Emerging role of carfilzomib in treatment of relapsed and refractory lymphoid neoplasms and multiple myeloma

被引：40

作者：

Jain, Salvia ^{[1
]}

Diefenbach, Catherine ^{[1
]}

Zain, Jasmine ^{[1
]}

O'Connor, Owen A. ^{[1
]}

机构：

[1] NYU, Langone Med Ctr, NYU Canc Inst, Div Hematol & Med Oncol, New York, NY 10003 USA

来源：

CORE EVIDENCE | 2011年 / 6卷

关键词：

carfilzomib; multiple myeloma; pharmacology; safety; efficacy;

D O I：

10.2147/CE.S13838

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Proteasome inhibition forms the cornerstone of antimyeloma therapy. The first-in-class proteasome inhibitor, bortezomib, either alone or in combination with other chemotherapeutic agents, induces high overall response rates and response qualities in patients with clinically and molecularly defined high-risk disease. However, resistance to bortezomib and neurotoxicity associated with the treatment remain challenging issues. Carfilzomib is a novel, well tolerated, irreversible proteasome inhibitor with minimal neurotoxicity. Carfilzomib demonstrates promising activity in myeloma patients who are refractory to bortezomib and immunomodulatory agents. This review focuses on the pharmacology, safety, and efficacy of carfilzomib for the treatment of multiple myeloma in bortezomib-naive and bortezomibexposed populations.

引用

页码：43 / 57

页数：15

共 78 条

[21] Phase II study of proteasome inhibitor bortezomib in relapsed or refractory B-Cell non-Hodgkin's lymphoma [J].

Goy, A ;

Younes, A ;

McLaughlin, P ;

Pro, B ;

Romaguera, JE ;

Hagemeister, F ;

Fayad, L ;

Dang, NH ;

Samaniego, F ;

Wang, M ;

Broglio, K ;

Samuels, B ;

Gilles, F ;

Sarris, AH ;

Hart, S ;

Trehu, E ;

Schenkein, D ;

Cabanillas, F ;

Rodriguez, AM .

JOURNAL OF CLINICAL ONCOLOGY, 2005, 23 (04) :667-675

[22] Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of β-lactone ring opening and a mechanism for irreversible binding [J].

Groll, M ;

Huber, R ;

Potts, BCM .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (15) :5136-5141

[23] Crystal structure of epoxomicin:20S proteasome reveals a molecular basis for selectivity of α′,β′-epoxyketone proteasome inhibitors [J].

Groll, M ;

Kim, KB ;

Kairies, N ;

Huber, R ;

Crews, CM .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2000, 122 (06) :1237-1238

[24]

Hajek R, 2008, BLOOD, V112

[25]

Jagannath S, 2009, J CLIN ONCOL, V27

[26]

JAKUBOWIAK AJ, 2009, BLOOD, V114

[27] Improved survival of patients with multiple myeloma after the introduction of novel agents and the applicability of the International Staging System (ISS): an analysis of the Greek Myeloma Study Group (GMSG) [J].

Kastritis, E. ;

Zervas, K. ;

Symeonidis, A. ;

Terpos, E. ;

Delimbassi, S. ;

Anagnostopoulos, N. ;

Michali, E. ;

Zomas, A. ;

Katodritou, E. ;

Gika, D. ;

Pouli, A. ;

Christoulas, D. ;

Roussou, M. ;

Kartasis, Z. ;

Economopoulos, T. ;

Dimopoulos, M. A. .

LEUKEMIA, 2009, 23 (06) :1152-1157

[28]

KIM Y, 2008, BLOOD, V112

[29] Pharmacokinetics, pharmacodynamics and anti-tumor efficacy of PR-171, a novel inhibitor of the 20S proteasome. [J].

Kirk, CJ ;

Bennett, MK ;

Buchholz, TJ ;

Demo, SD ;

Ho, MN ;

Jiang, J ;

Laidig, GJ ;

Lewis, ER ;

Shenk, KD ;

Smyth, MS ;

Sun, CM ;

Vallone, MK ;

Woo, TM ;

Molineaux, CJ .

BLOOD, 2005, 106 (11) :181A-181A

[30] Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate [J].

Kisselev, AF ;

Callard, A ;

Goldberg, AL .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (13) :8582-8590

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