the purified glycopeptide fractions and by TLC and 600-MHz 1H NMR spectroscopic analysis of their mild acid hydrolysates. Finally, the ubiquitous occurrence of oligo-Neu5Gc chains as glycoproteinaceous components in Wistar rat tissue was immunochemically indicated. This is the first example demonstrating the diversity in oligo/poly-Sia structure in mammalian glycoproteins, where only poly-N- acetylneuraminic acid is known to occur. Such diversity in oligo/poly-Sia structure also implicates a diverged array of biological functions of this glycan unit in glycoproteins.

DOI： 10.1074/jbc.273.5.2575

Occurrence of terminal α2 → 8-linked disialylated poly-N-acetyllactosamine chains with Le(X) and I antigenic glycotopes in tetraantennary arms of an N-linked glycoprotein isolated from rainbow trout ovarian fluid Open Access

Funakoshi Y., Taguchi T., Sato C., Kitajima K., Inoue S., Morris H.R., Dell A., Inoue Y.

Glycobiology 7 巻 ( 2 ) 頁： 195 - 205 1997年3月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：Glycobiology

The Pronase digestion of a 54K glycoprotein present in ovarian fluid of rainbow trout yielded a major glycopeptide. Carbohydrate compositional analysis revealed that this glycopeptide was likely to possess a single large N-glycan chain having low molecular weight oligomers of N-acetylneuraminic acid (oligoNeu5Ac). Structural studies of this glycopeptide revealed novel α2 → 8-linked disialylated poly-N-acetyllactosamine chains with Le(X) and I antigenic determinants on the N-linked tetraantennary core glycan. In our recent studies (Kitazume, S., Kitajima, K., Inoue, S., Inoue, Y. and Troy, F.A. (1994) J. Biol. Chem. 269, 10330-10340) we presented evidence that synthesis of α2 → 8-linked polysialic acid (polySia) chains is a two-step process in which chain initiation is catalyzed by an α2 → 8-sialyltransferase (α2 → 8-ST; initiase) that catalyzes synthesis of the first Sia α2 → 8-linkage, forming the disialic acid (diSia) unit, Siaα2 → 8-Siaα2 → 6-Gal-.Chain polymerization is then postulated to be catalyzed by a second enzyme, an α2 → 8-polyST ('polymerase') that converts the diSia units to polySia chains. The present structural studies leading to the discovery of α2 → 8-linked disialylated units that terminate poly-N-acetyllactosamine chains in an N-linked glycoprotein is further evidence in support of our hypothesis that more than one sialyltransferase activity is required for polySia chain synthesis and polymerization.

DOI： 10.1093/glycob/7.2.195

Assembly of neuron- and radial glial-cell-derived extracellular matrix molecules promotes radial migration of developing cortical neurons 査読有り Open Access

Mubuchi A, Takechi M, Nishio S, Matsuda T, Itoh Y, Sato C, Kitajima K, Kitagawa H, Miyata S.

eLife 12 巻頁： RP92342 2024年3月

Identification of a buried β-strand as a novel disease-related motif in the human polysialyltransferases. 査読有り国際共著 Open Access

Hatanaka R, Hane M, Hayakawa K, Morishita S, Ohno S, Yamaguchi Y, Wu D, Kitajima K, Sato C

The Journal of biological chemistry 300 巻 ( 1 ) 頁： 105564 - 105564 2024年1月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：Journal of Biological Chemistry

The polysialyltransferases ST8SIA2 and ST8SIA4 and their product, polysialic acid (polySia), are known to be related to cancers and mental disorders. ST8SIA2 and ST8SIA4 have conserved amino acid (AA) sequence motifs essential for the synthesis of the polySia structures on the neural cell adhesion molecule. To search for a new motif in the polysialyltransferases, we adopted the in silico Individual Meta Random Forest program that can predict disease-related AA substitutions. The Individual Meta Random Forest program predicted a new eight-amino-acids sequence motif consisting of highly pathogenic AA residues, thus designated as the pathogenic (P) motif. A series of alanine point mutation experiments in the pathogenic motif (P motif) showed that most P motif mutants lost the polysialylation activity without changing the proper enzyme expression levels or localization in the Golgi. In addition, we evaluated the enzyme stability of the P motif mutants using newly established calculations of mutation energy, demonstrating that the subtle change of the conformational energy regulates the activity. In the AlphaFold2 model, we found that the P motif was a buried β-strand underneath the known surface motifs unique to ST8SIA2 and ST8SIA4. Taken together, the P motif is a novel buried β-strand that regulates the full activity of polysialyltransferases from the inside of the molecule.

DOI： 10.1016/j.jbc.2023.105564

Interactions between polysialic acid and dopamine-lead compounds as revealed by biochemical and in silico docking simulation analyses. 査読有り

Hayakawa K, Hane M, Hamagami H, Imai M, Tanaka H, Kitajima K, Sato C

Glycoconjugate journal 40 巻 ( 4 ) 頁： 461 - 471 2023年8月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：Glycoconjugate Journal

Polysialic acid is an important glyco-epitope in vertebrate brains, while altered expressions of polySia and biosynthetic enzyme have been reported in brain diseases such as schizophrenia and depression. Recently, the binding between polySia and dopamine and the involvement of this in Akt signaling has been demonstrated. However, the molecular mechanism underlying the binding of polySia and dopamine remains unknown. Therefore, here, we demonstrated the interaction between dopamine and polySia using frontal affinity chromatography alongside docking simulations. In addition, we prepared dopamine-lead compounds to understand the detailed molecular basis of polySia binding by frontal affinity chromatography, enzyme-linked immunosorbent assay, and docking simulations.

DOI： 10.1007/s10719-023-10119-6

その他リンク： https://link.springer.com/article/10.1007/s10719-023-10119-6/fulltext.html

Implication of N-glycolylneuraminic acid in regulation of cell adhesiveness of C2C12 myoblast cells during differentiation into myotube cells. 国際誌

Go S, Sato C, Hane M, Go S, Kitajima K

Glycoconjugate journal 39 巻 ( 5 ) 頁： 619 - 631 2022年10月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：Glycoconjugate Journal

A transition of sialic acid (Sia) species on GM3 ganglioside from N-acetylneuraminic acid (Neu5Ac) to N-glycolylneuraminic acid (Neu5Gc) takes place in mouse C2C12 myoblast cells during their differentiation into myotube cells. However, the meaning of this Sia transition remains unclear. This study thus aims to gain a functional insight into this phenomenon. The following lines of evidence show that the increased de novo synthesis of Neu5Gc residues in differentiating myoblast cells promotes adhesiveness of the cells, which is beneficial for promotion of differentiation. First, the Sia transition occurred even in the C2C12 cells cultured in serum-free medium, indicating that it happens through de novo synthesis of Neu5Gc. Second, GM3(Neu5Gc) was localized in myoblast cells, but not in myotube cells, and related to expression of the CMP-Neu5Ac hydroxylase (CMAH) gene. Notably, expression of CMAH precedes myotube formation not only in differentiating C2C12 cells, but also in mouse developing embryos. Since the myoblast cells were attached on the dish surface more strongly than the myotube cells, expression of GM3(Neu5Gc) may be related to the surface attachment of the myoblast cells. Third, exogenous Neu5Gc, but not Neu5Ac, promoted differentiation of C2C12 cells, thus increasing the number of cells committed to fuse with each other. Fourth, the CMAH-transfected C2C12 cells were attached on the gelatin-coated surface much more rapidly than the mock-cells, suggesting that the expression of CMAH promotes cell adhesiveness through the expression of Neu5Gc.

DOI： 10.1007/s10719-022-10049-9

The α2,8-sialyltransferase 6 (St8sia6) localizes in the ER and enhances the anchorage-independent cell growth in cancer. 国際誌 Open Access

Hatanaka R, Araki E, Hane M, Go S, Wu D, Kitajima K, Sato C

Biochemical and biophysical research communications 608 巻頁： 52 - 58 2022年6月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：Biochemical and Biophysical Research Communications

Sialylation, the final stage of post-translational modification of proteins, is achieved in the Golgi apparatus and is related to the malignant phenotype of cancer. Disialylation of ganglioside (GD3) by St8sia1 and polysialylation by St8sia2 and 4 have been shown to be related to malignant phenotypes; however, di/oligosialylation by St8sia6 is still unknown. In this study, we analyzed the malignant phenotype of St8sia6 and found that upregulation of St8sia6 in melanoma B16 cells increased anchorage-independent cell growth, which was not due to sialic acid cleavage by a sialidase. Moreover, unlike other sialyltransferases, St8sia6 localized to the endoplasmic reticulum (ER). We found that the localization to the Golgi apparatus could be regulated by swapping experiments using St8sia2; however, the malignant phenotype did not change. These data demonstrate that the enhancement of anchorage-independent cell growth by St8sia6 is not due to its localization of ER, but is due to the expression of the protein itself.

DOI： 10.1016/j.bbrc.2022.03.146

Comprehensive Analysis of Oligo/Polysialylglycoconjugates in Cancer Cell Lines. 国際誌 Open Access

Hane M, Kitajima K, Sato C

International journal of molecular sciences 23 巻 ( 10 ) 頁： 5569 2022年5月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：International Journal of Molecular Sciences

In cancer cells, cell-surface sialylation is altered, including a change in oligo/polysialic acid (oligo/polySia) structures. Since they are unique and rarely expressed in normal cells, oligo/polySia structures may serve as promising novel biomarkers and targets for therapies. For the diagnosis and treatment of the disease, a precise understanding of the oligo/polySia structures in cancer cells is necessary. In this study, flow cytometric analysis and gene expression datasets were obtained from sixteen different cancer cell lines. These datasets demonstrated the ability to predict glycan structures and their sialylation status. Our results also revealed that sialylation patterns are unique to each cancer cell line. Thus, we can suggest promising combinations of antibody and cancer cell for glycan prediction. However, the precise prediction of minor glycans need to be further explored.

DOI： 10.3390/ijms23105569

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