Biochemistry of Collagens, Laminins and Elastin

- Structure, Function and Biomarkers

  • Format
  • Bog, paperback
  • Engelsk

Beskrivelse

Biochemistry of Collagens, Laminins, and Elastin: Structure, Function, and Biomarkers provides a comprehensive introduction to collagen and structural proteins. Type I collagen is one of the most abundant molecules in the body, playing essential roles in different tissues, particularly bone and skin. A key aspect of type I collagen is its post-translational modifications which are essential for correct synthesis and structural integrity of collagens, for tissue-specific functionality, as well as for application as biomarkers of different pathologies. This volume summarizes current data on key structural proteins (collagens, laminins and elastin), reviews how these molecules affect pathologies, and describes selected modifications of proteins that result in altered signaling properties of the original extracellular matrix component. Further, it discusses the novel concept that an increasing number of components of the ECM harbor cryptic signaling functions that may be viewed as endocrine functions. Additionally, it highlights how this knowledge can be exploited to modulate fibrotic disease.

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Detaljer
  • SprogEngelsk
  • Sidetal272
  • Udgivelsesdato26-08-2016
  • ISBN139780128098479
  • Forlag Academic Press Inc
  • FormatPaperback
Størrelse og vægt
  • Vægt430 g
  • coffee cup img
    10 cm
    book img
    15,1 cm
    22,9 cm

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    PTM Cancer Kidney Organization Osteoarthritis. Muscle cells Musculoskeletal Diseases Arthritis Wound healing Tourette syndrome Alzheimer Disease Structure Fibrosis Liver Skin Thymus Collagen Lung Articular cartilage Ovarian cancer Extracellular matrix Chondrocytes Muscular Dystrophy Autoimmune diseases Cartilage Ovary Therapy Bone Calcification Endothelial Cells Skin Disease Testis Basement Membrane Epidermolysis bullosa Eye Abnormalities Tumor Head and neck cancer Therapeutic target Posttranslational Modifications Bleomycin Fibrillogenesis Function Biomarkers Smooth Muscle Cells Amyloid plaque Prostate cancer Tumor tissue Ligand Chemoresistance Embryogenesis Fibronectin Colon cancer Biomarker Microfibrils Neuromuscular junctions Breast carcinoma Antiangiogenesis Mechanical stress Hepatocarcinoma Alport syndrome Skeletogenesis HNSCC Type II collagen 120-kDa linear IgA dermatosis antigen 97-kDa linear IgA dermatosis antigen Achilles tendinopathy BACE-1 Basement membrane zone ASPD COL26A1 Collagen Fibers CCDD COL25A1 Collagen II Collagen XI Collagen XXIV Blood vessel assembly CLAC Cross-linkage COL20A1 BP180 Early-onset osteoarthritis EDS/myopathy overlap syndrome Cell Attachment chondrodysplasia facit EMID2 Fibril-associated collagen Ehlers�Danlos syndrome COL21A1 COL22A1 COL23A1 Emilin COL27A1 Collagen XV Endochondral bone Goodpasture syndrome FACIT collagen Fibrillar Collagen Frizzled domain Descemet membrane Growth-plate cartilage Integrin a11�1 Homotrimer Endostatin Endotrophin Integrin a2�1 Matrikines Fibrillar Fibrillar-associated collagen Fibrillation Fibrogenesis Knocbloch syndrome Focal Adhesions Multiplexin Multiplexin family Matrix quality NC1 Muscle dystrophies Microfibril Furin convertase Furin protease NSCLC cancer Myotendinous junctions Hypertrophic Chondrocytes P5NP Palmoplantar Keratoderma P5CP Interstitial matrix Inflammation-associated Sclerotic capillaries Schmidt metaphyseal chondrodysplasia serum biomarker Steel syndrome Type VIII collagen Type XII collagen Type XVIII collagen Type XX collagen Type XXI collagen Type XXVII collagen urine biomarker Vastatin Interrupted triple helices Type XVII collagen XVVIII Tumstatin Type IV collagen Type XVI Unmyelinated fibers Multiple epiphyseal dysplasia Kidney fibrosis Membrane collagen Osteoblast Differentiation Myocytes Pro-C5 Nonfibrillar Nonfibrillar collagen Skeletal abnormalities Restin Type XXII collagen Postnatal growth Type V collagen xix Skin blistering disorders Type I collagen Type Iii Type X collagen Type XIV Transmembrane collagen Type IX Collagen Type VI collagen Type VII Collagen Type XIII Type XXIII collagen

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