Variation in type I collagen fibril nanomorphology

the significance and origin

Research output: Contribution to journalReview ArticleOtherpeer-review

Abstract

Although the axial D-periodic spacing is a well-recognized nanomorphological feature of type I collagen fibrils,the existence of a distribution of values has been largely overlooked since its discovery seven decades ago.Studies based on single fibril measurements occasionally noted variation in D-spacing values, but accredited it with nobiological significance. Recent quantitative characterizations supported that a 10-nm collagen D-spacing distribution is intrinsic to collagen fibrils in various tissues as well as in vitro self-assembly of reconstituted collagen. In addition,the distribution is altered in Osteogenesis Imperfecta and long-term estrogen deprivation. Bone collagen is organized into lamellar sheets of bundles at the micro-scale, and D-spacings within a bundle of a lamella are mostly identical,whereas variations among different bundles contribute to the full-scale distribution. This seems to be a very general phenomenon for the protein as the same type of D-spacing/bundle organization is observed for dermal and tendon collagen. More research investigation of collagen nanomorphology in connection to bone biology is required to fully understand these new observations. Here we review the data demonstrating the existence of a D-spacing distribution, the impact of disease on the distribution and possible explanations for the origin of D-spacing variations based on various collagen fibrillogenesis models.
Original languageEnglish
Article number394
Number of pages8
JournalBoneKEy Reports
Volume2
DOIs
Publication statusPublished - 2013
Externally publishedYes

Cite this

@article{ee04591a5f434b929ffa450ee40d2723,
title = "Variation in type I collagen fibril nanomorphology: the significance and origin",
abstract = "Although the axial D-periodic spacing is a well-recognized nanomorphological feature of type I collagen fibrils,the existence of a distribution of values has been largely overlooked since its discovery seven decades ago.Studies based on single fibril measurements occasionally noted variation in D-spacing values, but accredited it with nobiological significance. Recent quantitative characterizations supported that a 10-nm collagen D-spacing distribution is intrinsic to collagen fibrils in various tissues as well as in vitro self-assembly of reconstituted collagen. In addition,the distribution is altered in Osteogenesis Imperfecta and long-term estrogen deprivation. Bone collagen is organized into lamellar sheets of bundles at the micro-scale, and D-spacings within a bundle of a lamella are mostly identical,whereas variations among different bundles contribute to the full-scale distribution. This seems to be a very general phenomenon for the protein as the same type of D-spacing/bundle organization is observed for dermal and tendon collagen. More research investigation of collagen nanomorphology in connection to bone biology is required to fully understand these new observations. Here we review the data demonstrating the existence of a D-spacing distribution, the impact of disease on the distribution and possible explanations for the origin of D-spacing variations based on various collagen fibrillogenesis models.",
author = "Ming Fang and {Banaszak Holl}, {Mark M.}",
year = "2013",
doi = "10.1038/bonekey.2013.128",
language = "English",
volume = "2",
journal = "BoneKEy Reports",
issn = "2047-6396",
publisher = "Nature Publishing Group",

}

Variation in type I collagen fibril nanomorphology : the significance and origin. / Fang, Ming; Banaszak Holl, Mark M.

In: BoneKEy Reports, Vol. 2, 394, 2013.

Research output: Contribution to journalReview ArticleOtherpeer-review

TY - JOUR

T1 - Variation in type I collagen fibril nanomorphology

T2 - the significance and origin

AU - Fang, Ming

AU - Banaszak Holl, Mark M.

PY - 2013

Y1 - 2013

N2 - Although the axial D-periodic spacing is a well-recognized nanomorphological feature of type I collagen fibrils,the existence of a distribution of values has been largely overlooked since its discovery seven decades ago.Studies based on single fibril measurements occasionally noted variation in D-spacing values, but accredited it with nobiological significance. Recent quantitative characterizations supported that a 10-nm collagen D-spacing distribution is intrinsic to collagen fibrils in various tissues as well as in vitro self-assembly of reconstituted collagen. In addition,the distribution is altered in Osteogenesis Imperfecta and long-term estrogen deprivation. Bone collagen is organized into lamellar sheets of bundles at the micro-scale, and D-spacings within a bundle of a lamella are mostly identical,whereas variations among different bundles contribute to the full-scale distribution. This seems to be a very general phenomenon for the protein as the same type of D-spacing/bundle organization is observed for dermal and tendon collagen. More research investigation of collagen nanomorphology in connection to bone biology is required to fully understand these new observations. Here we review the data demonstrating the existence of a D-spacing distribution, the impact of disease on the distribution and possible explanations for the origin of D-spacing variations based on various collagen fibrillogenesis models.

AB - Although the axial D-periodic spacing is a well-recognized nanomorphological feature of type I collagen fibrils,the existence of a distribution of values has been largely overlooked since its discovery seven decades ago.Studies based on single fibril measurements occasionally noted variation in D-spacing values, but accredited it with nobiological significance. Recent quantitative characterizations supported that a 10-nm collagen D-spacing distribution is intrinsic to collagen fibrils in various tissues as well as in vitro self-assembly of reconstituted collagen. In addition,the distribution is altered in Osteogenesis Imperfecta and long-term estrogen deprivation. Bone collagen is organized into lamellar sheets of bundles at the micro-scale, and D-spacings within a bundle of a lamella are mostly identical,whereas variations among different bundles contribute to the full-scale distribution. This seems to be a very general phenomenon for the protein as the same type of D-spacing/bundle organization is observed for dermal and tendon collagen. More research investigation of collagen nanomorphology in connection to bone biology is required to fully understand these new observations. Here we review the data demonstrating the existence of a D-spacing distribution, the impact of disease on the distribution and possible explanations for the origin of D-spacing variations based on various collagen fibrillogenesis models.

U2 - 10.1038/bonekey.2013.128

DO - 10.1038/bonekey.2013.128

M3 - Review Article

VL - 2

JO - BoneKEy Reports

JF - BoneKEy Reports

SN - 2047-6396

M1 - 394

ER -