ISSLS Prize Winner: Effect of Link Protein Peptide on Human Intervertebral Disc Cells
Explore this paper's citation graph
Summary
LPP could have value in stimulating the growth and regeneration of degenerated discs with less concern of creating unwanted bone and has relatively little osteoinductive effect compared with BMP2 and BMP7.
- Type
- article
- Published
- 2013-08-01
- Cited by
- 22
- References
- 27
- OpenAlex
- https://openalex.org/W1966906374
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:44967032
Keywords
Aggrecan, Proteoglycan, Glycosaminoglycan, Extracellular matrix, Downregulation and upregulation
References
- Structure of the complex between hyaluronic acid, the hyaluronic acid-binding region, and the link protein of proteoglycan aggregates from the swarm rat chondrosarcoma.
- Biosynthesis of cartilage proteoglycan and link protein.
- Intradiscal Administration of Osteogenic Protein-1 Increases Intervertebral Disc Height and Proteoglycan Content in the Nucleus Pulposus in Normal Adolescent Rabbits
- Assembly of newly synthesized proteoglycan and link protein into aggregates in cultures of chondrosarcoma chondrocytes.
- Intervertebral Disk Degeneration and Emerging Biologic Treatments
- Recombinant Human Osteogenic Protein-1 Upregulates Proteoglycan Metabolism of Human Anulus Fibrosus and Nucleus Pulposus Cells
- BMP-2 and CDMP-2: stimulation of chondrocyte production of proteoglycan
- The macromolecular characteristics of cartilage proteoglycans do not change when synthesis is up-regulated by link protein peptide.
- Molecular therapy of the intervertebral disc
- Aggrecan degradation in human articular cartilage explants is mediated by both ADAMTS-4 and ADAMTS-5.
- Biologic Solutions for Degenerative Disk Disease
- Osteogenic protein-1 is most effective in stimulating nucleus pulposus and annulus fibrosus cells to repair their matrix after chondroitinase ABC-induced in vitro chemonucleolysis.
- Biological repair of the degenerated intervertebral disc by the injection of growth factors
- An N-terminal peptide from link protein can stimulate biosynthesis of collagen by human articular cartilage.
- A synthetic peptide of link protein stimulates the biosynthesis of collagens II, IX and proteoglycan by cells of the intervertebral disc
- An N-terminal peptide from link protein stimulates proteoglycan biosynthesis in human articular cartilage in vitro.
- Effect of Synthetic Link N Peptide on the Expression of Type I and Type II Collagens in Human Intervertebral Disc Cells
- Restoration of Disc Height Loss by Recombinant Human Osteogenic Protein-1 Injection Into Intervertebral Discs Undergoing Degeneration Induced by an Intradiscal Injection of Chondroitinase ABC
- A critical review of recombinant human bone morphogenetic protein-2 trials in spinal surgery: emerging safety concerns and lessons learned.
- Pathophysiology of the human intervertebral disc.
Cited by
- Link N and Mesenchymal Stem Cells Can Induce Regeneration of the Early Degenerate Intervertebral Disc
- Best paper NASS 2013: link-N can stimulate proteoglycan synthesis in the degenerated human intervertebral discs.
- Future advances for treating lumbar disc herniation and degeneration: Nucleus replacement, annular repair, and biologics
- Regenerative medicine: Rebuilding the backbone
- Intervertebral disc regeneration: do nutrients lead the way?
- Link-N is Cleaved by Human Annulus Fibrosus Cells Generating a Fragment with Retained Biological Activity
- Differences in calcification and osteogenic potential of herniated discs according to the severity of degeneration based on Pfirrmann grade: a cross-sectional study
- A Global Pictorial Assessment of theIntervertebral Disc Cell in Several SpeciesReveals a Remarkable Biodiversity in this Cell Type which should be taken into Account in Experimental Studies on Intervertebral Disc Repair
- Short Link N Stimulates Intervertebral Disc Repair in a Novel Long-Term Organ Culture Model that Includes the Bony Vertebrae
- The Effect of Link N on Mesenchymal Stem Cell Under IL-1β Stimulation
- Link protein N-terminal peptide and fullerol promote matrix production and decrease degradation enzymes in rabbit annulus cells
- Molecular Biology and Interactions in Intervertebral Disc Development, Homeostasis, and Degeneration, with Emphasis on Future Therapies: A Systematic Review
- Link N as a therapeutic agent for discogenic pain
- Nutrient supply and nucleus pulposus cell function: effects of the transport properties of the cartilage endplate and potential implications for intradiscal biologic therapy
- Exogenous Delivery of Link N mRNA into Chondrocytes and MSCs—The Potential Role in Increasing Anabolic Response
- Matrix modification for enhancing the transport properties of the human cartilage endplate to improve disc nutrition
- Nanostructured TiC Layer is Highly Suitable Surface for Adhesion, Proliferation and Spreading of Cells
- LIPUS far-field exposimetry system for uniform stimulation of tissues in-vitro: development and validation with bovine intervertebral disc cells
- Mechanisms and clinical implications of intervertebral disc calcification
- Drug retention after intradiscal administration
Related papers
- TIMP-3 inhibits aggrecan breakdown in pig articular cartilage stimulated with IL-1
- ADAMTS‐4 and ADAMTS‐5 sequestration and activity in chondrocyte‐agarose cultures
- ADAMTS‐5: A difficult teenager turning 20
- Aggrecanase and Aggrecan Degradation in Osteoarthritis: A Review
- LRP‐1‐mediated endocytosis regulates extracellular activity of ADAMTS‐5 in articular cartilage
- IL-1β promotes ADAMTS enzyme-mediated aggrecan degradation through NF-κB in human intervertebral disc
- Expression of ADAMTS-7 and ADAMTS-12 in the nucleus pulposus during degeneration of rat caudal intervetebral disc.
- Rat tail static compression model mimics extracellular matrix metabolic imbalances of matrix metalloproteinases, aggrecanases, and tissue inhibitors of metalloproteinases in intervertebral disc degeneration
- Matrix synthesis and degradation in human intervertebral disc degeneration.
- Inhibition of P2Y11R ameliorated TNF-α-induced degradation of extracellular matrix in human chondrocytic SW1353 cells.