Related Experiment Video
Updated: Dec 27, 2025
09:14
Tracking Hypoxic Signaling within Encapsulated Cell Aggregates
Published on: December 16, 2011
10.9K
Is Desmin Propensity to Aggregate Part of its Protective Function?
Sonia R Singh1,2, Hikmet Kadioglu3, Krishna Patel3
1Institute of Experimental Pharmacology and Toxicology, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany.
Cells
|February 26, 2020
Summary
Desmin protein aggregates in heart failure (HF) may protect against acute stress but contribute to disease long-term. Understanding desmin
Area of Science:
- Muscle cell biology
- Cardiovascular research
- Protein biochemistry
Background:
- Desmin is a key intermediate filament (IF) protein in muscle cytoskeletons.
- Accumulation of misfolded desmin is a hallmark of heart failure (HF).
- Therapeutic reversal of desmin alterations suggests a causal role in HF development.
Purpose of the Study:
- To review the function of IFs, particularly desmin.
- To propose a model for desmin's role in stress protection.
- To explore desmin's contribution to heart failure.
Main Methods:
- Literature review of intermediate filament function.
- Analysis of desmin's role in cardiac stress.
- Proposal of an evolutionary model for desmin aggregation.
Main Results:
- IFs are known to protect cells from stress, but mechanisms are unclear.
- The heart's cyclic contraction makes it a model for IF function under mechanical stress.
- Desmin aggregation may dissipate mechanical and redox stress.
Conclusions:
- Desmin misfolding might protect against acute injury.
- Sustained desmin aggregate accumulation can impair proteostasis.
- This aggregation may contribute to heart failure pathogenesis.
Related Concept Videos
01:05Desmosomes
7.0K
The term desmosome derives from the Greek words "desmo" and "soma" meaning "adhesion bodies." This structure was first observed during the late 1800s and described as small, dense nodules in the epidermis. Desmosomes are button-like structures that help form an interlinked network of intermediate filaments across the cells. These junctions are essential to hold cells together under mechanical stress and to maintain tissue integrity. Desmosomes are multi-protein...
7.0K
03:03Amyloid Fibrils
11.5K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
11.5K
01:11Fibril-associated Collagen
3.2K
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...
3.2K
01:03Anchoring Junctions
4.7K
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:...
4.7K
02:41Protein Complex Assembly
16.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.5K
00:55Laminins are the Adhesive Proteins of Basal Lamina
2.9K
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...
2.9K