Jan 5, 2002

Chondrogenic activity of the heparan sulfate proteoglycan perlecan maps to the N-terminal domain I

Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research
Margaret M FrenchD D Carson

Abstract

C3H10T1/2 cells differentiate along a chondrogenic pathway when plated onto the extracellular matrix (ECM) protein perlecan (Pln). To identify the region(s) within the large Pln molecule that provides a differentiation signal, recombinant Pln-sequence-based polypeptides representing distinct structural domains were assayed for their ability to promote chondrogenesis in C3H10T1/2 cells. Five distinct domains, along with structural variations, were tested. The N-terminal domain I was tested in two forms (IA and IB) that contain only heparan sulfate (HS) chains or both HS and chondroitin sulfate (CS) chains, respectively. A mutant form of domain I lacking attachment sites for both HS and CS (Pln I(mut)) was tested also. Other constructs consecutively designated Pln domains II, III(A-C), IV(A,B), and V(A,B) were used to complete the structure-function analysis. Cells plated onto Pln IA or Pln IB but no other domain rapidly assembled into cellular aggregates of 40-120 microm on average. Aggregate formation was dependent on the presence of glycosaminoglycan (GAG) chains, because Pln I-based polypeptides lacking GAG chains either by enzymatic removal or mutation of HS/CS attachment sites were inactive. Aggregates formed on GAG-bearing...Continue Reading

  • References25
  • Citations32

References

Mentioned in this Paper

Chondroitin Sulfate, Zinc Salt
Glycosaminoglycans
Proteins, Recombinant DNA
Tertiary Protein Structure
Mucopolysaccharidosis III
Chondrocyte
Chondrogenesis
Cell Differentiation Process
Heparitin Sulfate
Hspg2 protein, rat

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