Collagen is most abundant in animal tissues as very long fibrils with a
characteristic axial periodic structure. The fibrils provide the major
biomechanical scaffold for cell attachment and anchorage of
macromolecules, allowing the shape and form of tissues to be defined and
maintained, How the fibrils are formed from their monomeric precursors
is the primary concern of this review. Collagen fibril formation is
basically a self-assembly process (i.e. one which is to a large extent
determined by the intrinsic properties of the collagen molecules
themselves) but it is also sensitive to cell-mediated regulation,
particularly in young or healing tissues. Recent attention has been
focused on `early fibrils' or `fibril segments' of similar to 10 mu m in
length which appear to be intermediates in the formation of mature
fibrils that can grow to be hundreds of micrometres in length. Data from
several laboratories indicate that these early fibrils can be unipolar
(with all molecules pointing in the same direction) or bipolar (in which
the orientation of collagen molecules reverses at a single location
along the fibril). The occurrence of such early fibrils has major
implications for tissue morphogenesis and repair. In this article we
review the current understanding of the origin of unipolar and bipolar
fibrils, and how mature fibrils are assembled from early fibrils. We
include preliminary evidence from invertebrates which suggests that the
principles for bipolar fibril assembly were established at least 500
million years ago.
%0 Journal Article
%1 kad-hol
%A Kadler, KE
%A Holmes, DF
%A Trotter, JA
%A Chapman, JA
%C 59 PORTLAND PLACE, LONDON, ENGLAND W1N 3AJ
%D 1996
%I PORTLAND PRESS
%J BIOCHEMICAL JOURNAL
%K collagen lung
%N Part 1
%P 1-11
%T Collagen fibril formation
%V 316
%X Collagen is most abundant in animal tissues as very long fibrils with a
characteristic axial periodic structure. The fibrils provide the major
biomechanical scaffold for cell attachment and anchorage of
macromolecules, allowing the shape and form of tissues to be defined and
maintained, How the fibrils are formed from their monomeric precursors
is the primary concern of this review. Collagen fibril formation is
basically a self-assembly process (i.e. one which is to a large extent
determined by the intrinsic properties of the collagen molecules
themselves) but it is also sensitive to cell-mediated regulation,
particularly in young or healing tissues. Recent attention has been
focused on `early fibrils' or `fibril segments' of similar to 10 mu m in
length which appear to be intermediates in the formation of mature
fibrils that can grow to be hundreds of micrometres in length. Data from
several laboratories indicate that these early fibrils can be unipolar
(with all molecules pointing in the same direction) or bipolar (in which
the orientation of collagen molecules reverses at a single location
along the fibril). The occurrence of such early fibrils has major
implications for tissue morphogenesis and repair. In this article we
review the current understanding of the origin of unipolar and bipolar
fibrils, and how mature fibrils are assembled from early fibrils. We
include preliminary evidence from invertebrates which suggests that the
principles for bipolar fibril assembly were established at least 500
million years ago.
@article{kad-hol,
abstract = {{Collagen is most abundant in animal tissues as very long fibrils with a
characteristic axial periodic structure. The fibrils provide the major
biomechanical scaffold for cell attachment and anchorage of
macromolecules, allowing the shape and form of tissues to be defined and
maintained, How the fibrils are formed from their monomeric precursors
is the primary concern of this review. Collagen fibril formation is
basically a self-assembly process (i.e. one which is to a large extent
determined by the intrinsic properties of the collagen molecules
themselves) but it is also sensitive to cell-mediated regulation,
particularly in young or healing tissues. Recent attention has been
focused on `early fibrils' or `fibril segments' of similar to 10 mu m in
length which appear to be intermediates in the formation of mature
fibrils that can grow to be hundreds of micrometres in length. Data from
several laboratories indicate that these early fibrils can be unipolar
(with all molecules pointing in the same direction) or bipolar (in which
the orientation of collagen molecules reverses at a single location
along the fibril). The occurrence of such early fibrils has major
implications for tissue morphogenesis and repair. In this article we
review the current understanding of the origin of unipolar and bipolar
fibrils, and how mature fibrils are assembled from early fibrils. We
include preliminary evidence from invertebrates which suggests that the
principles for bipolar fibril assembly were established at least 500
million years ago.}},
added-at = {2013-01-07T11:25:24.000+0100},
address = {{59 PORTLAND PLACE, LONDON, ENGLAND W1N 3AJ}},
affiliation = {{Kadler, KE (Reprint Author), UNIV MANCHESTER,SCH BIOL SCI,WELLCOME TRUST CTR CELL MATRIX RES,STOPFORD BLDG 2205,OXFORD RD,MANCHESTER M13 9PT,LANCS,ENGLAND..
UNIV MANCHESTER,DEPT MED BIOPHYS,MANCHESTER M13 9PT,LANCS,ENGLAND.
UNIV NEW MEXICO,SCH MED,DEPT ANAT,ALBUQUERQUE,NM 87131.}},
author = {Kadler, KE and Holmes, DF and Trotter, JA and Chapman, JA},
biburl = {https://www.bibsonomy.org/bibtex/2f9550555e2301c477dff8846665f2311/jehiorns},
doc-delivery-number = {{UM293}},
interhash = {c601efb2dc2fda72591df09c26d49485},
intrahash = {f9550555e2301c477dff8846665f2311},
issn = {{0264-6021}},
journal = {{BIOCHEMICAL JOURNAL}},
journal-iso = {{Biochem. J.}},
keywords = {collagen lung},
keywords-plus = {{SELF-ASSEMBLY INVITRO; AMINO-ACID SEQUENCE; SYNDROME TYPE-VIIB;
X-RAY-DIFFRACTION; I COLLAGEN; ELECTRON-MICROSCOPE; CONNECTIVE-TISSUE;
FIBRILLOGENESIS INVITRO; DERMATAN SULFATE; PC-COLLAGEN}},
language = {{English}},
month = {{MAY 15}},
number = {{Part 1}},
number-of-cited-references = {{107}},
pages = {{1-11}},
publisher = {{PORTLAND PRESS}},
research-areas = {{Biochemistry \& Molecular Biology}},
times-cited = {{506}},
timestamp = {2013-01-07T11:25:24.000+0100},
title = {{Collagen fibril formation}},
type = {{Review}},
unique-id = {{ISI:A1996UM29300001}},
volume = {{316}},
web-of-science-categories = {{Biochemistry \& Molecular Biology}},
year = {{1996}}
}