Related Experiment Video
Updated: Nov 21, 2025
06:56
Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
Published on: September 28, 2020
1.2K
Fibronectin assembly regulates lumen formation in breast acini
Carina Magdaleno1, Trenton House1, Jogendra S Pawar1
1Department of Chemistry and Biochemistry, Northern Arizona University, Flagstaff, Arizona, USA.
Journal of Cellular Biochemistry
|January 13, 2021
Summary
Fibronectin fibril formation in epithelial cells decreases under hypoxia, reducing cell migration. Disrupting these fibrils promotes lumen filling and loss of polarity, mimicking pre-invasive breast changes.
Area of Science:
- Extracellular matrix (ECM) biology
- Cancer cell biology
- Tumor microenvironment research
Background:
- Fibronectin (FN) fibrils in the ECM influence cancer progression.
- Epithelial cell FN matrix roles in cancer are less understood.
- Hypoxia in tumors affects ECM organization.
Purpose of the Study:
- Investigate epithelial cell FN matrix formation and function.
- Determine the impact of hypoxia on epithelial FN fibrils.
- Elucidate the role of epithelial FN fibrils in breast acini development.
Main Methods:
- Utilized the MCF10 breast epithelial cell line series (normal to invasive).
- Studied FN fibril formation under hypoxic conditions.
- Assessed 3D acinar growth and apicobasal polarity after FN fibril disruption.
Main Results:
- Hypoxia decreased FN fibril formation and epithelial cell migration.
- Disruption of FN fibrils in normal cells induced lumen filling.
- Fibril disruption led to loss of apicobasal polarity, resembling pre-invasive cells.
Conclusions:
- Epithelial FN fibril changes are critical in breast acini lumen clearing.
- Fibril-mediated changes contribute to maintaining untransformed growth characteristics.
- This study links epithelial FN matrix dynamics to early breast cancer development.
Related Concept Videos
01:25Fibronectins Connect Cells with ECM
3.0K
Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
3.0K
01:11Formation of Higher-order Actin Filaments
3.3K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
The high-order actin...
3.3K
00:55Laminins are the Adhesive Proteins of Basal Lamina
2.7K
Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
2.7K
01:03Anchoring Junctions
4.5K
Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
4.5K
01:56Structural Protein Function
29.3K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
29.3K
01:24Adherens Junctions
5.6K
Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types – adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
Adherens Junctions are Dynamic
5.6K