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Tuesday, November 8, 2016

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Wednesday, November 2, 2016

Highlighted Article: Molecular Mechanisms of Anti-cancer Activities of β-elemene: Targeting Hallmarks of Cancer



Molecular Mechanisms of Anti-cancer Activities of β-elemene: Targeting Hallmarks of Cancer


Author(s):

Shiyu Jiang, Chunhua Ling, Wei Li, Hongxin Jiang, Qiaoming Zhi and Min Jiang   Pages 1426 - 1434 (9)

Abstract:


Increasing knowledge on the hallmark characteristics of cancer and tumor pharmacology has promoted the introduction of phytochemicals, such as traditional Chinese medicine (TCM) in cancer therapy, which modulate numerous molecular targets and exert anticancer activities. β-elemene, an active and non-toxic compound isolated from the Chinese medicinal herb Rhizoma Zedoariae, has been explored as a potent anti-cancer agent against multiple cancers in extensive clinical trials and experimental research in vivo and in vitro. β-elemene exerts therapeutic potential via modulation of core hallmark capabilities of cancer by suppressing proliferative signaling, such as MAPK and PI3K/Akt/mTOR pathway, inducing cell death, up-regulating growth suppressors, deactivating invasion and metastasis and interacting replicative immortality and attenuating angiogenesis. Recent studies have significantly improved our understanding of anti-cancer activities and underlying molecular mechanisms of this Chinese medicine. This review presents these novel findings regarding the unique properties of β-elemene as an agent for cancer treatment, with an emphasis on multi-targeting biological and molecular regulation.

Keywords:

β-elemene; anti-cancer activity; hallmarks of cancer; drug resistance.

Affiliation:

Department of General Surgery, The First Affiliated Hospital of Soochow University, No. 188, Shi Zi Road, Suzhou 215006, China., Department of Oncology, The First Affiliated Hospital of Soochow University, No. 188, Shi Zi Road, Suzhou 215006, China.

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For More Information Please Visit Our Website Anti Cancer Agents in Medicinal Chemistry


Tuesday, October 25, 2016

Most Cited Article: Cytochromes P450 and Skin Cancer: Role of Local Endocrine Pathways

Cytochromes P450 and Skin Cancer: Role of Local Endocrine Pathways

Author(s):
Andrzej T. Slominski, Michal A. Zmijewski, Igor Semak, Blazej Zbytek, Alexander Pisarchik, Wei Li, Jordan Zjawiony and Robert C. TuckeyPages 77-96 (20)
Abstract:

Skin is the largest body organ forming a metabolically active barrier between external and internal environments. The metabolic barrier is composed of cytochromes P450 (CYPs) that regulate its homeostasis through activation or inactivation of biologically relevant molecules. In this review we focus our attention on local steroidogenic and secosteroidogenic systems in relation to skin cancer, e.g., prevention, attenuation of tumor progression and therapy. The local steroidogenic system is composed of locally expressed CYPs involved in local production of androgens, estrogens, gluco- and mineralo-corticosteroids from cholesterol (initiated by CYP11A1) or from steroid precursors delivered to the skin, and of their metabolism and/or inactivation. Cutaneous 7-hydroxylases (CYP7A1, CYP7B1 and CYP39) potentially can produce 7-hydroxy/oxy-steroids/sterols with modifying effects on local tumorigenesis. CYP11A1 also transforms 7-dehydrocholesterol (7DHC)→22(OH)7DHC→20,22(OH)2-7DHC→7-dehydropregnenolone, which can be further metabolized to other 5,7- steroidal dienes. These 5,7-dienal intermediates are converted by ultraviolet radiation B (UVB) into secosteroids which show pro-differentiation and anti-cancer properties. Finally, the skin is the site of activation of vitamin D3 through two alternative pathways. The classical one involves sequential hydroxylation at positions 25 and 1 to produce active 1,25(OH)2D3, which is further inactivated through hydroxylation at C24. The novel pathway is initiated by CYP11A1 with predominant production of 20(OH)D3 which is further metabolized to biologically active but non-calcemic D3-hydroxyderivatives. Classical and non-classical (novel) vitamin D analogs show pro-differentiation, anti-proliferative and anticancer properties. In addition, melatonin is metabolized by local CYPs. In conclusion cutaneously expressed CYPs have significant effects on skin physiology and pathology trough regulation of its chemical milieu.
Keywords:
CYP, melatonin, secosteroids, skin cancer, steroids, vitamin D.
Affiliation:
Department of Pathology and Laboratory Medicine, University of Tennessee Health Science Center, 930 Madison Avenue, RM525, Memphis, TN 38163.



For More Information Please Visit Our Website Anticancer Agent in Medicinal Chemistry



Wednesday, October 19, 2016

Podcast on Brain Delivery of Chemotherapeutics in Brain Cancer



Podcast Brain Delivery of Chemotherapeutics in Brain Cancer





Tuesday, October 4, 2016

New Issue ::: Anti-Cancer Agents in Medicinal Chemistry, 16 Issue 8





Anti-Cancer Agents in Medicinal Chemistry aims to cover all the latest and outstanding developments in medicinal chemistry and rational drug design for the discovery of anti-cancer agents.
Each issue contains a series of timely in-depth reviews and guest edited issues written by leaders in the field covering a range of current topics in cancer medicinal chemistry. The journal only considers high quality research papers for publication.
Anti-Cancer Agents in Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments in cancer drug discovery.

Articles from the journal Anti-Cancer Agents in Medicinal Chemistry, 16 Issue 8

For details on the articles, please visit this link :: http://bit.ly/2aYuKvJ

Thursday, June 23, 2016

Disintegrins from Snake Venoms and their Applications in Cancer Research and Therapy

Author(s):

Jessica Kele Arruda Macedo, Jay W. Fox and Mariana de Souza CastroPages 532-548 (17)

Abstract:


Integrins regulate diverse functions in cancer pathology and in tumor cell development and contribute to important processes such as cell shape, survival, proliferation, transcription, angiogenesis, migration, and invasion. A number of snake venom proteins have the ability to interact with integrins. Among these are the disintegrins, a family of small, non-enzymatic, and cysteine-rich proteins found in the venom of numerous snake families. The venom proteins may have a potential role in terms of novel therapeutic leads for cancer treatment. Disintegrin can target specific integrins and as such it is conceivable that they could interfere in important processes involved in carcinogenesis, tumor growth, invasion and migration. Herein we present a survey of studies involving the use of snake venom disintegrins for cancer detection and treatment. The aim of this review is to highlight the relationship of integrins with cancer and to present examples as to how certain disintegrins can detect and affect biological processes related to cancer. This in turn will illustrate the great potential of these molecules for cancer research. Furthermore, we also outline several new approaches being created to address problems commonly associated with the clinical application of peptide-based drugs such as instability, immunogenicity, and availability.

Keywords:

Antitumor, carcinogenesis, cell death, integrins, metastasis, snake venoms, tumor promotion.

Affiliation:

Department of Microbiology, Immunology and Cancer Biology, University of Virginia School of Medicine, USA.

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Targeting EZH2 for Cancer Therapy: Progress and Perspective

Author(s):

Chi Han Li and Yangchao ChenPages 559-570 (12)

Abstract:


Enhancer of Zeste Homolog 2 (EZH2) is the core component of the polycomb repressive complex 2 (PRC2), possessing the enzymatic activity in generating di/tri-methylated lysine 27 in histone H3. EZH2 has important roles during early development, and its dysregulation is heavily linked to oncogenesis in various tissue types. Accumulating evidences suggest a remarkable therapeutic potential by targeting EZH2 in cancer cells. The first part reviews current strategies to target EZH2 in cancers, and evaluates the available compounds and agents used to disrupt EZH2 functions. Then we provide insight to the future direction of the research on targeting EZH2 in different cancer types. We comprehensively discuss the current understandings of the 1) structure and biological activity of EZH2, 2) its role during the assembling of PRC2 and recruitment of other protein components, 3) the molecular events directing EZH2 to target genomic regions, and 4) post-translational modification at EZH2 protein. The discussion provides the basis to inspire the development of novel strategies to abolish EZH2-related effects in cancer cells.

Keywords:

Chemotherapy, DNA methylation, DZNep, EZH2, H3K27me3, LncRNA, PRC2, SET domain.

Affiliation:

School of Biomedical Sciences, Faculty of Medicine, the Chinese University of Hong Kong, Shatin, NT, Hong Kong.

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Mutations of Chromatin Structure Regulating Genes in Human Malignancies

Author(s):

Jian Chen, Franklin H. Herlong, John R. Stroehlein and Lopa MishraPages 411-437 (27)

Abstract:


Chromatin structure regulating processes mediated by the adenosine triphosphate (ATP) – dependent chromatin remodeling complex and the covalent histone-modifying complexes are critical to gene transcriptional control and normal cellular processes, including cell stemness, differentiation, and proliferation. Gene mutations, structural abnormalities, and epigenetic modifications that lead to aberrant expression of chromatin structure regulating members have been observed in most of human malignancies. Advances in next-generation sequencing (NGS) technologies in recent years have allowed in-depth study of somatic mutations in human cancer samples. The Cancer Genome Atlas (TCGA) is the largest effort to date to characterize cancer genome using NGS technology. In this review, we summarize somatic mutations of chromatin-structure regulating genes from TCGA publications and other cancer genome studies, providing an overview of genomic alterations of chromatin regulating genes in human malignancies.

Keywords:

Somatic mutation, Cancer, Chromatin structure, Chromatin remodeling, Chromatin modification, TCGA.

Affiliation:

Department of Gastroenterology, Hepatology and Nutrition, The University of Texas MD Anderson Cancer Center, Houston, Texas 77030, USA.

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The Melanocortin Receptor System: A Target for Multiple Degenerative Diseases

Author(s):

Minying Cai and Victor J. HrubyPages 488-496 (9)

Abstract:


The melanocortin receptor system consists of five closely related G-protein coupled receptors (MC1R, MC2R, MC3R, MC4R and MC5R). These receptors are involved in many of the key biological functions for multicellular animals, including human beings. The natural agonist ligands for these receptors are derived by processing of a primordial animal gene product, proopiomelanocortin (POMC). The ligand for the MC2R is ACTH (Adrenal Corticotropic Hormone), a larger processed peptide from POMC. The natural ligands for the other 4 melanocortin receptors are smaller peptides including α-melanocyte stimulating hormone (α-MSH) and related peptides from POMC (β-MSH and γ-MSH). They all contain the sequence His-Phe-Arg-Trp that is conserved throughout evolution. Thus, there has been considerable difficulty in developing highly selective ligands for the MC1R, MC3R, MC4R and MC5R. In this brief review, we discuss the various approaches that have been taken to design agonist and antagonist analogues and derivatives of the POMC peptides that are selective for the MC1R, MC3R, MC4R and MC5R receptors, via peptide, nonpeptide and peptidomimetic derivatives and analogues and their differential interactions with receptors that may help account for these selectivities.

Keywords:

Melanocortin Receptors (MCRs: MC1R, MC2R, MC3R, MC4R, MC5R); α-MSH: α -melanocyte stimulate hormone; POMC: Proopiomelanocortin; ACTH: adrenal corticotropic hormone; GPCRs: G-protein coupled receptors; ASIP: agouti signaling protein; AGRP: agouti related protein; MTI: Ac-Ser-Tyr-Ser-Met-Glu-His-DPhe-Arg-Trp-Gly-Lys-Pro-Val- NH2; MT-II: Ac-Nle4-c[Asp5, D-Phe7, Lys10]α-MSH(4-10)-NH2, (Ac-Nle-c[Asp-His-DPhe-Arg-Trp-Lys]-NH2). SHU9119: Ac- Nle4-c[Asp5, D-Nal(2’)7, Lys10]α-MSH(4-10)-NH2, (Ac-Nle-c[Asp-His- D-Nal(2’)-Arg-Trp-Lys]-NH2).

Affiliation:

Department of Chemistry & Biochemistry, University of Arizona, 1306 E. University Blvd, Tucson, AZ 85721, USA.

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