Target type: biologicalprocess
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a fibronectin fibril. [GOC:dph, GOC:TermGenie, PMID:20690820]
Fibronectin fibril organization is a complex process that plays a crucial role in the formation and maintenance of the extracellular matrix (ECM). This process involves a series of steps, including:
1. **Fibronectin secretion:** Fibronectin is a large, multidomain glycoprotein that is synthesized and secreted by cells.
2. **Fibronectin binding to the cell surface:** Secreted fibronectin molecules bind to cell surface integrins, which are transmembrane receptors that mediate cell-matrix interactions.
3. **Fibronectin assembly into fibrils:** The initial binding of fibronectin to the cell surface triggers a conformational change in the molecule, exposing cryptic binding sites that promote self-assembly. Fibronectin molecules then associate with each other in a head-to-tail fashion, forming elongated, rope-like structures called fibrils.
4. **Fibronectin fibril elongation and stabilization:** As fibrils elongate, they become stabilized by cross-linking interactions between fibronectin molecules, as well as by interactions with other ECM components, such as collagen and proteoglycans.
5. **Fibril organization and alignment:** Fibronectin fibrils are often organized into a network of interconnected fibers that provide structural support to tissues. This organization is influenced by cellular forces, such as cell migration and contraction, as well as by mechanical stresses applied to the ECM.
6. **Fibril turnover and remodeling:** Fibronectin fibrils are not static structures but are constantly being remodeled and turned over. This process involves the degradation of old fibrils by matrix metalloproteinases (MMPs) and the synthesis of new fibrils by cells.
The formation of fibronectin fibrils is a tightly regulated process that is essential for tissue development, wound healing, and cell migration. Defects in fibronectin fibril organization can lead to various diseases, including cancer, fibrosis, and cardiovascular disease.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Lysyl oxidase homolog 3 | A lysyl oxidase homolog 3 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P58215] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| pyrithione | pyrithione : A pyridinethione that is pyridine-2(1H)-thione in which the hydrogen attached to the nitrogen is replaced by a hydroxy group. It is a Zn(2+) ionophore; the zinc salt is used as an antifungal and antibacterial agent. pyrithione: split from cephalosporin molecule; some metal complexes of this have fumarate reductase inhibitory activity and may be useful against trypanosomes; RN given refers to parent cpd; structure | monohydroxypyridine; pyridinethione | ionophore |
| aminopropionitrile | Aminopropionitrile: Reagent used as an intermediate in the manufacture of beta-alanine and pantothenic acid. | aminopropionitrile | antineoplastic agent; antirheumatic drug; collagen cross-linking inhibitor; plant metabolite |
| disulfiram | organic disulfide; organosulfur acaricide | angiogenesis inhibitor; antineoplastic agent; apoptosis inducer; EC 1.2.1.3 [aldehyde dehydrogenase (NAD(+))] inhibitor; EC 3.1.1.1 (carboxylesterase) inhibitor; EC 3.1.1.8 (cholinesterase) inhibitor; EC 5.99.1.2 (DNA topoisomerase) inhibitor; ferroptosis inducer; fungicide; NF-kappaB inhibitor | |
| thiram | thiram : An organic disulfide that results from the formal oxidative dimerisation of N,N-dimethyldithiocarbamic acid. It is widely used as a fungicidal seed treatment. Thiram: A dithiocarbamate chemical, used commercially in the rubber processing industry and as a fungicide. In vivo studies indicate that it inactivates the enzyme GLUTATHIONE REDUCTASE. It has mutagenic activity and may induce chromosomal aberrations. | organic disulfide | antibacterial drug; antifungal agrochemical; antiseptic drug |