Related Experiment Video
Updated: Apr 15, 2026

07:51
Differentiating Chondrocytes from Peripheral Blood-derived Human Induced Pluripotent Stem Cells
Published on: July 18, 2017
9.7K
Collagen II regulates chondroycte integrin expression profile and differentiation
Wei Xin1, Juliane Heilig, Mats Paulsson
1Central Laboratory, Shandong Provincial Hospital affiliated to Shandong University , Jinan , China .
Connective Tissue Research
|March 25, 2015
Summary
Chondrocytes adapt to the absence of collagen II by producing collagen I and altering integrin expression. This impacts cell signaling and differentiation, highlighting collagen II
Area of Science:
- Biochemistry
- Cell Biology
- Genetics
Background:
- Collagen II is the primary fibril-forming collagen in cartilage, essential for skeletal development.
- COL2A1 gene mutations cause osteochondrodysplasias in humans, but chondrocyte responses to collagen II absence are poorly understood.
Purpose of the Study:
- To investigate chondrocyte responses to the absence of collagen II in their extracellular matrix.
- To elucidate the role of collagen II in maintaining chondrocyte differentiation and signaling pathways.
Main Methods:
- Primary mouse chondrocytes were cultured and collagen II expression suppressed using siRNA targeting Col2α1.
- Gene and protein expression (integrins, matrix proteins) analyzed via RT-PCR and immunoblots.
- Chondrocyte differentiation and signaling pathways (Ihh/PTHrP) assessed by flow cytometry and RT-PCR.
Main Results:
- Chondrocytes produced collagen I in the absence of collagen II.
- Integrin expression profiles changed, and some collagen II binding partners were lost from the matrix.
- Alterations in the Indian hedgehog/parathyroid hormone-related protein (Ihh/PTHrP) pathway were observed, correlating with altered chondrocyte differentiation.
Conclusions:
- Collagen II is not essential for chondrocyte survival in vitro but crucial for maintaining chondrocyte differentiation.
- A crosstalk between the extracellular matrix and chondrocytes, mediated by integrins and the Ihh/PTHrP pathway, regulates differentiation.
Related Concept Videos
Fibril-associated Collagen
3.8K
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...
3.8K
Matrix Proteoglycans and Glycoproteins
5.7K
Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
5.7K
Collagens are the Major Structural Proteins of ECM
6.5K
Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
Connective tissue proper includes loose...
6.5K
Extracellular Matrix
6.7K
Unlike epithelial tissue, which is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. This extracellular matrix (ECM) is composed of fibrous proteins like collagen, elastin, and fibronectin in a ground substance consisting of interstitial fluid, cell adhesion proteins, and proteoglycans. The proteoglycans form a gel-like material in the spaces between cells and provide hydration, buffering, binding, and force...
6.7K
Type IV Collagen of Basal Lamina
3.4K
Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
A type IV collagen molecule has six alpha chains which can...
3.4K
Integrins
6.2K
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
6.2K

