Related Experiment Video
Updated: Jul 13, 2026
09:20
Laser Capture Microdissection of Mouse Embryonic Cartilage and Bone for Gene Expression Analysis
Published on: December 18, 2019
S100A8/S100A9 and their association with cartilage and bone
H Zreiqat1, C R Howlett, S Gronthos
1Biomaterials and Tissue Engineering Research Unit, Biomedical Engineering, School of AMME, The University of Sydney, Sydney, NSW, Australia. hzreiqat@usyd.edu.au
Journal of Molecular Histology
|July 20, 2007
Summary
S100A8 and S100A9 proteins are found in bone and cartilage cells. These proteins may play a role in cartilage calcification and bone formation, as well as regulating bone resorption.
Area of Science:
- Biochemistry
- Cell Biology
- Orthopedics
Background:
- S100A8 and S100A9 are calcium-binding proteins involved in inflammatory diseases.
- S100A9 is linked to calcification in atherosclerosis.
- Their role in bone and cartilage is not fully understood.
Purpose of the Study:
- To investigate the expression and potential roles of S100A8 and S100A9 in bone and cartilage.
- To explore their involvement in cellular differentiation and matrix calcification.
Main Methods:
- Immunohistochemical analysis of S100A8 and S100A9 expression in murine and human bone and cartilage tissues.
- Localization of proteins in various cell types including preosteogenic cells, osteoblasts, osteoclasts, and chondrocytes.
Main Results:
- S100A8 and S100A9 are expressed in osteoclasts and hypertrophic chondrocytes.
- S100A8 is present in preosteogenic cells, while both proteins show weak expression in osteoblasts.
- S100A9 is found in the vascular osteogenic tissue during endochondral ossification.
Conclusions:
- S100A8 and S100A9 are expressed in specific bone and cartilage cell types.
- These proteins may contribute to cartilage matrix calcification and bone formation.
- They might also regulate redox processes in bone resorption.
Related Concept Videos
01:27Growth 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...
01:23Glycosaminoglycans
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
01:09Spongy 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...
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...
01:24Bone Formation by Endochondral Ossification
Bone formation, or ossification, begins around the sixth to seventh week of embryonic development. Most bones develop from a cartilaginous template through the process of endochondral ossification. Cartilage formation begins when clusters of mesenchymal cells differentiate into chondrocytes. These chondrocytes proliferate rapidly and secrete an extracellular matrix that becomes encased in a membrane called the perichondrium. The resulting cartilage model provides a template that resembles the...
01:11Fibril-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...
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...
01:20Introduction to the Skeletal System
The skeletal system is the central framework of the body, consisting of different connective tissues: bones, cartilage, tendons, and ligaments.
Components of the Skeletal System
Bone, or osseous tissue, is a hard connective tissue that forms an internal support structure for the human body. Bones shield vulnerable organs and soft tissue from external forces. For example, the vertebral bones protect and support the spinal cord.
Cartilage, a semi-rigid connective tissue found in regions such as...
Components of the Skeletal System
Bone, or osseous tissue, is a hard connective tissue that forms an internal support structure for the human body. Bones shield vulnerable organs and soft tissue from external forces. For example, the vertebral bones protect and support the spinal cord.
Cartilage, a semi-rigid connective tissue found in regions such as...