title: Fibrillar, fibril-associated and basement membrane collagens of the arterial wall: architecture, elasticity and remodeling under stress.
abstract: The ability of a human artery to pass through 150 million liters of blood sustaining 2 billion pulsations of blood pressure with minor deterioration depends on unique construction of the arterial wall. Viscoelastic properties of this construction enable to re-seal the occuring damages apparently without direct immediate participance of the constituent cells. Collagen structures are considered to be the elements that determine the mechanoelastic properties of the wall in parallel with elastin responsible for elasticity and resilience. Collagen scaffold architecture is the function-dependent dynamic arrangement of a dozen different collagen types composing three distinct interacting forms inside the extracellular matrix of the wall. Tightly packed molecules of collagen types I, III, V provide high tensile strength along collagen fibrils but toughness of the collagen scaffold as a whole depends on molecular bonds between distinct fibrils. Apart of other macromolecules in the extracellular matrix (ECM), collagen-specific interlinks involve microfilaments of collagen type VI, meshwork-organized collagen type VIII, and FACIT collagen type XIV. Basement membrane collagen types IV, XV, XVIII and cell-associated collagen XIII enable transmission of mechanical signals between cells and whole artery matrix. Collagen scaffold undergoes continuous remodeling by decomposition promoted with MMPs and reconstitution from newly produced collagen molecules. Pulsatile stress-strain load modulates both collagen synthesis and MMP-dependent collagen degradation. In this way the ECM structure becomes adoptive to mechanical challenges. The mechanoelastic properties of the arterial wall are changed in atherosclerosis concomitantly with collagen turnover both type-specific and dependent on the structure. Improving the feedback could be another approach to restore sufficient blood circulation.
authors.forename: M S
authors.initials: MS
authors.lastname: Osidak
authors.forename: E O
authors.initials: EO
authors.lastname: Osidak
authors.forename: M A
authors.initials: MA
authors.lastname: Akhmanova
authors.forename: S P
authors.initials: SP
authors.lastname: Domogatsky
authors.affiliation: Division of Matrix Biology, Department of Medical Biochemistry and BIophysics, Karolinska Institute, 171 77, Stockholm, Sweden. anna.domogatskaya@ki.se.
authors.forename: A S
authors.initials: AS
authors.lastname: Domogatskaya
mesh_terms: D001158:Arteries / Q000033:anatomy & histology / Q000473:pathology / Q000502:physiology*; D050197:Atherosclerosis / Q000473:pathology / Q000503:physiopathology*; D001485:Basement Membrane / Q000502:physiology*; D004548:Elasticity / Q000502:physiology*; D005109:Extracellular Matrix / Q000502:physiology; D024021:Fibril-Associated Collagens / Q000502:physiology*; D024022:Fibrillar Collagens / Q000502:physiology*; D006801:Humans; D020782:Matrix Metalloproteinases / Q000097:blood; D013314:Stress, Mechanical; D066253:Vascular Remodeling / Q000502:physiology*
chemical_list: D024021:Fibril-Associated Collagens; D024022:Fibrillar Collagens; D020782:Matrix Metalloproteinases