Health Sciences University of Hokkaido Academic Repository / 北海道医療大学学術リポジトリ

北海道医療大学歯学会

38588

北海道医療大学学術リポジトリ
目次
著者 北海道医療大学歯学会
雑誌名 北海道医療大学歯学雑誌
巻 40
号 2
発行年 2021-12-31
URL http://id.nii.ac.jp/1145/00065023/
北海道医療大学歯学雑誌
第40巻 第2号 令和3年12月
目 次
〔REVIEW〕
1 Effectiveness of Bee Pollen as an Anti−Aging Agent
Ariuntsetseg KHURELCHULUUN, Durga PAUDEL, Osamu UEHARA, Takahashi SHUHEI,
Dedy ARIWANSA, Koki YOSHIDA, Tetsuro MORIKAWA, Fumiya HARADA, Jun SATO, Hiroko MIURA,
Hiroki NAGAYASU, Yoshihiro ABIKO ………………………………………………………………………（117）
11 The role of flavonoids in maintaining epithelial barrier : A review
Sarita GIRI, Ayuko TAKADA, Durga PAUDEL, Osamu UEHARA, Yoshihiro ABIKO and Yasushi FURUICHI
……………………………………………………………………………………………………………………（127）
〔原著〕
21 骨格性Ⅰ級不正咬合の抜歯非抜歯ボーダーライン症例における治療前後の比較
山田 隆介，中尾 友也，飯嶋 雅弘 ………………………………………………………………………（137）
33 Metagenomic analyses of oral and vaginal microbiome in ovariectomized rats
Durga PAUDEL, Osamu UEHARA, Tetsuro MORIKAWA, Koki YOSHIDA, Sarita GIRI, Takao KITAGAWA,
Yuya NAKAO, Jin TSUCHIDA, Masahiro IIJIMA, Hiroko MIURA, Yasuhiro KURAMITSU, Yoshihiro ABIKO
……………………………………………………………………………………………………………………（149）
〔MINI REVIEW〕
43 The role of protein kinase C in protein secretion from salivary glands
Rezon Yanuar and Akihiko Tanimura……………………………………………………………………………（159）
〔解説〕
47 新しい非接触型3Dスキャナによる顎矯正手術前後の軟組織変化の評価
―著しい側貌の改善が得られた重度下顎前突症例による一例―
川村 尚彦，中尾 友也，南田 康人，志茂 剛，飯嶋 雅弘 …………………………………………（163）
〔歯学情報〕
63 最近のトピックス ……………………………………………………………………………………………………（179）
72 北海道医療大学歯学会会則 …………………………………………………………………………………………（188）
74 北海道医療大学歯学雑誌 投稿規程 ………………………………………………………………………………（190）
81 編集後記 ………………………………………………………………………………………………………………（197）
】Ｓｅｒｖｅｒ／歯学雑誌／第４０巻２号　　　４Ｃ１５０　１Ｃ１３３／目次　ＯＴＦ／目次（和文）  2022.02.10 10.29.03  Page 1 


Japanese

Durga, PAUDEL

38614

Osamu, UEHARA

38615

Tetsuro, MORIKAWA

38616

Koki, YOSHIDA

38617

Sarita, GIRI

38618

Takao, KITAGAWA

38619

Yuya, NAKAO

38620

Jin, TSUCHIDA

38621

Masahiro, IIJIMA

38622

Hiroko, MIURA

38623

Yasuhiro, KURAMITSU

38624

Yoshihiro, ABIKO

38625

English

Metagenomic analyses of oral and vaginal microbiome in ovariectomized rats

北海道医療大学博士（歯学）令和3年度thesi

Gazi, Mehedi Hasan

38659

Corrosion Behavior of Dental Implant Materials in Acidic Fluoride Solution

北海道医療大学人間基礎科学論集編集委員会

38583

北海道医療大学学術リポジトリ
奥付
著者 北海道医療大学人間基礎科学論集編集委員会
雑誌名 北海道医療大学人間基礎科学論集
号 47
発行年 2021-11-30
URL http://id.nii.ac.jp/1145/00065018/
執筆者（掲載順）
ショーン ホガード（看護福祉学部講師 英語）
塚 越 博 史（歯学部教授 英語）
礒 部 太 一（歯学部講師 生命倫理・科学技術社会論）
北海道医療大学人間基礎科学論集 第４７号 編集委員会
委員長 白 鳥 亜矢子（医療技術学部講師 英語）
委 員 安 部 博 史（心理科学部教授 多職種連携）
塚 越 博 史（歯学部教授 英語）
井 上 貴 翔（看護福祉学部講師 文学）
姫 嶋 瑞 穂（薬学部講師 法学）
森 元 良 太（リハビリテーション科学部・心理科学部准教授 哲学）
北海道医療大学人間基礎科学論集 第４７号
発 行 日 令和三年１１月３０日
発行兼編集者 北海道医療大学人間基礎科学論集編集委員会
〒０６１―０２９３ 北海道石狩郡当別町金沢１７５７
電話 ０１３３―２３―１２１１
印 刷 所 山藤三陽印刷株式会社
〒０６３―００５１ 札幌市西区宮の沢１条４丁目１６―１
電話 ０１１―６６１―７１６３
Ｓｅｒｖｅｒ／北海道医療大学人間基礎科学論集／第４７号　，。　印刷はしない／本文／おくづけ　　　　　　　　　　　　　　　Ｅ  2022.01.19 13.05.42  Page 1008 


奥付

Rezon, Yanuar

38626

Akihiko, Tanimura

38627

北海道医療大学学術リポジトリ
The role of protein kinase C in protein
secretion from salivary glands
著者 Rezon Yanuar, Akihiko Tanimura
journal or
publication title
The Dental Journal of Health Sciences
University of Hokkaido
volume 40
number 2
page range 43-46
year 2021-12-31
URL http://id.nii.ac.jp/1145/00065029/
Protein secretion from salivary glands has been studied
extensively using parotid acinar cells, and stimulation of β−
adrenergic receptors (β−AR) expressed on these cells in-
duces exocytotic secretion of amylase. This process is in-
duced by the Gs protein−mediated activation of adenylyl
cyclase (AC), and by the subsequent production of cAMP
and the activation of cAMP−dependent protein kinase (PKA)
(Baum, 1987 ; Shimomura et al., 2004 ; Takuma & Ichida,
1994). Protein kinase C (PKC) is also involved in amylase
secretion from parotid acinar cells via stimulation of mus-
carinic receptors (Satoh et al. , 2009 ; Shimomura et al. ,
1988 ; Terzian et al., 1996).
PKA− and PKC−dependent amylase secretion was origi-
nally thought to occur via separate pathways activated by
sympathetic and parasympathetic stimulation, respectively.
However, accumulating evidence indicates that PKC func-
tions downstream of PKA and promotes protein secretion
via phosphorylation of myristoylated alanine−rich C kinase
substrate (MARCKS) (Fig. 1).
MARCKS is a major cellular substrate for PKC. Phospho-
rylated MARCKS (MARCKSp) translocates from the plasma
membrane to the cytosol, and this process facilitates exocy-
tosis ( Aderem, 1992 ) . MARCKS phosphorylation is in-
volved in protein secretion from exocrine glands, such as
parotid glands and pancreas (Satoh et al., 2009 ; Satoh et al.,
2016 ; Satoh et al., 2019).
It has been found that β−AR−mediated amylase secretion
from parotid acinar cells is reduced to 50%−70% by MANS
peptide (a MARCKS inhibitor), calphostin C (CalC ; a non−
selective PKC inhibitor), and rottlerin (a PKCδ−specific in-
hibitor). In addition, β−AR−mediated MARCKS phospho-
rylation is inhibited by H89 (a PKA inhibitor), CalC, and
rottlerin. H89 also inhibits β−AR−mediated activation of
PKCδ (Satoh et al. , 2009 ) . These findings indicate that
MARCKS is phosphorylated by PKCδ through the activa-
tion of PKA, and this phosphorylation induces amylase se-
cretion from parotid acinar cells (Fig. 1).
PKC has several isoforms that are classified into three
types : 1) diacylglycerol (DAG) and Ca2+−dependent conven-
tional PKCs (cPKC) , which contain the isoforms PKCα,
PKCβ, and PKCγ ; 2) DAG−dependent and Ca2+−independ-
ent novel PKC (nPKC), which contain the isoforms PKCδ,
PKCε, PKCη, and PKCθ ; and 3) DAG and Ca2+−independ-
ent atypical PKC (aPKC), which contain the isoforms PKCι,
PKCκ, and PKCλ (Jaken, 1996 ; Newton, 1995). Rat parotid
acinar cells express PKCα, PKCδ, PKCε, and PKCζ
(Terzian et al., 1996), whereas rat sublingual acinar cells ex-
press PKCα, PKCβ1, PKCδ, PKCε, and PKCη (Culp et al.,
2011).
PKCδ is a nPKC, which is activated by DAG in a Ca2+−
independent manner ; thus PKCδ is expected to be involved
in Gq/11 protein−mediated protein secretion. Indeed, the role
of PKCδ − MARKCS in cholecystokinin ( CCK ) − induced
amylase release was demonstrated in rat pancreatic acinar
cells (Satoh et al., 2016). CCK is a peptide hormone in gas-
trointestinal system and stimulates exocytotic release of di-
gestive enzymes including amylase from pancreatic acinar
cells. The CCK receptor is a Gq/11 protein−coupled receptor
and activates phospholipase Cβ ( PLCβ ) to catalyze the
cleavage of the membrane lipid phosphatidylinositol 4,5−
biphosphate (PIP2) and to generate the second messengers
inositol 1,4,5−triphosphate (IP3) and DAG. The PLCβ−medi-
ated production of DAG could induce amylase secretion
through the activation of PKCδ and subsequent phosphoryla-
tion of MARKS.
In parotid acinar cells, however, β−AR agonists induce
amylase secretion via the activation of PKA. How does
〔MINI REVIEW〕
The role of protein kinase C in protein secretion from salivary glands
Rezon Yanuar and Akihiko Tanimura
Division of Pharmacology, School of Dentistry, Health Sciences University of Hokkaido
Key words : salivary gland, protein secretion, myristoylated alanine−rich C kinase substrate, protein kinase C, cAMP−depend-
ent protein kinase
43北海道医療大学歯学雑誌 40（43－46）令和3年
（159）
第４０巻２号　　　４Ｃ１５０　１Ｃ１３３／本文　※３１‐１から組体裁変更　ＯＴＦ／０４３～０４６　ミニレビュ　Ｙａｎｕａｒ  2022.02.09 20.44.20  Page 43 
PKA activate PKCδ? There are two possible mechanisms for
the PKA−mediated activation of PKCδ. One possibility is
that PKA directly phosphorylates PKCδ, although there is
no reported evidence to support this notion. Another possi-
ble mechanism is that PKCδ is activated by phospholipase D
(PLD) through a pathway that involves DAG production
mediated by the PLD–phosphatidic acid (PA) phosphatase
pathway (Fig. 1).
Phospholipase D is a membrane−bound enzyme that cata-
lyzes the hydrolysis of phospholipid substrates, including
phosphatidylcholine (PC), to generate PA and water−soluble
bases. In addition, PA phosphatase converts PA to form
DAG (Su & Frohman, 2010).
The role of PKA in the activation of PLD was suggested
by studies showing that PKA inhibitors suppress PLD activ-
ity in the rat mast cell line RBL−2H3 (Choi et al., 2002).
Moreover, a PLD inhibitor suppresses GLP−1−induced amy-
lase release in rat pancreatic acinar cells (Satoh & Kashi-
mata, 2018). In rat parotid acinar cells, activation of PLD
occurs through a Ca2+−independent pathway (Guillemain &
Rossignol, 1994), and PLD contributes to β−AR−mediated
amylase release (Dohke et al., 2002). Taken together, these
findings indicate that PKCδ is likely activated by DAG
through the PKA−mediated activation of PLD (Fig. 1).
The studies described above show that PKCδ is a key en-
zyme in protein exocytosis and is involved in both Gs− and
Gq/11−protein−mediated protein secretion from parotid acinar
cells. Namely, PKCδ is activated in a DAG−dependent man-
ner by PKA−induced activation of PLD−PA phosphatase,
which mediates Gs protein−mediated protein secretion, and is
also directly activated by PLC, which mediates Gq/11 protein−
mediated protein secretion (Fig. 1).
Unlike amylase secretion from parotid acinar cells which
is controlled primarily by sympathetic nerve, mucin secre-
tion from sublingual glands is predominantly regulated by
parasympathetic nerve. Interestingly, mucous secretion from
rat sublingual glands is regulated by muscarinic receptors
through the activation of PLCβ and subsequent activation of
PKCα, without the involvement of PKCδ (Fig. 2) (Culp et
al. , 2011 ; Culp et al. , 2020) . In this signaling pathway,
PLCβ produces DAG and IP3, and then IP3 triggers an in-
crease in the intracellular Ca2+ concentration ([Ca2+]i) via IP3
Figure 1. A schematic illustration of intracellular signaling pathways involved in protein secretion from parotid acinar cells.
Stimulation of M3 muscarinic receptors (M3R) results in the dissociation of Gq/11 proteins and activation of phospholipase C−β(PLCβ),
which hydrolyzes the membrane lipid phosphatidylinositol 4,5−biphosphate (PIP2) to generate inositol 1,4,5−triphosphate (IP3) and DAG
(blue line). PKCδ is activated by DAG and phosphorylates MARCKS protein. Phosphorylated MARCKS translocates from the mem-
brane to the cytosol to facilitate exocytosis in parotid acinar cells (red line). On the other hand, stimulation of β−adrenergic receptors (β
−AR) results in the dissociation of Gs proteins and activates adenylyl cyclase (AC), which converts ATP to cAMP, followed by the acti-
vation of PKA and then PLD. The activation of PLD causes hydrolysis of phosphatidylcholine (PC) to generate phosphatidic acid (PA),
which is then involved in the formation of diacylglycerol (DAG) (orange line) . PKCδ is activated by DAG and phosphorylates
MARCKS protein (red lines).
AC : adenylate cyclase, β−AR : β−adrenergic receptor, DAG : diacylglycerol, IP3 : inositol 1,4,5−triphosphate, M3R : M3 muscarinic recep-
tor, PA : phosphatidic acid, PC : phosphatidylcholine, PIP2 : phosphatidylinositol 4,5−biphosphate, PLCβ : phospholipase C−β, PLD :
phospholipase D.
44 Rezon Yanuar et al.／The role of protein kinase C in protein secretion from salivary glands
（160）
第４０巻２号　　　４Ｃ１５０　１Ｃ１３３／本文　※３１‐１から組体裁変更　ＯＴＦ／０４３～０４６　ミニレビュ　Ｙａｎｕａｒ  2022.02.09 20.44.20  Page 44 
receptor−mediated Ca2+ release from intracellular stores and
subsequent Ca2+ entry into the cell via store−operated Ca2+
entry (Putney, 2010).
Protein exocytosis from the sublingual gland occurs in
two phases, during which DAG and [Ca2+]i act together to
mediate mucin secretion via PKCα. In the resting state,
PKCα is detected in the lateral and basal /perinuclear re-
gions. After 1 minute of CCh stimulation, PKCα is detected
in apical regions, where it persists for at least 30 min. This
finding suggests that the translocation of PKCα to the apical
membrane is responsible for the priming or docking of mu-
cin granules during exocytosis (Culp et al., 2011).
Together, these studies reveal that PKC isoforms induce
protein secretion through different mechanisms in parotid
(Fig. 1) and sublingual acinar cells (Fig. 2). The studies also
show that PKC isoforms have different cell−specific func-
tions that are dependent upon their expression patterns and
the expression of other regulatory molecules.
References
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Figure 2. A schematic illustration of the intracellular signaling pathways involved in protein secretion from sublingual acinar cells.
Stimulation of the M3 muscarinic receptor (M3R) results in the dissociation of Gq/11 proteins and the activation of PLCβ, which hydro-
lyzes the membrane lipid phosphatidylinositol 4,5−biphosphate (PIP2) to form inositol 1,4,5−triphosphate (IP3) and diacylglycerol (DAG).
IP3 activates IP3 receptors (IP3Rs) on the endoplasmic reticulum and releases stored Ca2+ into the cytosol (blue line). PKCα is activated
by DAG together with Ca2+, translocates to the apical membrane of the acinar cell, and promotes protein exocytosis from sublingual aci-
nar cells (red line).
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biphosphate, PLCβ : phospholipase C−β.
45The Dental Journal of Health Sciences University of Hokkaido 40 2021
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−induced amylase release in rat pancreatic acini. Am J
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46 Rezon Yanuar et al.／The role of protein kinase C in protein secretion from salivary glands
（162）
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The role of protein kinase C in protein secretion from salivary glands

38656

北海道医療大学学術リポジトリ
編集後記
著者 北海道医療大学歯学会
雑誌名 北海道医療大学歯学雑誌
巻 40
号 2
発行年 2021-12-31
URL http://id.nii.ac.jp/1145/00065041/
編 集 後 記
次号（第41巻，第1号）の発行は令和4年6月30日です．
投稿原稿募集の締め切りは令和4年3月31日必着と致します．期日厳守の上，ご投稿をお願いします．本誌投
稿規定は，2021年第40巻，第2号の巻末をご参照ください．
昨今のコロナ感染拡大の再燃の状況におきましても，精力的に論文等を投稿していただいた皆様並びに論文の査読
を快く引き受けていただいた先生方に心から感謝申し上げます．
本号は総説（ミニレビューを含む）3編，原著論文2編，解説論文1編並びに最近のトピックス5編から成り，ボ
リューム満点のものになりました．巻頭の総説ではSarita Giri先生（歯周歯内治療学分野）から上皮のバリア機能に
おけるフラボノイドの役割，Ariuntsetseg Khurelchuluun先生（臨床口腔病理学分野）からはミツバチ花粉のアンチエ
ージング効果並びにRezon Yanuar先生（薬理学分野）からは唾液タンパク分泌におけるPKCの役割についてそれぞれ
紹介されています．原著論文では，山田隆介先生（歯科矯正学分野）から骨格性Ⅰ級抜歯・非抜歯ボーダーライン症
例の矯正歯科治療における独自の評価法が示されています．また，Durga Paudel先生（臨床口腔病理学分野）の原著
論文では，更年期女性にみられる口腔等の灼熱感や乾燥状態と細菌叢の変化との因果関係が示唆されています．解説
論文では，川村尚彦先生（歯科矯正学分野）から新しい非接触型3Dスキャナによる顎矯正手術前後の軟組織変化の
評価法について，実際の症例に基づいてわかりやすく解説されています．さらに，最近のトピックスでは，Nisrina
Ekayani Nasrun先生（組織再建口腔外科学分野）から骨の成長や骨折の治癒機転と全身栄養状態との関連（2編），村
田 勝先生（口腔再生医学分野）からは歯の移植術に関する最新の歯根膜保護装置，Jia Tang先生（同済大学）から
は新たな歯髄幹細胞の発見と臨床応用への可能性，及びDedy Ariwansa先生（臨床口腔病理学分野）からは精神活動
と口腔粘膜疾患との関連性を取り扱う新領域の精神病理学についてそれぞれ紹介されています．いずれも大変興味深
い内容ですので，是非ご一読ください．
コロナと人類の世界大戦は，長期戦の模様を呈しています．しかしながら，医療の新たな展開と人間本来の生存能
力の覚醒によって，人類はこの難局を乗り越えていくことでしょう．その時，再び自由が我々に訪れるのではないで
しょうか，いつの日か．今後も，歯学雑誌のさらなる充実に努めて参りますので，引き続きご支援ご協力を賜ります
ようどうかよろしくお願いいたします．（石井 記）
81
（197）
第４０巻２号　　　４Ｃ１５０　１Ｃ１３３／本文　※３１‐１から組体裁変更　ＯＴＦ／０８１　　　　　編集後記  2022.02.15 09.51.11  Page 81 


編集後記

北海道医療大学博士（歯学）令和2年度thesi

蓑輪, 映里佳

38395

北海道医療大学学術リポジトリ
【歯肉繊維芽細胞に対するフェニトイン(PHT)の作
用】ー生理活性物質を介するCa2+応答に対するPHT
の増強作用ー
著者 蓑輪 映里佳
学位名 博士（歯学）
学位授与機関 北海道医療大学
学位授与年度 令和2年度
学位授与番号 30110甲第347号
URL http://id.nii.ac.jp/1145/00064957/
Abstract 
 
 
Effects of phenytoin in human gingival fibroblasts 
-Augmentation of PHT on the calcium responses  
mediated by physiologically active substances- 
 
 
 
 
 
 
 
 
 
2020 
Graduate School of Dentistry, 
Health Sciences University of Hokkaido 
 
MINOWA Erika 
Introduction  
 Antiepileptic agent phenytoin (PHT) is known to inhibit voltage-gated Na+ channel and 
reduces neuronal excitability by decreasing Na+ influx. PHT is also known to induce gingival 
overgrowth, which is likely caused by the proliferation of human gingival fibroblasts (HGF) 
and the unbalance of collagen metabolism. It is suggested that the exacerbation of 
Drug-induced gingival enlargement (DIGE) is induced by environmental factors such as 
gingival inflammation. Bioactive substances produced by inflammatory responses regulate 
various cellular functions through increases in intracellular Ca2+ concentration ([Ca2+]i). It is 
also known that PHT induces [Ca2+]i elevation in HGF. These findings suggest that PHT 
causes gingival overgrowth by interacting with these bioactive substances. The purpose of this 
study was to clarify the mechanism of [Ca2+]i elevation by PHT in HGF using live cell 
imaging with Ca2+ indicators fura-2 and to investigate the effect of PHT on the Ca2+ responses 
by inflammatory bioactive substances. The results of this study demonstrate that PHT 
enhances the weak Ca2+ response by ATP and Histamine, and this finding suggests the 
interaction of PHT and inflammatory bioactive substances may cause exacerbations of DIGE. 
 
Materials & Methods  
 HGFCell Line Servicewere cultured in Dulbecco's Modified Eagle Medium including 10% 
Fetal bovine serum. HGF were seeded on recording chambers and incubated with fura-2/AM 
(2 µM) in Hanks’ balanced salt solution buffered with HEPES (HBSS-H) for 20 min at room 
temperature. Fura-2-loaded cells were washed with HBSS-H and allowed to rest for at least 30 
min prior to the Ca2+ measurement. To monitor fura-2 fluorescence, cells were alternately 
excited at 345 and 380 nm, and emission signals were recorded at 500-530 nm using an 
inverted fluorescence microscope TE-2000 (Nikon) coupled with EM-CCD camera and 
controlled with AQUACOSMOS imaging software (Hamamatsu-photonics). These 
experiments were performed at room temperature. 
 
Results & Discussion  
 The applications of 100 µM PHT elevated [Ca2+]i in HGF. This PHT-induced [Ca2+]i 
elevation was also observed in the absence of extracellular Ca2+. PHT also enhanced Ca2+ 
elevation after the treatment with thapsigargin (ThG), an inhibitor of endoplasmic reticulum 
Ca2+pump. Since ThG is known to deplete the intracellular Ca2+ stores, the involvement of 
Ca2+ release from intracellular stores in the PHT-induced Ca2+ elevations were excluded. 
Together with these results inhibitory effects of PHT on the excretion of cytosolic Ca2+ were 
suggested. 
 To investigate the effects of PHT on Na+/Ca2+ exchanger (NCX), one of the intracellular Ca2+ 
excretion mechanisms, PHT-induced Ca2+ elevation in HGF was examined in the presence and 
absence of extracellular Na+. PHT induced [Ca2+]i elevation was strongly attenuated in the 
absence of extracellular Na+. In addition, removal of extracellular Na+ increased [Ca2+]i by the 
Ca2+ entry through the reverse mode of NCX, and this [Ca2+]i elevation was strongly 
attenuated by PHT. These results provide strong evidence for the inhibitory effect of PHT on 
NCX. 
  These results provide an assumption that the suppression of the excretion of intracellular 
Ca2+ by PHT may enhance Ca2+ response with various stimuli, and thus effects of PHT on the 
Ca2+ response by ATP and Histamine were examined. Ca2+ responses with 1 µM ATP and 10 
µM were diminished at the second application of same concentrations of ATP by the receptor 
desensitization. However, the second application of ATP was potentiated in the presence of 
PHT. In particular, cells that were unresponsive to 1 µM ATP showed clear Ca2+ responses at 
the second application in the presence of PHT. Ca2+ responses with 3 µM Histamine were also 
potentiated by PHT. These results suggest that the administration of PHT enhances the Ca2+ 
responses by weak physiological stimulations. 
 
Conclusion  
 The present study elucidated that PHT increases [Ca2+]i due to the reduction of Ca2+ 
excretion by the suppression of NCX in HGF. Due to the inhibitory effect on the Ca2+ 
excretion, PHT enhanced the Ca2+ response of HGF by low concentrations of ATP and 
Histamine. These results raise the possibility that PHT enhances Ca2+ responses by mechanical 
stimulations and inflammation. These interactions between PHT and bioactive substances may 
cause the exacerbation of DIGE. 
 


Effects of phenytoin in human gingival fibroblasts -Augmentation of PHT on the calcium responses mediated by physiologically active substances-

柳瀨, 舜佑

38398

北海道医療大学学術リポジトリ
歯周炎はアテローム性動脈硬化症の発症に影響し、
ナタマメエキスはそれを抑制する：ーアテローム性
動脈硬化症モデルマウス及びin vitroでの研究ー
著者 柳? 舜佑
学位名 博士（歯学）
学位授与機関 北海道医療大学
学位授与年度 令和2年度
学位授与番号 30110甲第349号
URL http://id.nii.ac.jp/1145/00064959/





Periodontitis affects the development of atherosclerosis, and sword bean extract suppresses it: -the study using atherosclerosis model mice and in vitro-

38412

北海道医療大学学術リポジトリ
目次
著者 北海道医療大学歯学会
雑誌名 北海道医療大学歯学雑誌
巻 40
号 1
発行年 2021-06-30
URL http://id.nii.ac.jp/1145/00064967/
北海道医療大学歯学雑誌
第40巻 第1号 令和3年6月
目 次
〔総説〕
1 Network modifiers of bioactive glasses : a review
Enrique Ezra ZUÑIGA−HEREDIA, Ryota NAGASAKI, Naohiko KAWAMURA, Masahiro IIJIMA…………（1）
〔原著〕
13 保険外併用療養の特別の料金における都道府県格差の状況：
－歯科の選定療養における金合金および白金加金について－
岡村 敏弘，山口 摂崇，川上 智史，越智 守生，永易 裕樹，芦田 眞治…………………………（13）
29 抜歯窩に埋入したハイドロキシアパタイト顆粒周囲の歯周組織再生におけるエナメルタンパクの影響
渋井 徹，高橋 昌己，矢嶋 俊彦，坂倉 康則，越智 守生，井上 寛一，入江 一元……………（29）
37 ホップ抽出物キサントフモールによる口腔扁平上皮癌由来細胞株SASのマトリックスプロテアーゼの発現変化
原田 文也，植原 治，平木 大地，森川 哲郎，杉山 のどか，江端 一馬，古市 保志，
志茂 剛，三浦 宏子，安彦 善裕，永易 裕樹……………………………………………………………（37）
45 アルカリ性電解水とナタマメ茶を用いた30秒間の洗口による歯周病原性細菌への効果
松本 崇嗣，加藤 幸紀，清水伸太郎，古市 保志…………………………………………………………（45）
〔症例報告〕
61 歯科矯正用アンカースクリューを用いて非抜歯治療で改善した叢生症例
岡山 三紀，溝口 到，飯嶋 雅弘……………………………………………………………………………（61）
〔解説〕
71 3Dプリンターを用いたインダイレクトボンディング法用トランスファートレーの考案
保田 好隆，前田 悠冴，飯嶋 雅弘…………………………………………………………………………（71）
〔歯学情報〕
77 最近のトピックス………………………………………………………………………………………………………（77）
79 北海道医療大学歯学会第39回学術大会 定例講演会・一般演題抄録……………………………………………（79）
102 会務報告 ………………………………………………………………………………………………………………（102）
108 北海道医療大学歯学会会則 …………………………………………………………………………………………（108）
110 北海道医療大学歯学雑誌 投稿規程 ………………………………………………………………………………（110）
115 編集後記 ………………………………………………………………………………………………………………（115）
】Ｓｅｒｖｅｒ／歯学雑誌／第４０巻１号　　　４Ｃ１５０　１Ｃ１３３／目次　ＯＴＦ／目次（和文）  2021.07.09 08.58.50  Page 1 


岡村, 敏弘

38418

山口, 摂崇

38419

川上, 智史

38420

越智, 守生

38421

永易, 裕樹

38422

芦田, 眞治

38423

The present state of prefectural disparities in additional fees for treatment according to the patients’ choice : －Gold alloy and platinum added gold alloy (Metal restorations of anterior tooth and metal plate complete dentures)－

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目次