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Article ; Online: Chemotherapy and targeted therapies: are we making progress in castrate-resistant prostate cancer?

Hoffman-Censits, Jean / Fu, Maofu

2013 Volume 40, Issue 3, Page(s) 361–374

Abstract: First-line therapy for men with metastatic or recurrent prostate cancer following definitive local therapy is medical or surgical castration. Though effective initially in most patients, the majority of tumors develop castration resistance, necessitating ...

Abstract	First-line therapy for men with metastatic or recurrent prostate cancer following definitive local therapy is medical or surgical castration. Though effective initially in most patients, the majority of tumors develop castration resistance, necessitating the addition of further therapy. The historic treatment paradigm of second-line androgen manipulation, followed by cytotoxic salvage chemotherapy, has changed in recent years with better understanding of mechanisms that lead to castration resistance. This review will outline the data supporting the use of targeted and chemotherapeutic agents for prostate cancer, review data leading to US Food and Drug Administration (FDA) approval of the newest agents abiraterone, enzalutamide, and cabazitaxel, as well as review ongoing studies of novel agents.
MeSH term(s)	Androgen Receptor Antagonists/pharmacology ; Androgen Receptor Antagonists/therapeutic use ; Androgens/biosynthesis ; Animals ; Antineoplastic Agents, Hormonal/pharmacology ; Antineoplastic Agents, Hormonal/therapeutic use ; Biosynthetic Pathways/drug effects ; Enzyme Inhibitors/pharmacology ; Enzyme Inhibitors/therapeutic use ; Humans ; Male ; Molecular Targeted Therapy ; Prostatic Neoplasms/drug therapy ; Randomized Controlled Trials as Topic
Chemical Substances	Androgen Receptor Antagonists ; Androgens ; Antineoplastic Agents, Hormonal ; Enzyme Inhibitors
Language	English
Publishing date	2013-06
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	189220-4
ISSN	1532-8708 ; 0093-7754
ISSN (online)	1532-8708
ISSN	0093-7754
DOI	10.1053/j.seminoncol.2013.04.015
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Article ; Online: Molecular Mechanism of V(D)J Recombination from Synaptic RAG1-RAG2 Complex Structures.

Ru, Heng / Chambers, Melissa G / Fu, Tian-Min / Tong, Alexander B / Liao, Maofu / Wu, Hao

Cell

2015 Volume 163, Issue 5, Page(s) 1138–1152

Abstract: Diverse repertoires of antigen-receptor genes that result from combinatorial splicing of coding segments by V(D)J recombination are hallmarks of vertebrate immunity. The (RAG1-RAG2)2 recombinase (RAG) recognizes recombination signal sequences (RSSs) ... ...

Abstract	Diverse repertoires of antigen-receptor genes that result from combinatorial splicing of coding segments by V(D)J recombination are hallmarks of vertebrate immunity. The (RAG1-RAG2)2 recombinase (RAG) recognizes recombination signal sequences (RSSs) containing a heptamer, a spacer of 12 or 23 base pairs, and a nonamer (12-RSS or 23-RSS) and introduces precise breaks at RSS-coding segment junctions. RAG forms synaptic complexes only with one 12-RSS and one 23-RSS, a dogma known as the 12/23 rule that governs the recombination fidelity. We report cryo-electron microscopy structures of synaptic RAG complexes at up to 3.4 Å resolution, which reveal a closed conformation with base flipping and base-specific recognition of RSSs. Distortion at RSS-coding segment junctions and base flipping in coding segments uncover the two-metal-ion catalytic mechanism. Induced asymmetry involving tilting of the nonamer-binding domain dimer of RAG1 upon binding of HMGB1-bent 12-RSS or 23-RSS underlies the molecular mechanism for the 12/23 rule.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cryoelectron Microscopy ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/ultrastructure ; Homeodomain Proteins/chemistry ; Homeodomain Proteins/genetics ; Homeodomain Proteins/ultrastructure ; Humans ; Mice ; Molecular Sequence Data ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/ultrastructure ; Mutation ; Sequence Alignment ; V(D)J Recombination ; Zebrafish
Chemical Substances	DNA-Binding Proteins ; Homeodomain Proteins ; Multiprotein Complexes ; V(D)J recombination activating protein 2 ; RAG-1 protein (128559-51-3)
Language	English
Publishing date	2015-11-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2015.10.055
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Article: Molecular Mechanism of V(D)J Recombination from Synaptic RAG1-RAG2 Complex Structures

Ru, Heng / MelissaÂ G. Chambers / Tian-Min Fu / AlexanderÂ B. Tong / Maofu Liao / Hao Wu

Cell. 2015 Nov. 19, v. 163

2015

Abstract	Diverse repertoires of antigen-receptor genes that result from combinatorial splicing of coding segments by V(D)J recombination are hallmarks of vertebrate immunity. The (RAG1-RAG2)2 recombinase (RAG) recognizes recombination signal sequences (RSSs) containing a heptamer, a spacer of 12 or 23 base pairs, and a nonamer (12-RSS or 23-RSS) and introduces precise breaks at RSS-coding segment junctions. RAG forms synaptic complexes only with one 12-RSS and one 23-RSS, a dogma known as the 12/23 rule that governs the recombination fidelity. We report cryo-electron microscopy structures of synaptic RAG complexes at up to 3.4Â Ã resolution, which reveal a closed conformation with base flipping and base-specific recognition of RSSs. Distortion at RSS-coding segment junctions and base flipping in coding segments uncover the two-metal-ion catalytic mechanism. Induced asymmetry involving tilting of the nonamer-binding domain dimer of RAG1 upon binding of HMGB1-bent 12-RSS or 23-RSS underlies the molecular mechanism for the 12/23 rule.
Keywords	cryo-electron microscopy ; genes ; immunity ; signal peptide ; vertebrates
Language	English
Dates of publication	2015-1119
Size	p. 1138-1152.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2015.10.055
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Article ; Online: Factor XII Structure-Function Relationships.

Shamanaev, Aleksandr / Litvak, Maxim / Ivanov, Ivan / Srivastava, Priyanka / Sun, Mao-Fu / Dickeson, S Kent / Kumar, Sunil / He, Tracey Z / Gailani, David

Seminars in thrombosis and hemostasis

2023

Abstract: Factor XII (FXII), the zymogen of the protease FXIIa, contributes to pathologic processes such as bradykinin-dependent angioedema and thrombosis through its capacity to convert the homologs prekallikrein and factor XI to the proteases plasma kallikrein ... ...

Abstract	Factor XII (FXII), the zymogen of the protease FXIIa, contributes to pathologic processes such as bradykinin-dependent angioedema and thrombosis through its capacity to convert the homologs prekallikrein and factor XI to the proteases plasma kallikrein and factor XIa. FXII activation and FXIIa activity are enhanced when the protein binds to a surface. Here, we review recent work on the structure and enzymology of FXII with an emphasis on how they relate to pathology. FXII is a homolog of pro-hepatocyte growth factor activator (pro-HGFA). We prepared a panel of FXII molecules in which individual domains were replaced with corresponding pro-HGFA domains and tested them in FXII activation and activity assays. When in fluid phase (not surface bound), FXII and prekallikrein undergo reciprocal activation. The FXII heavy chain restricts reciprocal activation, setting limits on the rate of this process. Pro-HGFA replacements for the FXII fibronectin type 2 or kringle domains markedly accelerate reciprocal activation, indicating disruption of the normal regulatory function of the heavy chain. Surface binding also enhances FXII activation and activity. This effect is lost if the FXII first epidermal growth factor (EGF1) domain is replaced with pro-HGFA EGF1. These results suggest that FXII circulates in blood in a "closed" form that is resistant to activation. Intramolecular interactions involving the fibronectin type 2 and kringle domains maintain the closed form. FXII binding to a surface through the EGF1 domain disrupts these interactions, resulting in an open conformation that facilitates FXII activation. These observations have implications for understanding FXII contributions to diseases such as hereditary angioedema and surface-triggered thrombosis, and for developing treatments for thrombo-inflammatory disorders.
Language	English
Publishing date	2023-06-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	196901-8
ISSN	1098-9064 ; 0094-6176
ISSN (online)	1098-9064
ISSN	0094-6176
DOI	10.1055/s-0043-1769509
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Zs.A 1259: Show issues

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Article: Histone acetylation/deacetylation as a regulator of cell cycle gene expression.

Wang, Chenguang / Fu, Maofu / Pestell, Richard G

Methods in molecular biology (Clifton, N.J.)

2004 Volume 241, Page(s) 207–216

MeSH term(s)	Acetylation ; Acetyltransferases/metabolism ; Biochemistry/methods ; Cell Cycle ; Cell Line ; Chromatin/metabolism ; Gene Expression Regulation ; Histone Acetyltransferases ; Histone Deacetylases/metabolism ; Histones/chemistry ; Humans ; Precipitin Tests ; Protein Structure, Tertiary
Chemical Substances	Chromatin ; Histones ; Acetyltransferases (EC 2.3.1.-) ; Histone Acetyltransferases (EC 2.3.1.48) ; Histone Deacetylases (EC 3.5.1.98)
Language	English
Publishing date	2004-01-01
Publishing country	United States
Document type	Journal Article
ISSN	1064-3745
ISSN	1064-3745
DOI	10.1385/1-59259-646-0:207
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Article: SIRT1 and endocrine signaling.

Yang, Tianle / Fu, Maofu / Pestell, Richard / Sauve, Anthony A

Trends in endocrinology and metabolism: TEM

2006 Volume 17, Issue 5, Page(s) 186–191

Abstract: Sirtuins (Sir2-related enzymes) are a recently discovered class of NAD(+)-dependent protein deacetylases that regulate gene expression in a variety of organisms by deacetylation of modified lysine residues on histones, transcription factors and other ... ...

Abstract	Sirtuins (Sir2-related enzymes) are a recently discovered class of NAD(+)-dependent protein deacetylases that regulate gene expression in a variety of organisms by deacetylation of modified lysine residues on histones, transcription factors and other proteins. Conservation of sirtuin regulation of the insulin-insulin-like growth factor I signaling pathway has been observed for Caenorhabditis elegans and mammals, indicating an ancient role for sirtuins in the modulation of organism adaptations to nutritional intake. The human sirtuin SIRT1 regulates a number of transcription factors that modulate endocrine signaling, including peroxisome proliferator-activated receptor gamma, peroxisome proliferator-activated receptor gamma coactivator 1alpha, forkhead-box transcription factors and p53.
MeSH term(s)	Adipocytes/metabolism ; Animals ; Apoptosis ; Cellular Senescence ; Endocrine Glands/physiology ; Evolution, Molecular ; Forkhead Transcription Factors/metabolism ; Glucose/metabolism ; Growth Substances/metabolism ; Humans ; Insulin/metabolism ; Insulin Secretion ; Insulin-Like Growth Factor I/metabolism ; Liver/metabolism ; PPAR gamma/metabolism ; Pancreas/metabolism ; Signal Transduction ; Sirtuin 1 ; Sirtuins/physiology ; Synteny
Chemical Substances	Forkhead Transcription Factors ; Growth Substances ; Insulin ; PPAR gamma ; Insulin-Like Growth Factor I (67763-96-6) ; SIRT1 protein, human (EC 3.5.1.-) ; Sirtuin 1 (EC 3.5.1.-) ; Sirtuins (EC 3.5.1.-) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2006-05-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1042384-9
ISSN	1879-3061 ; 1043-2760
ISSN (online)	1879-3061
ISSN	1043-2760
DOI	10.1016/j.tem.2006.04.002
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Article: Epigenetic regulation of nuclear steroid receptors.

Leader, Jennifer E / Wang, Chenguang / Fu, Maofu / Pestell, Richard G

Biochemical pharmacology

2006 Volume 72, Issue 11, Page(s) 1589–1596

Abstract: Histone modifier proteins have come to the forefront in the study of gene regulation. It is now known that histone methyltransferases, acetytransferases, kinases, ubiquitinases, deacetylases and demethylases orchestrate expression of target genes by ... ...

Abstract	Histone modifier proteins have come to the forefront in the study of gene regulation. It is now known that histone methyltransferases, acetytransferases, kinases, ubiquitinases, deacetylases and demethylases orchestrate expression of target genes by modifying both histone and non-histone proteins. The nuclear receptor (NR) superfamily govern such diverse biological processes as development, physiology and disease, including human cancer. The involvement of NR in complexes with coactivators and corepressors is necessary for regulation of target genes. This review focuses on the newly recognized interactions between the NR and histone modifying enzymes. In addition to regulating histones, the histone modifying proteins directly modify and thereby regulate NR activity. In the same manner that signaling platforms exist within the histone tails that are post-translationally processed by histone modifying proteins, cascades of post-translational modification have been identified within the NR that coordinate their activity. This review focuses on the regulation of the NR estrogen receptor (ERalpha), androgen receptor (AR) and peroxisome proliferator activated receptor-gamma (PPARgamma), given their role in tumor onset and progression.
MeSH term(s)	Epigenesis, Genetic ; Female ; Gene Expression Regulation, Neoplastic ; Histones/metabolism ; Humans ; Male ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Receptors, Steroid/genetics ; Receptors, Steroid/metabolism ; Signal Transduction
Chemical Substances	Histones ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid
Language	English
Publishing date	2006-11-30
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	208787-x
ISSN	1873-2968 ; 0006-2952
ISSN (online)	1873-2968
ISSN	0006-2952
DOI	10.1016/j.bcp.2006.05.024
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Article: Nuclear receptor modifications and endocrine cell proliferation.

Fu, Maofu / Wang, Chenguang / Zhang, Xueping / Pestell, Richard

The Journal of steroid biochemistry and molecular biology

2003 Volume 85, Issue 2-5, Page(s) 133–138

Abstract: Heritable and reversible changes in gene expression can occur without alterations in DNA sequence largely dependent upon the position of a gene within an accessible (euchromatic) chromatin environment. This position effect variegation in Drosophila and S. ...

Abstract	Heritable and reversible changes in gene expression can occur without alterations in DNA sequence largely dependent upon the position of a gene within an accessible (euchromatic) chromatin environment. This position effect variegation in Drosophila and S. pombe, and higher order chromatin structure regulation in yeast, is orchestrated by modifier genes of the Su(var) group (e.g. histone deacetylases (HDACs), protein phosphatases) and enhancer E(var) group (e.g. ATP-dependent nucleosome remodeling proteins). Higher order chromatin structure is regulated in part by covalent modification of the N-terminal histone tails of chromatin and histone tails in turn serve as platforms for recruitment of signaling modules that include non-histone proteins such as HP1 and NuRD. As the enzymes governing chromatin structure through covalent modifications of histones (acetylation, methylation, phosphorylation, ubiquitination) can also target non-histone substrates, a mechanism is in place by which epigenetic regulatory processes can affect the function of these alternate substrates. The nuclear receptor (NR) superfamily consists of conserved modular transcriptional regulators. Herein, we review the functional properties of nuclear receptors regulated by their direct acetylation including ligand-dependent activation, cellular growth and apoptosis.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cell Division/physiology ; Endocrine System/cytology ; Endocrine System/physiology ; Female ; Humans ; Male ; Receptors, Androgen/chemistry ; Receptors, Androgen/physiology ; Receptors, Cytoplasmic and Nuclear/physiology ; Receptors, Estrogen/chemistry ; Receptors, Estrogen/physiology ; Receptors, Steroid/physiology ; Sequence Alignment ; Sequence Homology, Amino Acid
Chemical Substances	Receptors, Androgen ; Receptors, Cytoplasmic and Nuclear ; Receptors, Estrogen ; Receptors, Steroid
Language	English
Publishing date	2003-05-01
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1049188-0
ISSN	1879-1220 ; 0960-0760
ISSN (online)	1879-1220
ISSN	0960-0760
DOI	10.1016/s0960-0760(03)00223-1
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Zs.A 708: Show issues

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Article: Mechanisms involved in hereditary angioedema with normal C1-inhibitor activity.

Shamanaev, Aleksandr / Dickeson, S Kent / Ivanov, Ivan / Litvak, Maxim / Sun, Mao-Fu / Kumar, Sunil / Cheng, Quifang / Srivastava, Priyanka / He, Tracey Z / Gailani, David

Frontiers in physiology

2023 Volume 14, Page(s) 1146834

Abstract: Patients with the inherited disorder hereditary angioedema (HAE) suffer from episodes of soft tissue swelling due to excessive bradykinin production. In most cases, dysregulation of the plasma kallikrein-kinin system due to deficiency of plasma C1 ... ...

Abstract	Patients with the inherited disorder hereditary angioedema (HAE) suffer from episodes of soft tissue swelling due to excessive bradykinin production. In most cases, dysregulation of the plasma kallikrein-kinin system due to deficiency of plasma C1 inhibitor is the underlying cause. However, at least 10% of HAE patients have normal plasma C1 inhibitor activity levels, indicating their syndrome is the result of other causes. Two mutations in plasma protease zymogens that appear causative for HAE with normal C1 inhibitor activity have been identified in multiple families. Both appear to alter protease activity in a gain-of-function manner. Lysine or arginine substitutions for threonine 309 in factor XII introduces a new protease cleavage site that results in formation of a truncated factor XII protein (Δ-factor XII) that accelerates kallikrein-kinin system activity. A glutamic acid substitution for lysine 311 in the fibrinolytic protein plasminogen creates a consensus binding site for lysine/arginine side chains. The plasmin form of the variant plasminogen cleaves plasma kininogens to release bradykinin directly, bypassing the kallikrein-kinin system. Here we review work on the mechanisms of action of the FXII-Lys/Arg
Language	English
Publishing date	2023-05-23
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2564217-0
ISSN	1664-042X
ISSN	1664-042X
DOI	10.3389/fphys.2023.1146834
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Article ; Online: High molecular weight kininogen interactions with the homologs prekallikrein and factor XI: importance to surface-induced coagulation.

Mohammed, Bassem M / Sun, Mao-Fu / Cheng, Qiufang / Litvak, Maxim / McCrae, Keith R / Emsley, Jonas / McCarty, Owen J T / Gailani, David

Journal of thrombosis and haemostasis : JTH

2023 Volume 22, Issue 1, Page(s) 225–237

Abstract: Background: In plasma, high molecular weight kininogen (HK) is either free or bound to prekallikrein (PK) or factor (F) XI (FXI). During contact activation, HK is thought to anchor PK and FXI to surfaces, facilitating their conversion to the proteases ... ...

Abstract	Background: In plasma, high molecular weight kininogen (HK) is either free or bound to prekallikrein (PK) or factor (F) XI (FXI). During contact activation, HK is thought to anchor PK and FXI to surfaces, facilitating their conversion to the proteases plasma kallikrein and FXIa. Mice lacking HK have normal hemostasis but are resistant to injury-induced arterial thrombosis. Objectives: To identify amino acids on the HK-D6 domain involved in PK and FXI binding and study the importance of the HK-PK and HK-FXI interactions to coagulation. Methods: Twenty-four HK variants with alanine replacements spanning residues 542-613 were tested in PK/FXI binding and activated partial thromboplastin time clotting assays. Surface-induced FXI and PK activation in plasma were studied in the presence or absence of HK. Kng1 Results: Overlapping binding sites for PK and FXI were identified in the HK-D6 domain. HK variants with defects only in FXI binding corrected the activated partial thromboplastin time of HK-deficient plasma poorly compared to a variant defective only in PK-binding. In plasma, HK deficiency appeared to have a greater deleterious effect on FXI activation than PK activation. Human HK corrected the defect in arterial thrombus formation in HK-deficient mice poorly due to a specific defect in binding to mouse FXI. Conclusion: Clinical observations indicate FXI is required for hemostasis, while HK is not. Yet, the HK-FXI interaction is required for contact activation-induced clotting in vitro and in vivo suggesting an important role in thrombosis and perhaps other FXI-related activities.
MeSH term(s)	Animals ; Humans ; Mice ; Kininogen, High-Molecular-Weight/metabolism ; Factor XI/metabolism ; Prekallikrein/metabolism ; Blood Coagulation ; Thrombosis
Chemical Substances	Kininogen, High-Molecular-Weight ; Factor XI (9013-55-2) ; Prekallikrein (9055-02-1)
Language	English
Publishing date	2023-10-09
Publishing country	England
Document type	Journal Article
ZDB-ID	2112661-6
ISSN	1538-7836 ; 1538-7933
ISSN (online)	1538-7836
ISSN	1538-7933
DOI	10.1016/j.jtha.2023.09.027
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