Hierarchical structures in fibrillar collagens

被引:224
|
作者
Ottani, V
Martini, D
Franchi, M
Ruggeri, A
Raspanti, M
机构
[1] Univ Bologna, Ist Anat Umana Normale, I-40126 Bologna, Italy
[2] Lab Morfol Umana Luigi Cattaneo, I-21100 Varese, Italy
关键词
collagen; quasi-hexagonal packing; Microfibrils; fibrils; ultrastructure;
D O I
10.1016/S0968-4328(02)00033-1
中图分类号
TH742 [显微镜];
学科分类号
摘要
The collagen family includes several large transcripts usually exceeding 1000 aminoacid residues per single chain. As a group, they make up 1/3 of all the protein of the body and are responsible for modelling the framework of connective tissues; individually, they show both a wide variety and a complex hierarchy of mutual interactions, and form a range of functional aggregates including a variety of fibrils, microfibrils and basal membranes. Of the collagens, the fibril-forming types (i.e. the types I, II, III, V and XI) are the most abundant and the most extensively studied. At the primary structure level, the amino acid sequence of all collagens is now known in detail and it shows a distinctive domain organization. its composition being dominated by the amino acid glycine (roughly 1/3 of all residues) and by post-translational hydroxylation of proline and lysine residues. Collagen secondary and tertiary structure, which together give origin to a classic triple helix, were painstakingly determined in the 1950s and 1960s. In contrast with the primary, secondary and tertiary structure, the supramolecular arrangement within collagen fibres seems to be far more elusive, and none of the models so far advanced can be said to be universally accepted. Half a century of research and debate spawned numerous mutually incompatible models, most of them focussing either on a quasi-crystalline supramolecular array or on several forms of microfibrillar aggregates, while radial fibrils, epitaxial fibrils and other Structural models have almost been ignored. In many cases, data gained with a single technique from a single tissue were arbitrarily given a general legitimacy, whilst other well-documented morphological evidence went virtually unnoticed by the scientific community. Moreover, in recent years there has been a growing interest in the multiple interactions of collagens with the other macromolecules of the extra-cellular matrix, as their structure and their functional role become known. It is now undisputable that collagen interacts and forms functional entities with several other macromolecules of the extracellual matrix. This paper will succinctly review some current concepts on the structural biology of collagen higher-order structures. (C) 2002 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:587 / 596
页数:10
相关论文
共 50 条
  • [41] FIBRILLAR STRUCTURES OF SYNTHETIC POLYMERS
    DISTLER, GI
    GERASIMO.YM
    LEBEDEVA, VN
    DOKLADY AKADEMII NAUK SSSR, 1966, 170 (04): : 880 - &
  • [42] Improved Adhesion and Compliancy of Hierarchical Fibrillar Adhesives
    Li, Yasong
    Gates, Byron D.
    Menon, Carlo
    ACS APPLIED MATERIALS & INTERFACES, 2015, 7 (30) : 16410 - 16417
  • [43] Straw, sticks, and bricks: Genome duplication and the evolution of fibrillar collagens in the vertebrate musculoskeletal system
    Root, Z. D.
    Allen, C.
    Brewer, M.
    Gould, C.
    Medeiros, D. M.
    INTEGRATIVE AND COMPARATIVE BIOLOGY, 2021, 61 : E758 - E759
  • [44] A Comprehensive Analysis of Fibrillar Collagens in Lamprey Suggests a Conserved Role in Vertebrate Musculoskeletal Evolution
    Root, Zachary D.
    Allen, Cara
    Gould, Claire
    Brewer, Margaux
    Jandzik, David
    Medeiros, Daniel M.
    FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY, 2022, 10
  • [45] Straw, Sticks, and Bricks: Understanding Vertebrate Musculoskeletal Evolution through Fibrillar Collagens and their Diversification
    Root, Z. D.
    Jandzik, D.
    Medeiros, D. M.
    INTEGRATIVE AND COMPARATIVE BIOLOGY, 2019, 59 : E398 - E398
  • [46] Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens
    Giudici, Camilla
    Raynal, Nicolas
    Wiedemann, Hanna
    Cabral, Wayne A.
    Marini, Joan C.
    Timpl, Rupert
    Baechinger, Hans Peter
    Farndale, Richard W.
    Sasaki, Takako
    Tenni, Ruggero
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (28) : 19551 - 19560
  • [47] Direct inhibition of elastase and matrixmetalloproteinases and stimulation of biosynthesis of fibrillar collagens, elastin, and fibrillins by xanthohumol
    Philips, Neena
    Samuel, Mathew
    Arena, Rosemarie
    Chen, Yu-Jun
    Conte, Jennifer
    Natrajan, Prashanti
    Haas, Gerhard
    Gonzalez, Salvador
    JOURNAL OF COSMETIC SCIENCE, 2010, 61 (02) : 125 - 132
  • [48] Non-fibrillar collagens: Key mediators of post-infarction cardiac remodeling?
    Shamhart, Patricia E.
    Meszaros, J. Gary
    JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY, 2010, 48 (03) : 530 - 537
  • [49] Changes in tarsal plate fibrillar collagens and elastic fibre phenotype in floppy eyelid syndrome
    Ezra, Daniel G.
    Ellis, James S.
    Gaughan, Christine
    Beaconsfield, Michele
    Collin, Richard
    Bunce, Catey
    Bailly, Maryse
    Luthert, Phil
    CLINICAL AND EXPERIMENTAL OPHTHALMOLOGY, 2011, 39 (06): : 563 - +
  • [50] Cloning of an annelid fibrillar-collagen gene and phylogenetic analysis of vertebrate and invertebrate collagens
    Sicot, FX
    Exposito, JY
    Masselot, M
    Garrone, R
    Deutsch, J
    Gaill, F
    EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 246 (01): : 50 - 58