Nothing Special   »   [go: up one dir, main page]

Ravi et al., 2013 - Google Patents

The role of furin in the development of skin cancer

Ravi et al., 2013

View HTML
Document ID
14603279426619247360
Author
Ravi R
Piva T
Publication year
Publication venue
Highlights in Skin Cancer; Intech: Rijeka, Croatia

External Links

Snippet

Skin cancer represents a major, and growing, public health problem, and is the most common type of cancer observed in Caucasians [1-3]. The three most common forms of skin cancer are basal cell carcinoma (BCC), squamous cell carcinoma (SCC) and melanoma …
Continue reading at www.intechopen.com (HTML) (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6489—Metalloendopeptidases (3.4.24)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424—Serine endopeptidases (3.4.21)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/43—Enzymes; Proenzymes; Derivatives thereof
    • A61K38/46—Hydrolases (3)
    • A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6402—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K31/00—Medicinal preparations containing organic active ingredients
    • A61K31/185—Acids; Anhydrides, halides or salts thereof, e.g. sulfur acids, imidic, hydrazonic, hydroximic acids
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K31/00—Medicinal preparations containing organic active ingredients
    • A61K31/33—Heterocyclic compounds
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K9/00—Medicinal preparations characterised by special physical form
    • A61K9/0012—Galenical forms characterised by the site of application

Similar Documents

Publication Publication Date Title
Rengel et al. Proteinases in the joint: clinical relevance of proteinases in joint destruction
Sárdy Role of matrix metalloproteinases in skin ageing
Zhang et al. Role of matrix metalloproteinases and therapeutic benefits of their inhibition in spinal cord injury
Mauviel Cytokine regulation of metalloproteinase gene expression
Folgueras et al. Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies
Kerkelä et al. Matrix metalloproteinases in tumor progression: focus on basal and squamous cell skin cancer
Kraiem et al. Matrix metalloproteinases and the thyroid
Kurzepa et al. Role of MMP-2 and MMP-9 and their natural inhibitors in liver fibrosis, chronic pancreatitis and non-specific inflammatory bowel diseases
Stawowy et al. Furin-like proprotein convertases are central regulators of the membrane type matrix metalloproteinase–pro-matrix metalloproteinase-2 proteolytic cascade in atherosclerosis
Madlener et al. Matrix metalloproteinases (MMPs) and their physiological inhibitors (TIMPs) are differentially expressed during excisional skin wound repair
Kim et al. Secreted and membrane-associated matrix metalloproteinases of IL-2-activated NK cells and their inhibitors
Shamamian et al. Activation of progelatinase A (MMP‐2) by neutrophil elastase, cathepsin G, and proteinase‐3: a role for inflammatory cells in tumor invasion and angiogenesis
Creemers et al. Matrix metalloproteinase inhibition after myocardial infarction: a new approach to prevent heart failure?
Jackson et al. Human microvascular endothelial cells differ from macrovascular endothelial cells in their expression of matrix metalloproteinases
DeClerck et al. Cooperation between matrix metalloproteinases and the plasminogen activator-plasmin system in tumor progression
Binder et al. Relaxin enhances in-vitro invasiveness of breast cancer cell lines by up-regulation of matrix metalloproteases
Bachmeier et al. Matrix metalloproteinases in cancer: comparison of known and novel aspects of their inhibition as a therapeutic approach
Herouy Matrix metalloproteinases in skin pathology
Speake et al. Radiation induced MMP expression from rectal cancer is short lived but contributes to in vitro invasion
Riihilä et al. Matrix metalloproteinases in keratinocyte carcinomas
Nissinen et al. Collagen turnover in wound repair––A macrophage connection
Wyganowska-Świątkowska et al. The plasminogen activation system in periodontal tissue
Herouy et al. Matrix metalloproteinases and venous leg ulceration
Ravi et al. The role of furin in the development of skin cancer
Yong The potential use of MMP inhibitors to treat CNS diseases