Related Experiment Video
Updated: Aug 8, 2026
09:25
A Protocol to Acquire the Degenerative Tenocyte from Humans
Published on: June 9, 2018
Analysis of structure and function of tenascin-C
Jakub Pas1, Eliza Wyszko, Katarzyna Rolle
1Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12, 61-704 Poznan, Poland.
Summary
Tenascin-C, a large extracellular matrix glycoprotein, was analyzed using bioinformatics and molecular modeling. This study identified tenascin-C
Area of Science:
- Biochemistry
- Molecular Biology
- Bioinformatics
Background:
- Tenascin-C is a large, multidomain extracellular matrix glycoprotein.
- Its monomer size (180-250 kDa) varies due to alternative splicing of fibronectin repeats.
- Understanding tenascin-C's structure and function is crucial for its potential applications.
Purpose of the Study:
- To conduct a detailed bioinformatic and molecular modeling analysis of tenascin-C organization.
- To investigate the potential role of tenascin-C in protein-protein interactions and stress response.
- To evaluate tenascin-C expression levels in human tumor tissues.
Main Methods:
- Bioinformatic analysis of the tenascin-C gene.
- Molecular modeling procedures for structural analysis.
- Polyacrylamide gel electrophoresis (PAGE), RT/PCR, and microarray data analysis.
Main Results:
- Heat shock protein 33 was detected in the tenascin-C N-terminal domain, suggesting roles in protein interactions and stress response.
- The number of fibronectin type III-like and epidermal growth factor-like repeats were corrected to 15 and 14, respectively.
- Elevated tenascin-C levels were observed in human brain, intestine, and breast tumor tissues.
Conclusions:
- Tenascin-C exhibits altered expression in various human tumors.
- The findings suggest tenascin-C's potential as a tumor marker.
- Tenascin-C may represent a novel drug target for cancer therapy.
Related Concept Videos
01:26Tension Response at Adherens Junctions
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
01:23Catenins
Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
01:56Structural Protein Function
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 form...
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 form...
01:56Structural Protein Function
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 form...
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 form...
01:08The Sarcomere
A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each myosin...
Each myosin...
01:25Structure of Cadherins
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...