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Cited by 89Proteoglycans and glycosaminoglycans researchConnective tissue disorders researchBone and Dental Protein Studies

βig-h3 Interacts Directly with Biglycan and Decorin, Promotes Collagen VI Aggregation, and Participates in Ternary Complexing with These Macromolecules

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Reinboth, Betty, Thomas, John, Hanssen, Eric, Gibson, Mark A.·2006·Journal of Biological Chemistry
DOI 10.1074/jbc.m511316200
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Abstract

Recombinant human beta ig-h3 was found to bind 125I-labeled small leucine-rich proteoglycans (SLRPs), biglycan, and decorin, in co-immunoprecipitation experiments. In each instance the binding could be blocked by an excess of the unlabeled proteoglycan, confirming the specificity of the interaction. Scatchard analysis showed that biglycan bound beta ig-h3 more avidly than decorin with Kd values estimated as 5.88 x 10(-8) and 1.02 x 10(-7) M, respectively. In reciprocal blocking experiments both proteoglycans inhibited the others binding to beta ig-h3 indicating that they may share the same binding site or that the two binding sites are in close proximity on the beta ig-h3 molecule. Since beta ig-h3 and the SLRPs are known to be associated with the amino-terminal region of collagen VI in tissue microfibrils, the effects of including collagen VI in the incubations were investigated. Co-immunoprecipitation of 125I-labeled biglycan incubated with equimolar mixtures of beta ig-h3 and pepsin-collagen VI was increased 6-fold over beta ig-h3 alone and 3-fold over collagen VI alone. Similar increases were also observed for decorin. The findings indicate that beta ig-h3 participates in a ternary complex with collagen VI and SLRPs. Static light scattering techniques were used to show that beta ig-h3 rapidly forms very high molecular weight complexes with both native and pepsin-collagen VI, either alone or with the SLRPs. Indeed beta ig-h3 was shown to form a complex with collagen VI and biglycan, which appeared to be much more extensive than that formed by beta ig-h3 with collagen VI and decorin or those formed between the collagen and beta ig-h3, biglycan, or decorin alone. Biglycan core protein was shown to inhibit the extent of complexing of beta ig-h3 with native and pepsin-collagen VI suggesting that the glycosaminoglycan side chains of the proteoglycan were important for the formation of the large ternary complexes. Further studies showed that the direct interaction between beta ig-h3 and biglycan and between biglycan and collagen VI were also important for the formation of these complexes. The globular domains of collagen VI also appeared to have an influence on the interaction of the three components. Overall the results indicate that beta ig-h3 can differentially modulate the aggregation of collagen VI with biglycan and decorin. Thus this interplay is likely to be important in tissues such as cornea where such complexes are considered to occur.

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  • TGFBI is a secreted RGD motif-containing protein that binds to ECMs such as collagen types I, II, and IV as well as proteoglycans.

    “TGFBI is a secreted Arg-Gly-Asp (RGD) motif-containing protein that also binds to ECMs such as collagen types I, II, and IV as well as proteoglycans (28).”

    From Reprogramming of three-dimensional microenvironments for in vitro hair follicle induction (2022) · cites this paper as [28]

    The introductory passage (page unavailable) identifies βig-h3/TGFBI as an extracellular-matrix protein and says it binds several collagen types; the discussion specifically mentions collagen I binding. The paper also reports direct binding to the proteoglycans biglycan and decorin. Our copy does not identify collagen II or IV as binding partners or explicitly establish that the protein is secreted and contains an RGD motif; it lists RGD-CAP as an alternative name. (LLM, conf=0.86)

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1 of the 40 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

  1. Bruns, R. R., Press, W., Engvall, E., Timpl, R., and Gross, J. (1986) J. Cell Biol. 103, 393-404

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Related

Authors
Reinboth, B., Thomas, J., Hanssen, E., & Gibson, M. A.
Affiliations
  • The University of Adelaide (AU)
  • University of South Australia (AU)
Corresponding author
Gibson, Mark A.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2006-03
Volume
281
Issue
12
Pages
7816-7824
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.m511316200
OpenAlex
W2062173898
Cited by
89
References
40
Citations by year
2025: 2 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 6 · 2020: 6 · 2019: 3 · 2018: 6 · 2017: 3 · 2016: 7 · 2015: 3 · 2014: 6 · 2013: 6 · 2012: 8
FWCI
2.48
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
Funders
  • Medical Research Council
  • National Health and Medical Research Council
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
  • Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
Keywords
biglycan, decorin, small leucine-rich proteoglycans, collagen VI, ternary complex, proteoglycan binding, binding affinity, glycosaminoglycan side chains, globular domain, high molecular weight complexes, extracellular matrix assembly, alpha-dystroglycan
MeSH terms
betaIG-H3 Protein, Binding Sites, Collagen, Dose-Response Relationship, Drug, Electrolytes, Electrophoresis, Polyacrylamide Gel, Glycosaminoglycans, Humans, Kinetics, Light, Mutation, Pepsin A, Polysaccharides, Protein Binding, Proteoglycans, Scattering, Radiation, Temperature, Time Factors, Transforming Growth Factor beta, Extracellular Matrix Proteins, Protein Structure, Tertiary, Collagen Type VI, Macromolecular Substances, Immunoprecipitation, Decorin, Biglycan

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