Interaction of osteogenin, a heparin binding bone morphogenetic protein, with type IV collagen

Vishwas M. Paralkar, Arvind K N Nandedkar, Richard H. Pointer, Hynda K. Kleinman, A Hari Reddi

Research output: Contribution to journalArticle

145 Citations (Scopus)

Abstract

Osteogenin, an extracellular matrix component of bone, is a heparin binding differentiation factor that initiates endochondral bone formation in rats when implanted subcutaneously with an insoluble collagenous matrix. We have examined the interaction of osteogenin with various extracellular matrix components including basement membranes. Osteogenin, purified from bovine bone, binds avidly to type IV collagen and to a lesser extent to both type I and IX collagens. Osteogenin binds equally well to both native and denatured type IV collagen. Both α1 and α2 chains of type IV collagen are recognized by osteogenin. Osteogenin binds to a collagen IV affinity column, and is eluted by 6.0 M urea with 1 M NaCl, pH 7.4, and the eluate contained the osteogenic activity as demonstrated in vivo. Binding of osteogenin to collagen IV is not influenced by either laminin or fibronectin. These results imply that osteogenin binding to extracellular matrix components including collagens I and IV and heparin may have physiological relevance, and such interactions may modulate its local action.

Original languageEnglish (US)
Pages (from-to)17281-17284
Number of pages4
JournalJournal of Biological Chemistry
Volume265
Issue number28
StatePublished - Oct 5 1990
Externally publishedYes

Fingerprint

Bone Morphogenetic Protein 3
Bone Morphogenetic Proteins
Collagen Type IV
Heparin
Carrier Proteins
Extracellular Matrix
Bone
Collagen
Collagen Type IX
Bone and Bones
Laminin
Collagen Type I
Fibronectins
Basement Membrane
Osteogenesis
Urea
Rats

ASJC Scopus subject areas

  • Biochemistry

Cite this

Paralkar, V. M., Nandedkar, A. K. N., Pointer, R. H., Kleinman, H. K., & Reddi, A. H. (1990). Interaction of osteogenin, a heparin binding bone morphogenetic protein, with type IV collagen. Journal of Biological Chemistry, 265(28), 17281-17284.

Interaction of osteogenin, a heparin binding bone morphogenetic protein, with type IV collagen. / Paralkar, Vishwas M.; Nandedkar, Arvind K N; Pointer, Richard H.; Kleinman, Hynda K.; Reddi, A Hari.

In: Journal of Biological Chemistry, Vol. 265, No. 28, 05.10.1990, p. 17281-17284.

Research output: Contribution to journalArticle

Paralkar, VM, Nandedkar, AKN, Pointer, RH, Kleinman, HK & Reddi, AH 1990, 'Interaction of osteogenin, a heparin binding bone morphogenetic protein, with type IV collagen', Journal of Biological Chemistry, vol. 265, no. 28, pp. 17281-17284.
Paralkar, Vishwas M. ; Nandedkar, Arvind K N ; Pointer, Richard H. ; Kleinman, Hynda K. ; Reddi, A Hari. / Interaction of osteogenin, a heparin binding bone morphogenetic protein, with type IV collagen. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 28. pp. 17281-17284.
@article{5b0f60c925004bb38b74b66c67a6dcef,
title = "Interaction of osteogenin, a heparin binding bone morphogenetic protein, with type IV collagen",
abstract = "Osteogenin, an extracellular matrix component of bone, is a heparin binding differentiation factor that initiates endochondral bone formation in rats when implanted subcutaneously with an insoluble collagenous matrix. We have examined the interaction of osteogenin with various extracellular matrix components including basement membranes. Osteogenin, purified from bovine bone, binds avidly to type IV collagen and to a lesser extent to both type I and IX collagens. Osteogenin binds equally well to both native and denatured type IV collagen. Both α1 and α2 chains of type IV collagen are recognized by osteogenin. Osteogenin binds to a collagen IV affinity column, and is eluted by 6.0 M urea with 1 M NaCl, pH 7.4, and the eluate contained the osteogenic activity as demonstrated in vivo. Binding of osteogenin to collagen IV is not influenced by either laminin or fibronectin. These results imply that osteogenin binding to extracellular matrix components including collagens I and IV and heparin may have physiological relevance, and such interactions may modulate its local action.",
author = "Paralkar, {Vishwas M.} and Nandedkar, {Arvind K N} and Pointer, {Richard H.} and Kleinman, {Hynda K.} and Reddi, {A Hari}",
year = "1990",
month = "10",
day = "5",
language = "English (US)",
volume = "265",
pages = "17281--17284",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "28",

}

TY - JOUR

T1 - Interaction of osteogenin, a heparin binding bone morphogenetic protein, with type IV collagen

AU - Paralkar, Vishwas M.

AU - Nandedkar, Arvind K N

AU - Pointer, Richard H.

AU - Kleinman, Hynda K.

AU - Reddi, A Hari

PY - 1990/10/5

Y1 - 1990/10/5

N2 - Osteogenin, an extracellular matrix component of bone, is a heparin binding differentiation factor that initiates endochondral bone formation in rats when implanted subcutaneously with an insoluble collagenous matrix. We have examined the interaction of osteogenin with various extracellular matrix components including basement membranes. Osteogenin, purified from bovine bone, binds avidly to type IV collagen and to a lesser extent to both type I and IX collagens. Osteogenin binds equally well to both native and denatured type IV collagen. Both α1 and α2 chains of type IV collagen are recognized by osteogenin. Osteogenin binds to a collagen IV affinity column, and is eluted by 6.0 M urea with 1 M NaCl, pH 7.4, and the eluate contained the osteogenic activity as demonstrated in vivo. Binding of osteogenin to collagen IV is not influenced by either laminin or fibronectin. These results imply that osteogenin binding to extracellular matrix components including collagens I and IV and heparin may have physiological relevance, and such interactions may modulate its local action.

AB - Osteogenin, an extracellular matrix component of bone, is a heparin binding differentiation factor that initiates endochondral bone formation in rats when implanted subcutaneously with an insoluble collagenous matrix. We have examined the interaction of osteogenin with various extracellular matrix components including basement membranes. Osteogenin, purified from bovine bone, binds avidly to type IV collagen and to a lesser extent to both type I and IX collagens. Osteogenin binds equally well to both native and denatured type IV collagen. Both α1 and α2 chains of type IV collagen are recognized by osteogenin. Osteogenin binds to a collagen IV affinity column, and is eluted by 6.0 M urea with 1 M NaCl, pH 7.4, and the eluate contained the osteogenic activity as demonstrated in vivo. Binding of osteogenin to collagen IV is not influenced by either laminin or fibronectin. These results imply that osteogenin binding to extracellular matrix components including collagens I and IV and heparin may have physiological relevance, and such interactions may modulate its local action.

UR - http://www.scopus.com/inward/record.url?scp=0025183767&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025183767&partnerID=8YFLogxK

M3 - Article

C2 - 2211625

AN - SCOPUS:0025183767

VL - 265

SP - 17281

EP - 17284

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 28

ER -