Localization of pN-type IIA procollagen on adult bovine vitreous collagen fibrils

Anthony Reardon; Linda Sandell; Carolyn J.P. Jones; David McLeod; Paul N. Bishop

doi:10.1016/S0945-053X(00)00058-5

Localization of pN-type IIA procollagen on adult bovine vitreous collagen fibrils

Anthony Reardon, Linda Sandell, Carolyn J.P. Jones, David McLeod, Paul N. Bishop

Department of Orthopedic Surgery

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

Abstract

Type II procollagen is synthesized in long (type IIA) and short (type IIB) forms because of alternative splicing of mRNA; the long form containing an additional cysteine-rich domain in the amino-propeptide. An antiserum (IIA) that recognizes this domain was used for immunolocalization studies on adult bovine vitreous at light and electron microscopic levels and for Western blot analyses. The immunolocalization studies revealed labelling by the IIA antiserum of the vitreous collagen fibrils. This labelling was removed by prior extraction of the fibrils with 6 M guanidine hydrochloride (GuHCl) and the extract was shown to contain pN-type IIA procollagen. Adult vitreous collagen fibrils are coated with pN-type IIA procollagen, a finding with potential implications for vitreous collagen fibril structure and function. (C) 2000 Elsevier Science B.V./International Society of Matrix Biology.

Original language	English
Pages (from-to)	169-173
Number of pages	5
Journal	Matrix Biology
Volume	19
Issue number	2
DOIs	https://doi.org/10.1016/S0945-053X(00)00058-5
State	Published - May 1 2000

Keywords

Amino-propeptide
Collagen
Type IIA procollagen
Vitreous

Access to Document

10.1016/S0945-053X(00)00058-5

Cite this

@article{fa8e7b052afb41e4addf12891faffc04,

title = "Localization of pN-type IIA procollagen on adult bovine vitreous collagen fibrils",

abstract = "Type II procollagen is synthesized in long (type IIA) and short (type IIB) forms because of alternative splicing of mRNA; the long form containing an additional cysteine-rich domain in the amino-propeptide. An antiserum (IIA) that recognizes this domain was used for immunolocalization studies on adult bovine vitreous at light and electron microscopic levels and for Western blot analyses. The immunolocalization studies revealed labelling by the IIA antiserum of the vitreous collagen fibrils. This labelling was removed by prior extraction of the fibrils with 6 M guanidine hydrochloride (GuHCl) and the extract was shown to contain pN-type IIA procollagen. Adult vitreous collagen fibrils are coated with pN-type IIA procollagen, a finding with potential implications for vitreous collagen fibril structure and function. (C) 2000 Elsevier Science B.V./International Society of Matrix Biology.",

keywords = "Amino-propeptide, Collagen, Type IIA procollagen, Vitreous",

author = "Anthony Reardon and Linda Sandell and Jones, {Carolyn J.P.} and David McLeod and Bishop, {Paul N.}",

note = "Funding Information: This work was supported by the Wellcome Trust. P.N.B. holds a Wellcome Trust Senior Research Fellowship in Clinical Science.",

year = "2000",

month = may,

day = "1",

doi = "10.1016/S0945-053X(00)00058-5",

language = "English",

volume = "19",

pages = "169--173",

journal = "Matrix Biology",

issn = "0945-053X",

number = "2",

}

TY - JOUR

T1 - Localization of pN-type IIA procollagen on adult bovine vitreous collagen fibrils

AU - Reardon, Anthony

AU - Sandell, Linda

AU - Jones, Carolyn J.P.

AU - McLeod, David

AU - Bishop, Paul N.

N1 - Funding Information: This work was supported by the Wellcome Trust. P.N.B. holds a Wellcome Trust Senior Research Fellowship in Clinical Science.

PY - 2000/5/1

Y1 - 2000/5/1

N2 - Type II procollagen is synthesized in long (type IIA) and short (type IIB) forms because of alternative splicing of mRNA; the long form containing an additional cysteine-rich domain in the amino-propeptide. An antiserum (IIA) that recognizes this domain was used for immunolocalization studies on adult bovine vitreous at light and electron microscopic levels and for Western blot analyses. The immunolocalization studies revealed labelling by the IIA antiserum of the vitreous collagen fibrils. This labelling was removed by prior extraction of the fibrils with 6 M guanidine hydrochloride (GuHCl) and the extract was shown to contain pN-type IIA procollagen. Adult vitreous collagen fibrils are coated with pN-type IIA procollagen, a finding with potential implications for vitreous collagen fibril structure and function. (C) 2000 Elsevier Science B.V./International Society of Matrix Biology.

AB - Type II procollagen is synthesized in long (type IIA) and short (type IIB) forms because of alternative splicing of mRNA; the long form containing an additional cysteine-rich domain in the amino-propeptide. An antiserum (IIA) that recognizes this domain was used for immunolocalization studies on adult bovine vitreous at light and electron microscopic levels and for Western blot analyses. The immunolocalization studies revealed labelling by the IIA antiserum of the vitreous collagen fibrils. This labelling was removed by prior extraction of the fibrils with 6 M guanidine hydrochloride (GuHCl) and the extract was shown to contain pN-type IIA procollagen. Adult vitreous collagen fibrils are coated with pN-type IIA procollagen, a finding with potential implications for vitreous collagen fibril structure and function. (C) 2000 Elsevier Science B.V./International Society of Matrix Biology.

KW - Amino-propeptide

KW - Collagen

KW - Type IIA procollagen

KW - Vitreous

UR - http://www.scopus.com/inward/record.url?scp=0034193659&partnerID=8YFLogxK

U2 - 10.1016/S0945-053X(00)00058-5

DO - 10.1016/S0945-053X(00)00058-5

M3 - Article

C2 - 10842100

AN - SCOPUS:0034193659

SN - 0945-053X

VL - 19

SP - 169

EP - 173

JO - Matrix Biology

JF - Matrix Biology

IS - 2

ER -

Localization of pN-type IIA procollagen on adult bovine vitreous collagen fibrils

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this