
Pathophysiological Aspects of Proteases in Cancer
- 1st Edition - October 22, 2024
- Imprint: Academic Press
- Editors: Sajal Chakraborti, Srijit Das, Cheorl-Ho Kim
- Language: English
- Paperback ISBN:9 7 8 - 0 - 4 4 3 - 3 0 0 9 8 - 1
- eBook ISBN:9 7 8 - 0 - 4 4 3 - 3 0 0 9 9 - 8
Pathophysiological Aspects of Proteases in Cancer provides a comprehensive overview of the multifaceted field of proteases in the cellular environment and focuses on the recent… Read more

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Request a sales quotePathophysiological Aspects of Proteases in Cancer provides a comprehensive overview of the multifaceted field of proteases in the cellular environment and focuses on the recently elucidated functions of complex proteolytic systems in physiology and pathophysiology. The book both gives insights on the general aspects of the role of proteases in cancer, their role as diagnostics and prognostics biomarkers, their impact on chemoresistance, and the future cutting-edge technologies like cocktail therapies and Cyber Knife technology. Given the breadth and depth of information covered in the respective contributions, the book will be immensely useful for researchers in oncology and working to identify targets for drug development.
Multidisciplinary in scope, the book bridges the gap between fundamental and translational research, with applications in the biomedical and pharmaceutical industry, making it a thought-provoking read for basic and applied scientists engaged in biomedical research.
Multidisciplinary in scope, the book bridges the gap between fundamental and translational research, with applications in the biomedical and pharmaceutical industry, making it a thought-provoking read for basic and applied scientists engaged in biomedical research.
- Gives insight into the spectrum of proteases, protease inhibitors, and protease interactors involved at the cellular and molecular level in cancer development
- Gives a comprehensive overview of the role of proteases in modulating cellular metabolism and chemoresistance to better understand how proteases play in early to the end point in cancer development and metastasis
- Provides a multidisciplinary approach demonstrating the biochemical and signal transduction mechanisms associated with dysregulation of proteases, leading to the manifestation of various diseases
- Highlights the roles and regulation of different types of proteases, as well as their synthetic and endogenous inhibitors
- Bridges the gap between fundamental and translational research, with applications in the biomedical and pharmaceutical industry
Researchers/scholars working in cancer biology
- Title of Book
- Cover image
- Title page
- Table of Contents
- Copyright
- Dedication
- Contributors
- Preface
- Section I. General aspects
- Chapter 1. Pathophysiological aspects of calpains in cancer
- 1 Introduction
- 2 Colorectal cancer
- 3 Renal cell carcinoma
- 4 Hepatocellular carcinoma
- 5 Gastric cancer
- 5.1 Inflammatory bowel disease
- 6 Breast cancer
- 7 B cell chronic lymphocytic leukemia
- 8 Oral squamous cell carcinoma
- 9 Pancreatic cancer
- 10 Calpain-6 and cancer and stem cells
- 11 Cervical cancer and calpain
- 12 Nasopharyngeal carcinoma
- 13 Glioblastoma multiforme
- 14 Osteosarcoma
- 15 Castration-resistant prostate cancer
- 16 Therapeutic intervention and calpain inhibition
- 17 Conclusion and future direction
- Chapter 2. Mitochondrial proteases in cancer development and progression
- 1 Introduction
- 2 A short overview of mitochondrial proteases
- 3 Mitochondrial protease in human diseases
- 4 Mitochondrial proteases and cancer prevalence
- 5 Mitochondrial proteases and cancer development
- 6 Mitochondrial proteases and cancer progression
- 7 Mitochondrial proteases and cancer metastasis
- 8 Mitochondrial proteases and cancer stem cells
- 9 The emerging role of mitochondrial protease in cancer therapy
- 10 Chemical modulators of mitochondrial proteases in cancer therapy
- 11 Conclusion and future perspectives
- Chapter 3. Proteases in head and neck cancer
- 1 Introduction
- 2 Metalloproteases
- 3 Serine proteases
- 4 Cysteine proteases
- 5 Aspartic proteases
- 6 Threonine proteases
- 7 Biomarker value of for different types of cancer
- 8 Biological fluids as source of proteases biomarkers
- 8.1 Serum
- 8.2 Saliva
- 8.3 Urine
- 9 Conclusions
- Chapter 4. Matrix metalloproteinases and uveal melanoma
- 1 Introduction
- 2 Molecular basis of UM
- 3 Cytogenetic and molecular alterations in UM
- 3.1 Oncogenic mutations in UM
- 4 Role of extracellular matrix in cancer progression
- 4.1 Matrix metalloproteinases and tissue inhibitors of matrix metalloproteinases and their role in physiology and pathology
- 4.2 Altered MMP/TIMP interaction and dysregulated ECM homeostasis in UM
- 5 Conclusions and future directions
- Chapter 5. Proteases in DNA damage, repair, and radioresistance: Cellular and molecular aspects
- 1 Introduction
- 2 Role of proteases in DNA damage, response, and repair
- 2.1 Protein cross-link proteases (DPC proteases)
- 2.1.1 Wss1 protease
- 2.1.2 SPRTN (Spartan)
- 2.1.3 CTLA-4
- 2.1.4 DVC1 (DNA damage protein targeting VCP)
- 2.1.5 ADAM 10
- 2.2 Aspartic proteases
- 2.2.1 DDI1
- 2.2.2 DNA damage-inducible 2
- 2.3 Proteasome
- 2.4 Ubiquitin-specific proteases
- 2.4.1 USP7
- 2.4.2 USP11
- 2.5 SUMO proteases
- 2.6 Calpains
- 2.7 Caspases
- 2.8 Metalloprotease FAN1
- 2.9 Caspase-activated DNase
- 2.10 FtsH protease
- 3 Proteases in radioresistance
- 3.1 USP 14
- 3.2 ClpPX protease
- 3.3 Lon protease
- 4 Conclusion and future perspective
- Chapter 6. Radiotherapy, proteases and gastric cancer: A complex interplay
- 1 Introduction
- 2 Gastric cancer
- 2.1 Stomach architecture and function
- 3 Proteases and its classification
- 4 Role of proteases from Helicobacter pylori in GC development
- 5 Role of host proteases in inflammatory response, cancer cell invasion, and metastasis
- 5.1 Role of serine proteases in GC
- 5.2 Role of MMPs in GC
- 5.3 Role of cysteine proteases in GC
- 6 Radiotherapy as a potential treatment modality of GC
- 7 Interplay of proteases and radiation therapy
- 8 Proteases as therapeutic targets in GC
- 9 Conclusion and future directions
- Chapter 7. Matrix metalloproteases in the pathogenesis of hepatocarcinoma
- 1 Introduction
- 2 MMPs and biomarkers in liver cancer
- 2.1 Mechanistic expression of MMP-9
- 3 Therapeutic MMP inhibitors in human diseases
- 4 Conclusion in human diseases
- Conflict of interest
- Publisher's note
- Chapter 8. Exploring synthetic and natural compounds for cathepsin B: Mechanisms and therapy
- 1 Introduction
- 2 Metastasis of breast cancer
- 2.1 Cathepsin B mediates breast cancer development and progression
- 2.2 Regulation of cathepsin B in breast cancer
- 3 CatB in the delivery of breast cancer therapeutics
- 4 Potential of cathepsin B inhibitors for breast cancer treatment
- 4.1 Natural CatB inhibitors against breast cancer
- 4.2 Synthetic inhibitors of cathepsin B for breast cancer
- 5 Conclusion
- Chapter 9. Kallikrein-related peptidase 3 (KLK3) as valuable biomarkers for prostate cancer
- 1 Prostate cancer
- 2 Diagnosis of prostate cancer
- 3 Kallikreins as important serum biomarkers
- 4 Clinical trials and case control studies
- 5 Conclusion
- Chapter 10. Ubiquitin specific protease 3,7 in bone cancer and squamous cell carcinoma
- 1 Introduction
- 2 Ubiquitin
- 3 Ubiquitination
- 4 Ubiquitin-specific proteases
- 4.1 Ubiquitin-specific protease 7
- 4.2 Ubiquitin-specific protease 3
- 5 USP role in osteoblastoma
- 6 USPs and pediatric primary bone tumors
- 7 Ewing's sarcoma
- 8 USP3 in esophageal squamous carcinoma
- 8.1 Ubiquitination modifications in oral squamous cell carcinoma
- 9 Conclusion
- Chapter 11. Serine protease: Structure, classification, mechanism and role in breast cancer
- 1 Introduction
- 2 Serine proteases—structure and classification
- 3 Mechanism of action
- 4 Physiological function of serine proteases
- 4.1 Digestion
- 4.2 Immune response
- 4.3 Blood coagulation
- 4.4 Reproduction
- 4.5 Protein degradation and signaling
- 5 Serine proteases as diagnostic and prognostic markers in breast cancer
- 6 Conclusion and future perspectives
- Section II. Proteases as diagnostics and prognostics biomarkers
- Chapter 12. Protease activator receptor-1 and matrix metalloproteinase-1 as prognostic factors and a novel therapeutic targets for gastric cancer
- 1 Introduction
- 2 Gastric cancer: Pathogenesis and clinical relevance
- 2.1 Gastric cancer: An overview of etiology and molecular mechanisms
- 2.2 Emerging biomarkers in gastric cancer diagnosis and treatment
- 2.2.1 HER2 amplification
- 2.2.2 PD-L1 expression
- 2.2.3 Microsatellite instability
- 3 Protease activator receptor 1 in gastric cancer
- 3.1 Structure and function of protease activator receptor 1
- 3.2 PAR-1 signaling pathways and their role in tumorigenesis
- 3.3 PAR-1 expression patterns in gastric cancer
- 4 Matrix metalloproteinase 1 and gastric cancer
- 4.1 Unraveling the role of matrix metalloproteinases in cancer invasion
- 5 Prognostic and predictive significance of PAR-1 and MMP1 in gastric cancer
- 6 Targeting PAR-1 and MMP1 for gastric cancer therapy
- 7 Future directions and challenges
- 8 Conclusion and future perspectives
- Chapter 13. Matrix metalloproteases as diagnostic and prognostic biomarkers in cancer
- 1 Introduction
- 1.1 Structure of MMP
- 1.2 Types of MMPs and their functions
- 1.3 Physiological functions of MMPs
- 2 Natural inhibitors of MMPs
- 3 Involvements of MMPs in cancer progression
- 3.1 Matrix remodeling and cell invasion
- 3.2 Angiogenesis
- 3.3 Apoptosis
- 4 MMPs as prognostic and diagnostic biomarkers in cancer
- 4.1 Breast cancer
- 4.2 Colorectal cancer
- 4.3 Lung cancer
- 4.4 Gastrointestinal cancers
- 4.5 Ovarian cancer
- 4.6 Pancreatic ductal adenocarcinoma
- 4.7 Skin cancer (melanoma)
- 4.8 Prostate cancer
- 4.9 Glioblastoma (brain cancer)
- 4.10 Liver cancer
- 4.11 Osteosarcoma
- 4.12 Urinary bladder cancer
- 5 Conclusions and future perspectives
- Chapter 14. From enzyme to predictors: Serine proteases in cancer diagnosis and prognosis
- 1 Introduction
- 2 Serine protease and cancer
- 2.1 Extracellular matrix remodeling and tumor invasion
- 2.2 Angiogenesis and metastasis
- 2.3 Manipulation of signaling pathways
- 3 Serine protease inhibitor
- 3.1 Role of serine protease inhibitors
- 4 Serine proteases as diagnostic biomarkers
- 4.1 Using NIR probes for cancer-associated proteases detection as diagnostic biomarkers
- 4.2 ANX A2 as a serine protease in cancer invasion and metastasis as a diagnostic biomarker
- 4.3 Salivary serine proteases as biomarkers for oral squamous cell carcinoma diagnosis
- 5 Serine proteases as prognostic biomarkers
- 5.1 As a prostate cancer prognosis biomarker
- 5.2 SPINK1 as a serine protease inhibitor and its role in lung adenocarcinoma progression
- 5.3 Pericellular proteolysis and cancer progression: Roles of PAR-2 and serine proteases
- 5.4 Role of serine proteases and inhibitors in colorectal cancer: Implications for tumor suppression and malignant progression
- 5.5 Expression of matriptase and its inhibitor HAI-1 in epithelial ovarian cancer
- 5.6 Maspin (SERPINB5) in lung adenocarcinoma: A prognostic biomarker and therapeutic target
- 6 Serine proteases in therapeutics
- 7 Conclusion
- Chapter 15. Cathepsins as diagnostic and prognostic markers in oral cancer
- 1 Introduction
- 2 Proteases and cathepsins
- 3 Cathepsins in cancer
- 4 Cathepsins in the progression and prognosis of oral cancer
- 4.1 Cathepsin B
- 4.2 Cathepsin D
- 4.3 Cathepsin L
- 4.4 Cathepsin S
- 4.5 Cathepsin K
- 4.6 Cathepsin C and H
- 5 Functions of cathepsins in the treatment of oral cancer
- 6 Conclusion
- Chapter 16. Role of kallikreins in prostate cancer
- 1 Introduction
- 2 KLK14
- 3 KLK2/KLK3/KLK4
- 3.1 KLK2
- 3.2 KLK3
- 3.3 KLK4
- 4 Other KLK-related peptidases
- 4.1 KLK1
- 4.2 KLK5 and KLK7
- 4.3 KLK6
- 4.4 KLK11, KLK12, KLK14, KLK15
- 5 Targeting KLK-related peptidases: A broad range of drugs
- 6 KLKs targeted agents in prostate cancer
- 6.1 KLK-engineered inhibitors
- 6.1.1 MDKP67b
- 6.1.2 Sunflower trypsin inhibitor (SFT-1)
- 6.1.3 KLK2 heptapeptide substrate (Acetyl-Gly-LysAla-Phe-Arg-Arg)
- 6.1.4 L-377,202
- 6.1.5 KLK3-activated TGX-D1
- 6.1.6 KLK3-activated LY294002
- 6.1.7 BSD352
- 6.1.8 PRX302
- 6.2 KLK-targeted miRNAs and siRNAs-/shRNAs
- 6.2.1 miR-143
- 6.2.2 Anti-KLK4 siRNAs/shRNAs
- 6.3 Vaccines and antibodies
- 6.3.1 PROSTVAC
- 7 Conclusion and future direction
- Chapter 17. Mechanistic aspects of serine protease as biomarkers in wound healing of lung cancer
- 1 Introduction
- 2 Classification
- 3 Mechanism of action of serine protease
- 4 Conclusion
- Chapter 18. The role of acetylcholinesterase in cancer development and possible therapeutic applications
- 1 Introduction
- 2 AChE structure and function
- 2.1 AChE isoforms
- 3 AChE in apoptosis
- 4 AChE in oxidative stress and inflammation
- 5 AChE in lung cancer
- 6 AChE in prostate cancer
- 7 AChE in leukemia
- 8 AChE in breast and ovarian cancer
- 9 AChE in gastric and hepatocellular cancer
- 10 AChE in brain tumor
- 11 Modulators of AChE activity as a therapeutics in cancer treatment
- 11.1 Inhibitors of AChE activity as a therapeutics in cancer treatment
- 11.2 Enhancers of AChE activity as a therapeutics in cancer treatment
- 12 Future perspective and conclusion
- Chapter 19. Therapeutics of animal-derived compounds in proteases-induced cancer
- 1 Introduction
- 2 Use of venom-derived compounds in medicine
- 3 Protease inhibitors from rare toxic marine species
- 3.1 Empirical studies and findings on the use of protease inhibitors from marine toxins in cancer therapy
- 4 Protease inhibitors from rare terrestrial venomous animals
- 4.1 Empirical studies and findings on protease inhibitors from terrestrial toxins in cancer therapy
- 5 Comparative analysis of protease inhibitors from toxic terrestrial and marine animals
- 6 The role of venom-based protease inhibitors in cancer research
- 7 Challenges and perspectives in the research of protease inhibitors from toxins
- 8 Conclusion
- Chapter 20. Molecular warriors: Proteases as sentinels in the war against cancer diagnosis and prognosis
- 1 Introduction
- 2 Proteases in cancer
- 2.1 What are proteases?
- 2.2 Proteases as prognostic markers
- 2.2.1 Matrix metalloproteases
- 2.2.2 Urokinase plasminogen activator
- 2.2.3 Cathepsins
- 2.3 Proteases as diagnostic markers
- 2.3.1 Diagnostic techniques using matrix metalloproteases
- 2.3.2 Diagnostic techniques using cathepsins
- 2.3.3 Diagnostic techniques for urokinase plasminogen activator
- 3 Conclusion
- Section III. Proteases, chemoresistance and cancer
- Chapter 21. Serine proteases and their contribution to chemoresistance in cancer
- 1 Introduction
- 2 Overview of serine proteases
- 2.1 Serine proteases
- 2.2 Types and classification of serine proteases
- 3 Mechanism of serine proteases in cancer
- 3.1 Influencing hallmarks of cancer
- 3.1.1 Sustaining proliferative signaling
- 3.1.2 Resisting cell death
- 3.1.3 Angiogenesis
- 3.1.4 Epithelial-to-mesenchymal cell transitions
- 3.2 Activation of signaling pathways
- 3.3 Remodeling of the tumor microenvironment
- 3.4 Interaction with specific chemotherapy agents
- 3.5 Modulation of drug efflux pumps
- 4 Cancers associated with over-expressed serine proteases
- 5 Conclusion
- 6 Future aspect
- Chapter 22. Cathepsins, chemoresistance, and cancer
- 1 Introduction
- 1.1 Cathepsin A
- 1.2 Cathepsin B
- 1.3 Cathepsin C
- 1.4 Cathepsin D
- 1.5 Cathepsin E
- 1.6 Cathepsin F
- 1.7 Cathepsin G
- 1.8 Cathepsin H
- 1.9 Cathepsin K
- 1.10 Cathepsin L, S, and O
- 1.11 Cathepsin V
- 1.12 Cathepsin W
- 1.13 Cathepsin X
- 2 Structure and function of cathepsins
- 2.1 Structure of cathepsin
- 2.2 Catalytic mechanism and function of cathepsin
- 2.2.1 Aspartic protease
- 2.2.2 Serine protease
- 2.2.3 Cysteine protease
- 3 Cellular and physiological role of cathepsin
- 4 Regulation of cathepsin activity
- 4.1 Endogenous inhibitors of cathepsins
- 4.1.1 Stefins
- 4.1.2 Cystatins
- 4.1.3 Kinins
- 4.1.4 Thyropins
- 4.1.5 Other inhibitors
- 4.2 Other regulators of cathepsin
- 4.3 Posttranslational modifications of cathepsins
- 4.4 Cathepsins in disease
- 4.4.1 Role of cathepsin in cancer
- 5 Therapeutic potential of cathepsins
- 5.1 Inhibitors of cathepsin activity as potential therapeutics in cancer
- 5.2 Cathepsin-targeted drug delivery in cancer
- 6 Conclusion and future perspectives
- Chapter 23. Matrix metalloproteinases, chemoresistance and cancer
- 1 Introduction
- 1.1 Occurrence of resistance to chemotherapy in cancers
- 1.2 Enhanced efflux of drugs
- 1.3 Genetic mutations and epigenetic alterations
- 1.4 Enhanced DNA repair capacity
- 1.5 Evasion of programmed cell death
- 1.6 Cancer stem cells and epithelial-mesenchymal transition
- 2 Matrix metalloproteinases
- 2.1 Matrix metalloproteinase-1
- 2.2 Matrix metalloproteinase-2
- 2.3 Matrix metalloproteinase-3
- 2.4 Matrix metalloproteinase-7
- 2.5 Matrix metalloproteinase-9
- 2.6 Matrix metalloproteinase-14
- 2.7 Other MMPs with possible involvement in cancer chemotherapy resistance
- 3 Conclusion and future perspectives
- Chapter 24. MMPs (-2 and -9)-mediated drug resistance and their reversal in gynecological cancer
- 1 Introduction
- 2 MMPs in gynecological cancers
- 2.1 MMP-2 and MMP-9 as targets of GyCs
- 2.2 MMP-2 and MMP-9 in chemoresistance of GyCs
- 3 Strategies to reverse chemoresistance
- 4 Future direction
- 5 Conclusion
- Chapter 25. The link between trypsinogen and chymotrypsinogen in gastrointestinal cancer
- 1 Introduction
- 2 Proteases and chemoresistance
- 3 Trypsinogen and chymotrypsinogen in GI cancer
- 3.1 Trypsinogen
- 3.2 Molecular genesis
- 3.2.1 Primary structure
- 3.2.2 Catalytic triad and activation sites
- 3.2.3 Synthesis and folding
- 3.2.4 Inhibition mechanisms
- 3.2.5 Transport, release and activation cascade
- 4 Catalytic proficiency of trypsinogen
- 5 Clinical implications
- 5.1 Pancreatitis: A consequence of dysregulation
- 5.2 Trypsinogen dysfunction in pancreatic disorders
- 5.3 Diagnostic biomarker in gastrointestinal cancers
- 6 Therapeutic targets
- 6.1 Chymotrypsinogen
- 6.1.1 Structure of chymotrypsinogen
- 6.1.2 Activation of chymotrypsinogen
- 6.1.3 Function and regulation of chymotrypsin activity
- 6.1.4 Physiological significance
- 6.1.5 Clinical implications
- 6.1.6 In-depth exploration of chymotrypsinogen
- 7 Role of chymotrypsinogen in GI cancers
- 8 Conclusion
- Chapter 26. Role of proteasome in the development of chemoresistance in multiple myeloma
- 1 Introduction
- 2 Proteasome
- 2.1 Structure of proteasome
- 2.2 Functions of proteasome
- 2.2.1 Protein recycling, degradation, and regulation
- 2.2.2 Cell cycle control
- 2.2.3 Antigen processing and immune response
- 2.2.4 Regulation of transcription factors
- 2.3 The action of the mechanism of proteasome in normal cells
- 2.3.1 NF-κB signaling pathway
- 2.3.2 Ubiquitin-proteasome pathway
- 3 Proteasome and multiple myeloma
- 4 Chemoresistance nature of MM
- 4.1 Pathophysiology involved in the chemoresistance nature of MM cells
- 5 The action of proteasome inhibitors on MM
- 5.1 Combinational therapies used in the treatment of MM
- 5.2 Biomarkers used in the identification of MM
- 5.3 Recent advancements undertaken for the treatment of MM
- 6 Conclusion and future directions
- Chapter 27. Role of cysteine cathepsin and matrix metalloproteinases in progression and chemoresistance in ovarian and breast cancer
- 1 Introduction
- 2 Role of cysteine cathepsin and MMPs in breast and ovarian cancer progression
- 2.1 Cysteine
- 2.1.1 Cysteine cathepsins in breast cancer progression
- 2.1.2 Cysteine cathepsins in ovarian cancer progression
- 2.2 Role of MMPs in breast and ovarian cancer progression
- 3 Cysteine cathepsins and MMPs in drug resistance
- 3.1 Overview of role of cysteine cathepsins in drug resistance
- 3.2 MMPs in drug resistance
- 4 Targeting cysteine cathepsins and MMPs in regulation of chemoresistance and apoptosis in cancer
- 4.1 Overview of cysteine cathepsin–mediated regulation of programmed cell death and drug resistance in cancer
- 4.2 Targeting MMPs in regulation of chemoresistance and apoptosis in cancer
- 5 Conclusion
- Chapter 28. Proteases, chemoresistance, and cancer
- 1 Introduction
- 2 Proteases
- 2.1 Cysteine protease
- 2.2 Serine protease
- 2.3 Matrix metalloproteinases
- 3 Chemoresistance
- 3.1 Overactivity of efflux pump
- 3.2 Inactivation of drug
- 3.3 DNA repair mechanism
- 3.4 Apoptosis
- 3.5 Cell signaling pathways
- 3.6 Tumor microenvironment
- 3.7 Multiple drug resistance
- 4 Conclusion and future perspectives
- Chapter 29. Breaking barriers: Proteases as key players in cancer chemoresistance
- 1 Introduction
- 1.1 Cysteine proteases
- 1.2 Serine proteases
- 1.2.1 Kallikerins
- 1.2.2 Trypsin
- 1.3 Aspartate proteases
- 1.4 Threonine proteases
- 1.5 Matrix metalloproteases
- 2 Role of proteases in various types of cancer
- 2.1 Serine proteases
- 2.1.1 HtrA1
- 2.1.2 HtrA2
- 2.1.3 HtrA3
- 2.1.4 HtrA4
- 2.1.5 Trypsin role in ovarian cancer
- 2.2 Cysteine protease
- 2.2.1 Cathepsin B role in breast cancer
- 2.2.2 Cathepsin L role in pancreatic cancer
- 2.3 Aspartate protease
- 2.3.1 Cathepsin D role in breast cancer and ovarian cancer
- 2.3.2 Cathepsin E
- 3 Chemoresistance
- 3.1 Types of chemoresistance
- 3.2 Intrinsic chemoresistance
- 3.2.1 BRCA mutations in breast and ovarian cancers
- 3.2.2 P-glycoprotein overexpression
- 3.2.3 TP53 mutations
- 3.2.4 Increased DNA repair capacity
- 3.2.5 Activation of antiapoptotic pathways
- 3.2.6 Altered drug metabolism
- 3.2.7 Microenvironment-mediated resistance
- 3.3 Inherent genetic mutations in tumors
- 3.4 Heterogeneity of tumor cell population
- 3.5 Pharmacological factors
- 4 Mechanism of chemoresistance in cancer
- 4.1 Drug influx–efflux
- 4.2 Epithelial–mesenchymal transition
- 4.3 Drug activation and inactivation
- 4.4 Alteration of drug targets
- 4.5 Enhanced DNA repair and impaired apoptosis
- 5 Techniques for preventing chemoresistance in cancer
- 5.1 Early diagnosis of cancer
- 5.2 Combination therapy
- 5.3 Enhancing the drug effectiveness
- 5.4 Early diagnosis of chemoresistance
- 5.5 Targeting cancer stem cells
- 6 Conclusion
- Section IV. Other aspects
- Chapter 30. Matrix metalloproteases–targeting low-molecular-weight compounds
- 1 Current human MMP therapeutics under clinical trials
- 2 Light molecular weight MMP inhibitors are especially candidates for ischemic stroke disorders
- 2.1 Ilomastat (GM6001)
- 2.2 JNJ0966
- 2.3 SB-3CT
- 2.4 Minocycline
- 2.5 GI254023X (GI4023, SRI028594)
- 2.6 Actinonin
- 2.7 NSC 405020
- 2.8 CL-82198
- 2.9 CTS-1027
- 2.10 T-26c
- 2.11 Histatin 5 TFA
- 2.12 (S,S)-TAPI-1
- 2.13 TAPI-0
- 2.14 ONO-4817
- 2.15 Quinazoline otaplimastat
- 2.16 PF-00356231
- 2.17 A dual tubulin and MMP inhibitor
- 2.18 MMP13-IN-5
- 2.19 MMP-2/-9-IN-1
- 2.20 ARP101
- 2.21 Marimastat
- 2.22 Cyclo(RLsKDK)
- 2.23 MMP-9-IN-6
- 2.24 N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid MMP-3 inhibitor
- 2.25 Inotilone
- 2.26 MMP13-IN-4
- 2.27 INCB3619
- 3 Conclusion and emerged MMP-9 inhibitor
- Chapter 31. Evidence from clinical trials on synthetic protease inhibitors in oral, head, and neck cancer
- 1 Introduction
- 2 Oral, head, and neck cancer
- 2.1 Different regions affected by HNC
- 2.2 Cancer
- 2.3 Standard therapies for HNC
- 3 Understanding proteases and their role in head and neck cancers
- 3.1 Matrix metalloproteinases and tissue inhibitors of metalloproteinases
- 3.1.1 Human studies on MMP inhibitors in cancer therapy and HNC
- 3.1.2 Conclusions on MMPIs potential in cancer and HNC therapy
- 3.2 Cathepsins
- 3.2.1 Cathepsin and HNC
- 3.2.2 Conclusions on cathepsin inhibitors in cancer and HNC therapy
- 3.3 Serine proteases
- 3.3.1 Studies on serine proteases inhibitors in cancer therapy and HNC
- 3.3.2 Conclusions on serine protease inhibitors in cancer and HNC therapy
- Chapter 32. Synthetic protease inhibitors in endocrine and gastroenterology cancers: Results of clinical trials
- 1 Introduction
- 1.1 Endocrine cancers
- 1.1.1 Thyroid cancer
- 1.1.2 Pituitary cancer
- 1.1.3 Adrenal cancer
- 1.1.4 Pancreas cancer
- 1.1.5 Ovarian cancer
- 1.2 Gastrointestinal cancers
- 1.2.1 Esophageal cancer
- 1.2.2 Gastric cancer
- 1.2.3 Colon cancer
- 1.3 Proteolysis
- 1.4 Types of proteases
- 1.5 Studies related to pituitary cancer
- 1.5.1 Studies related to ovarian cancer
- 1.5.2 Studies related to thyroid cancer
- 1.5.3 Studies related to pancreatic cancer
- 1.5.4 Studies related to testicular cancer
- 2 Other protease inhibitors implicated in endocrine cancers
- 2.1 Nelfinavir in different cancers
- 2.2 In thyroid cancer
- 2.3 In medullary thyroid cancer
- 2.4 In pancreatic cancer
- 2.5 In rectal cancer
- 2.6 In ovarian cancer
- 3 Conclusion
- Chapter 33. Side effects of synthetic protease inhibitors used in gynecology cancers
- 1 Introduction
- 1.1 Gynecological cancers
- 1.2 Basic science of protease inhibitors: Mechanism of action
- 1.3 Evolution and development of synthetic protease inhibitors in oncology
- 1.4 Protease inhibitors for the treatment of gynecological cancers
- 1.5 Types of protease inhibitors for the treatment of gynecological cancers
- 1.5.1 Protease inhibitors used in preclinical studies
- 1.5.2 Protease inhibitors used in clinical trial
- 1.6 General overview of common side effects in cancer treatment
- 1.7 Side effects of protease inhibitors in gynecological cancers treatment
- 1.8 Classification of side effects
- 1.8.1 Acute side effects
- 1.8.2 Chronic side effects
- 1.9 Exploration of common and rare side effects
- 1.10 Mechanism behind side effects
- 1.10 1 Biological basis of side effects
- 1.11 Management of side effects
- 1.11.1 Pharmacological and nonpharmacological management approaches
- 1.12 Future perspectives
- 1.13 The potential role of personalized medicine in minimizing side effects
- 1.14 Conclusion
- Chapter 34. The role of synthetic protease inhibitors in breast cancer
- 1 Breast cancer
- 2 Proteases
- 3 Protease inhibitors
- 4 Protease inhibitors in cancer
- 5 Protease inhibitors in breast cancer
- 6 Synthetic compounds with protease inhibitory activity in breast cancer
- 6.1 Marimastat
- 6.2 Batimastat
- 6.3 Prinomastat
- 6.4 Viracept (nelfinavir)
- 6.5 Ritonavir
- 6.6 γ-Secretase inhibitors
- 6.7 Aprotinin
- Chapter 35. Cathepsin-responsive nanomaterials for targeted delivery of malignant tumors
- 1 Introduction
- 2 Drug delivery systems for cancer therapy
- 2.1 Organic nanocarriers
- 2.1.1 Inorganic nanocarriers
- 3 Cathepsin family
- 4 Cathepsin-sensitive nanoparticles for malignant tumors
- 5 Cathepsin-sensitive nanosystems for imaging
- 6 Conclusions and future perspectives
- Index
- Edition: 1
- Published: October 22, 2024
- Imprint: Academic Press
- No. of pages: 648
- Language: English
- Paperback ISBN: 9780443300981
- eBook ISBN: 9780443300998
SC
Sajal Chakraborti
Dr. Sajal Chakraborti, PhD, DSc is a Professor at the Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, West Bengal, India. He did post-doctoral research at the Johns Hopkins Medical Institution, Baltimore; New York Medical College, New York; the University of Utah Health Sciences Center, Salt Lake City, Utah; and the University of Florida, Gainesville, Florida. He has over 35 years teaching and independent research experience in Biochemistry, Molecular Physiology and Cell Biology. He has published over 110 original research articles, dozens of review articles and book chapters, and also edited twelve books.
Affiliations and expertise
Professor, Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, IndiaSD
Srijit Das
Dr. Srijit Das is currently Professor of Anatomy at the Sultan Quaboos University in Oman. He has decades teaching experience in Anatomy including Embryology, Histology, Gross Anatomy, Neuroanatomy, Radiological Anatomy, Clinical Anatomy, and Surface Anatomy. He is member of World Association of Medical Editors. He published 500 articles in world-renowned journals, published 5 books and is editorial board member of numerous globally respected journals.
Affiliations and expertise
Professor of Anatomy, Department of Human and Clinical Anatomy, Sultan Qaboos University, OmanCK
Cheorl-Ho Kim
Prof/Dr Cheorl-Ho Kim has received his MS and PhD in The University of Tokyo during the period of 1985-1990. Currently, since 2006 he is professor and chair of Department of Biological Sciences, College of Science, Sungkyunkwan University and Samsung Advanced Institute of Health Science and Technology (SAIHST), Korea. He has successfully completed his Administrative responsibilities as Genome Program Head, Korea Research Institute of Bioscience and Biotechnology on 1990-1996 and Chairman, Department of Biochemistry and Molecular Biology, College of Oriental Medicine, Dongguk University during 1996-2006. His research has included the molecular biology of gene expression, ER-Golgi glycosyltransferases, oncogenesis, cancer metastasis and angiogenesis. He has authored more than 350 research articles/books with H-index 66. He is a member of International Scientific Advisory Board Member, International Symposium for Glycosyltransferases (GlycoT 2006), IUBMB symposium, Tsukuba and International Symposium for Glycosyltransferases (GlycoT 2008), Emory University, GA, USA, 2010 Tokai University GlycoResearch Center and 2015 Visiting Professor, The Ohio State University
Affiliations and expertise
Professor and Chair, Department of Biological Sciences, College of Science, Sungkyunkwan University and Samsung Advanced Institute of Health Science and Technology (SAIHST), KoreaRead Pathophysiological Aspects of Proteases in Cancer on ScienceDirect