The insoluble TGFBIp fraction of the cornea is covalently linked via a disulfide bond to type XII collagen

Kasper Runager; Gordon K Klintworth; Henrik Karring; Jan Johannes Enghild

doi:10.1021/bi400212m

The insoluble TGFBIp fraction of the cornea is covalently linked via a disulfide bond to type XII collagen

Kasper Runager, Gordon K Klintworth, Henrik Karring, Jan Johannes Enghild

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Abstract

TGFBIp, also known as keratoepithelin and βig-h3, is among the most abundant proteins in the human cornea, and approximately 60% is associated with the insoluble fraction following extraction in sodium dodecyl sulfate (SDS) sample buffer. TGFBIp is of particular interest because a wide range of mutations causes amyloid or fuchsinophilic crystalloid deposits in the cornea leading to visual impairment. We show that the SDS-insoluble fraction of TGFBIp from porcine and human corneas is covalently linked via a reducible bond to the NC3 domain of type XII collagen in a TGFBIp:type XII collagen stoichiometric ratio of 2:1. Because type XII collagen is anchored to striated collagen fibers of the extracellular matrix, its interaction with TGFBIp is likely to provide anchoring for cells to the extracellular matrix through the integrin binding capability of TGFBIp. Furthermore, the TGFBIp-type XII collagen molecule will affect our understanding of the molecular pathogenesis of the TGFBI-linked corneal dystrophies.

Originalsprog	Engelsk
Tidsskrift	Biochemistry
Vol/bind	52
Nummer	16
Sider (fra-til)	2821-2827
Antal sider	7
ISSN	0006-2960
DOI	https://doi.org/10.1021/bi400212m
Status	Udgivet - 23 apr. 2013

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10.1021/bi400212m

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title = "The insoluble TGFBIp fraction of the cornea is covalently linked via a disulfide bond to type XII collagen",

abstract = "TGFBIp, also known as keratoepithelin and βig-h3, is among the most abundant proteins in the human cornea, and approximately 60% is associated with the insoluble fraction following extraction in sodium dodecyl sulfate (SDS) sample buffer. TGFBIp is of particular interest because a wide range of mutations causes amyloid or fuchsinophilic crystalloid deposits in the cornea leading to visual impairment. We show that the SDS-insoluble fraction of TGFBIp from porcine and human corneas is covalently linked via a reducible bond to the NC3 domain of type XII collagen in a TGFBIp:type XII collagen stoichiometric ratio of 2:1. Because type XII collagen is anchored to striated collagen fibers of the extracellular matrix, its interaction with TGFBIp is likely to provide anchoring for cells to the extracellular matrix through the integrin binding capability of TGFBIp. Furthermore, the TGFBIp-type XII collagen molecule will affect our understanding of the molecular pathogenesis of the TGFBI-linked corneal dystrophies.",

author = "Kasper Runager and Klintworth, {Gordon K} and Henrik Karring and Enghild, {Jan Johannes}",

year = "2013",

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doi = "10.1021/bi400212m",

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pages = "2821--2827",

journal = "Biochemistry",

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T1 - The insoluble TGFBIp fraction of the cornea is covalently linked via a disulfide bond to type XII collagen

AU - Runager, Kasper

AU - Klintworth, Gordon K

AU - Karring, Henrik

AU - Enghild, Jan Johannes

PY - 2013/4/23

Y1 - 2013/4/23

N2 - TGFBIp, also known as keratoepithelin and βig-h3, is among the most abundant proteins in the human cornea, and approximately 60% is associated with the insoluble fraction following extraction in sodium dodecyl sulfate (SDS) sample buffer. TGFBIp is of particular interest because a wide range of mutations causes amyloid or fuchsinophilic crystalloid deposits in the cornea leading to visual impairment. We show that the SDS-insoluble fraction of TGFBIp from porcine and human corneas is covalently linked via a reducible bond to the NC3 domain of type XII collagen in a TGFBIp:type XII collagen stoichiometric ratio of 2:1. Because type XII collagen is anchored to striated collagen fibers of the extracellular matrix, its interaction with TGFBIp is likely to provide anchoring for cells to the extracellular matrix through the integrin binding capability of TGFBIp. Furthermore, the TGFBIp-type XII collagen molecule will affect our understanding of the molecular pathogenesis of the TGFBI-linked corneal dystrophies.

AB - TGFBIp, also known as keratoepithelin and βig-h3, is among the most abundant proteins in the human cornea, and approximately 60% is associated with the insoluble fraction following extraction in sodium dodecyl sulfate (SDS) sample buffer. TGFBIp is of particular interest because a wide range of mutations causes amyloid or fuchsinophilic crystalloid deposits in the cornea leading to visual impairment. We show that the SDS-insoluble fraction of TGFBIp from porcine and human corneas is covalently linked via a reducible bond to the NC3 domain of type XII collagen in a TGFBIp:type XII collagen stoichiometric ratio of 2:1. Because type XII collagen is anchored to striated collagen fibers of the extracellular matrix, its interaction with TGFBIp is likely to provide anchoring for cells to the extracellular matrix through the integrin binding capability of TGFBIp. Furthermore, the TGFBIp-type XII collagen molecule will affect our understanding of the molecular pathogenesis of the TGFBI-linked corneal dystrophies.

U2 - 10.1021/bi400212m

DO - 10.1021/bi400212m

M3 - Journal article

C2 - 23556985

SN - 0006-2960

VL - 52

SP - 2821

EP - 2827

JO - Biochemistry

JF - Biochemistry

IS - 16

ER -

The insoluble TGFBIp fraction of the cornea is covalently linked via a disulfide bond to type XII collagen

Abstract

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