An Overview of ADAM9: Structure, Activation, and Regulation in Human Diseases

被引：74

作者：

Chou, Cheng-Wei ^{[1
,2
]}

Huang, Yu-Kai ^{[1
]}

Kuo, Ting-Ting ^{[3
]}

Liu, Jing-Pei ^{[1
]}

Sher, Yuh-Pyng ^{[1
,3
,4
]}

机构：

[1] China Med Univ, Grad Inst Biomed Sci, Taichung 404, Taiwan

[2] Taichung Vet Gen Hosp, Div Hematol Med Oncol, Dept Med, Taichung 407, Taiwan

[3] China Med Univ Hosp, Ctr Mol Med, Taichung 404, Taiwan

[4] China Med Univ, Chinese Med Res Ctr, Taichung 404, Taiwan

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2020年 / 21卷 / 20期

关键词：

ADAM9; biological function; inflammation; cancer; HEPATOCELLULAR-CARCINOMA; PANCREATIC-CANCER; LUNG-CANCER; CELL-PROLIFERATION; TARGETING ADAM9; METALLOPROTEASE-DISINTEGRIN; CRYSTAL-STRUCTURES; ENDOTHELIAL-CELL; TUMOR-CELLS; EXPRESSION;

D O I：

10.3390/ijms21207790

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

ADAM9 (A disintegrin and a metalloprotease 9) is a membrane-anchored protein that participates in a variety of physiological functions, primarily through the disintegrin domain for adhesion and the metalloprotease domain for ectodomain shedding of a wide variety of cell surface proteins. ADAM9 influences the developmental process, inflammation, and degenerative diseases. Recently, increasing evidence has shown that ADAM9 plays an important role in tumor biology. Overexpression of ADAM9 has been found in several cancer types and is correlated with tumor aggressiveness and poor prognosis. In addition, through either proteolytic or non-proteolytic pathways, ADAM9 promotes tumor progression, therapeutic resistance, and metastasis of cancers. Therefore, comprehensively understanding the mechanism of ADAM9 is crucial for the development of therapeutic anti-cancer strategies. In this review, we summarize the current understanding of ADAM9 in biological function, pathophysiological diseases, and various cancers. Recent advances in therapeutic strategies using ADAM9-related pathways are presented as well.

引用

页码：1 / 22

页数：22

共 127 条

[1] Stromal Fibroblast-Specific Expression of ADAM-9 Modulates Proliferation and Apoptosis in Melanoma Cells In Vitro and In Vivo [J].

Abety, Anna N. ;

Fox, Jay W. ;

Schoenefuss, Alexander ;

Zamek, Jan ;

Landsberg, Jenny ;

Krieg, Thomas ;

Blobel, Carl ;

Mauch, Cornelia ;

Zigrino, Paola .

JOURNAL OF INVESTIGATIVE DERMATOLOGY, 2012, 132 (10) :2451-2458

[2] ADAM9 disintegrin domain activates human neutrophils through an autocrine circuit involving integrins and CXCR2 [J].

Amendola, Rafael S. ;

Martin, Ana Carolina B. M. ;

Selistre-de-Araujo, Heloisa S. ;

Paula-Neto, Heitor A. ;

Saldanha-Gama, Roberta ;

Barja-Fidalgo, Christina .

JOURNAL OF LEUKOCYTE BIOLOGY, 2015, 97 (05) :951-962

[3] Leukotriene receptor antagonists enhance HCC treatment efficacy by inhibiting ADAMs and suppressing MICA shedding [J].

Arai, Jun ;

Goto, Kaku ;

Otoyama, Yumi ;

Nakajima, Yoko ;

Sugiura, Ikuya ;

Kajiwara, Atsushi ;

Tojo, Masayuki ;

Ichikawa, Yuki ;

Uozumi, Shojiro ;

Shimozuma, Yuu ;

Uchikoshi, Manabu ;

Sakaki, Masashi ;

Nozawa, Hisako ;

Nakagawa, Ryo ;

Muroyama, Ryosuke ;

Kato, Naoya ;

Yoshida, Hitoshi .

CANCER IMMUNOLOGY IMMUNOTHERAPY, 2021, 70 (01) :203-213

[4] Predominance of regorafenib over sorafenib: Restoration of membrane-bound MICA in hepatocellular carcinoma cells [J].

Arai, Jun ;

Goto, Kaku ;

Stephanou, Anthony ;

Tanoue, Yasushi ;

Ito, Sayaka ;

Muroyama, Ryosuke ;

Matsubara, Yasuo ;

Nakagawa, Ryo ;

Morimoto, Sayuri ;

Kaise, Yoshimi ;

Lim, Lay Ahyoung ;

Yoshida, Hitoshi ;

Kato, Naoya .

JOURNAL OF GASTROENTEROLOGY AND HEPATOLOGY, 2018, 33 (05) :1075-1081

[5] Putative function of ADAM9, ADAM10, and ADAM17 as APP α-secretase [J].

Asai, M ;

Hattori, C ;

Szabó, B ;

Sasagawa, N ;

Maruyama, K ;

Tanuma, S ;

Ishiura, S .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 301 (01) :231-235

[6] Identification of the Cell-Surface Protease ADAM9 as an Entry Factor for Encephalomyocarditis Virus [J].

Baggen, Jim ;

Thibaut, Hendrik Jan ;

Hurdiss, Daniel L. ;

Wahedi, Maryam ;

Marceau, Caleb D. ;

van Vliet, Arno L. W. ;

Carette, Jan E. ;

van Kuppeveld, Frank J. M. .

MBIO, 2019, 10 (04)

[7] A Disintegrin and Metalloproteinase 9 Domain (ADAM9) Is a Major Susceptibility Factor in the Early Stages of Encephalomyocarditis Virus Infection [J].

Bazzone, Lindsey E. ;

King, Michael ;

MacKay, Christopher R. ;

Kyawe, Pyae P. ;

Meraner, Paul ;

Lindstrom, Daniel ;

Rojas-Quintero, Joselyn ;

Owen, Caroline A. ;

Wang, Jennifer P. ;

Brass, Abraham L. ;

Kurt-Jones, Evelyn A. ;

Finberg, Robert W. .

MBIO, 2019, 10 (01)

[8] An Overview of the Derivation and Function of Multinucleated Giant Cells and Their Role in Pathologic Processes [J].

Brooks, Patricia J. ;

Glogauer, Michael ;

McCulloch, Christopher A. .

AMERICAN JOURNAL OF PATHOLOGY, 2019, 189 (06) :1145-1158

[9] Active-site determinants of substrate recognition by the metalloproteinases TACE and ADAM10 [J].

Caescu, Cristina I. ;

Jeschke, Grace R. ;

Turk, Benjamin E. .

BIOCHEMICAL JOURNAL, 2009, 424 :79-88

[10] Quercetin suppresses the metastatic ability of lung cancer through inhibiting Snail-dependent Akt activation and Snail-independent ADAM9 expression pathways [J].

Chang, Jer-Hwa ;

Lai, Shu-Leung ;

Chen, Wan-Shen ;

Hung, Wen-Yueh ;

Chow, Jyh-Ming ;

Hsiao, Michael ;

Lee, Wei-Jiunn ;

Chien, Ming-Hsien .

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2017, 1864 (10) :1746-1758

← 1 2 3 4 5 6 7 8 9 10 →