Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

The Bone Matrix

The Bone Matrix

Bone contains a relatively small number of cells entrenched in a matrix of collagen fibers that provide an adherent surface for inorganic salt crystals. Both components of the matrix, organic and inorganic, contribute to the unusual properties of bone. Without collagen, bones would be brittle and shatter easily. Without mineral crystals, bones would flex and provide little support. This can be observed by an experiment: when the minerals of a bone are dissolved by soaking the bone in acid or...

Essential Minerals for Bone Health

Essential Minerals for Bone Health

The minerals contained in all of the food we consume are essential for our organ systems. However, certain essential minerals, such as calcium, phosphorus, magnesium, manganese, and fluoride, largely affect bone health.
Calcium and Phosphorus
Calcium is a critical component of bones, especially in the form of calcium phosphate and calcium carbonate. Since the body cannot make calcium, it must be obtained from the diet. However, calcium cannot be absorbed from the small intestine without...

Fibril-associated Collagen

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...

Spongy Bone

Spongy Bone

All bones comprise an outer layer of compact bone, and an interior made up of spongy bone tissue, also called cancellous or trabecular bone. In long bones, spongy bone tissue is mainly found in the interior of the epiphyses (broad ends of the bone).
Spongy bone is more porous, and less dense compared to compact bone. It is composed of concentric lamellae that are arranged irregularly to form the trabecular network. In some bones, the spaces between trabeculae contain red marrow, where...

Bone Remodeling

Bone Remodeling

Bone remodeling is a continuous and balanced process of bone resorption by osteoclasts and bone formation by osteoblasts. In adults, it helps maintain bone mass and calcium homeostasis. While mechanical stress can stimulate turnover as part of the normal maintenance and reparative process, several hormones also regulate bone remodeling.

Growth of Cartilage and Bone Tissue

Growth of Cartilage and Bone Tissue

Chondrocytes form a temporary cartilaginous model by dividing and secreting a thick gel-like extracellular matrix. Once the chondrocytes undergo programmed cell death, osteoblasts enter the site of the cartilaginous model. The process of replacing the temporary cartilaginous model with bone in an ordered manner is called endochondral ossification. In endochondral ossification, not all of the cartilage is replaced by bone tissue. Some cartilage that performs a protective and supportive function...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Liver-derived plasminogen mediates muscle stem cell expansion during caloric restriction through the plasminogen receptor Plg-R<sub>KT</sub>.

Cell reports·2024

Same author

Multi-omic rejuvenation and life span extension on exposure to youthful circulation.

Nature aging·2023

Same author

Editorial: The immune system and inflammation in musculoskeletal health, aging, and disease.

Frontiers in immunology·2023

Same author

Biological age is increased by stress and restored upon recovery.

Cell metabolism·2023

Same author

The Role of Urinary Modulators in the Development of Infectious Kidney Stones.

Journal of endourology·2022

Same author

Osteopontin phosphopeptide mitigates calcium oxalate stone formation in a Drosophila melanogaster model.

Urolithiasis·2022

Search research articles

Related Experiment Video

Updated: Jul 3, 2026

Synthesis of Graphene-Hydroxyapatite Nanocomposites for Potential Use in Bone Tissue Engineering

Synthesis of Graphene-Hydroxyapatite Nanocomposites for Potential Use in Bone Tissue Engineering

Published on: July 27, 2022

Bone sialoprotein-collagen interaction promotes hydroxyapatite nucleation.

Gurpreet S Baht¹, Graeme K Hunter, Harvey A Goldberg

¹CIHR Group in Skeletal Development and Remodeling, Department of Biochemistry and Schulich Dentistry, Schulich School of Medicine & Dentistry, University of Western Ontario, London, Ontario, Canada N6A 5C1.

Matrix Biology : Journal of the International Society for Matrix Biology

|July 16, 2008

Summary

This summary is machine-generated.

Bone sialoprotein (BSP) binds to native type I collagen via hydrophobic interactions, enhancing hydroxyapatite (HA) nucleation. This interaction is crucial for bone mineralization, highlighting a cooperative effect between BSP and collagen.

More Related Videos

Rapid Mix Preparation of Bioinspired Nanoscale Hydroxyapatite for Biomedical Applications

Rapid Mix Preparation of Bioinspired Nanoscale Hydroxyapatite for Biomedical Applications

Published on: February 23, 2017

Distinctive Capillary Action by Micro-channels in Bone-like Templates can Enhance Recruitment of Cells for Restoration of Large Bony Defect

Distinctive Capillary Action by Micro-channels in Bone-like Templates can Enhance Recruitment of Cells for Restoration of Large Bony Defect

Published on: September 11, 2015

Related Experiment Videos

Last Updated: Jul 3, 2026

Synthesis of Graphene-Hydroxyapatite Nanocomposites for Potential Use in Bone Tissue Engineering

Synthesis of Graphene-Hydroxyapatite Nanocomposites for Potential Use in Bone Tissue Engineering

Published on: July 27, 2022

Rapid Mix Preparation of Bioinspired Nanoscale Hydroxyapatite for Biomedical Applications

Rapid Mix Preparation of Bioinspired Nanoscale Hydroxyapatite for Biomedical Applications

Published on: February 23, 2017

Distinctive Capillary Action by Micro-channels in Bone-like Templates can Enhance Recruitment of Cells for Restoration of Large Bony Defect

Distinctive Capillary Action by Micro-channels in Bone-like Templates can Enhance Recruitment of Cells for Restoration of Large Bony Defect

Published on: September 11, 2015

Area of Science:

Biomineralization
Bone Biology
Protein-Collagen Interactions

Background:

Hydroxyapatite (HA) crystal deposition on type I collagen scaffolds in bone is not fully understood.
Bone sialoprotein (BSP) is an acidic phosphoprotein involved in mineralized tissue formation, binding collagen and nucleating HA.

Purpose of the Study:

To elucidate the mechanism of the interaction between bone sialoprotein (BSP) and type I collagen.
To understand the role of this interaction in hydroxyapatite (HA) nucleation during bone mineralization.

Main Methods:

Solid-phase binding assays and affinity chromatography were used to characterize BSP-collagen interactions.
Binding affinities were measured for native, heat-denatured, and pepsin-treated type I collagen.
Hydroxyapatite (HA) nucleation assays were performed using reconstituted fibrillar collagen and agarose gels.

Main Results:

Recombinant BSP (rBSP) exhibited high affinity for native triple-helical type I collagen (K(D) ≈ 13 nM), with lower affinity for heat-denatured collagen (K(D) ≈ 44 nM).
Collagen telopeptides are not involved in rBSP binding; hydrophobic interactions primarily stabilize the binding.
rBSP demonstrated a ten-fold greater HA nucleation potency in fibrillar collagen gels compared to agarose gels.

Conclusions:

Optimal bone sialoprotein (BSP) binding to type I collagen requires native triple-helical structure and is mediated by hydrophobic interactions.
The binding of BSP to collagen enhances its hydroxyapatite nucleation potency.
A cooperative effect between BSP and collagen is implied in the process of bone mineral formation.