GO:0030023 extracellular matrix constituent conferring elasticity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0030023 describes a molecular function: a component of the extracellular matrix that enables the matrix to recoil after transient stretching.
• Elasticity of the extracellular matrix is conferred mainly by elastin and associated microfibrillar proteins such as fibrillins and fibulins.
• The term is a molecular_function in the Gene Ontology, with synonyms including core extracellular matrix, core matrisome, and elastin.
• Defects in elastic fiber components are linked to Marfan syndrome and related connective tissue disorders.
• Studying this function requires integrating genomics, proteomics, imaging, and biomechanical assays.
• CRISPR-based models (knockout, point mutation, knock-in, overexpression) are powerful tools to dissect the causal roles of elastic matrix genes.
Description
The extracellular matrix (ECM) is not merely a passive scaffold; it actively determines tissue mechanics, cell signaling, and organ development. Among its many functions, the ability to stretch and then recoil is essential for tissues such as skin, lungs, and blood vessels. The Gene Ontology (GO) term GO:0030023, extracellular matrix constituent conferring elasticity, captures this specific molecular function: a component of the ECM that enables the matrix to recoil after transient stretching. This term is part of the molecular_function ontology and includes synonyms such as core extracellular matrix, core matrisome, and elastin. Understanding this function is critical because elastic fibers are complex supramolecular assemblies whose dysfunction underlies a range of human diseases, most notably Marfan syndrome and other connective tissue disorders. Research into GO:0030023 therefore spans biochemistry, genetics, and biomechanics, with direct relevance to developmental biology, aging, and regenerative medicine.
extracellular matrix constituent conferring elasticity At A Glance
| GO ID | GO:0030023 |
|---|---|
| GO term | extracellular matrix constituent conferring elasticity |
| Ontology | molecular_function |
| Synonym | core extracellular matrix, core matrisome, elastin |
| Definition | A component of the extracellular matrix that enables the matrix to recoil after transient stretching. |
| Major function | Provides elastic recoil to tissues such as skin, lungs, and blood vessels. |
| Related diseases | Marfan syndrome and other connective tissue disorders. |
| Key proteins | Elastin, fibrillins, fibulins, and other microfibril-associated proteins. |
What Is GO:0030023?
In simple terms, GO:0030023 defines a molecular function: any extracellular matrix component that allows the matrix to spring back after being stretched. According to the QuickGO definition, it is 'a component of the extracellular matrix that enables the matrix to recoil after transient stretching'. This function is typically performed by elastin and associated microfibrillar proteins, which form elastic fibers. The term is classified under molecular_function and carries synonyms including core extracellular matrix, core matrisome, and elastin.
Why Is extracellular matrix constituent conferring elasticity Important in Cell Biology?
GO:0030023 is important because elastic recoil is fundamental to the physiology of dynamic tissues. Without functional elastic fibers, tissues lose resilience, leading to pathologies such as aortic aneurysm, emphysema, and skin laxity. The term also serves as a hub for understanding how ECM components contribute to mechanical homeostasis and how mutations in elastic fiber genes cause disease. Moreover, because elastic fiber assembly is a complex process involving many proteins, studying GO:0030023 helps integrate knowledge across genetics, cell biology, and tissue engineering.
• Elastic recoil is essential for the normal function of arteries, lungs, and skin.
• Mutations in elastic fiber components cause Marfan syndrome and related disorders.
• The term helps annotate genes involved in ECM assembly and remodeling.
• It provides a framework for studying tissue mechanics in health and disease.
• Elastic fiber dysfunction is implicated in aging and degenerative conditions.
• Understanding this function can guide regenerative medicine and biomaterial design.
• It links molecular genetics to clinical phenotypes in connective tissue diseases.
• GO:0030023 is a key node for comparative genomics of ECM evolution.
Molecular Mechanism of extracellular matrix constituent conferring elasticity
Elastin and Microfibril Assembly
In simple terms: Elastin molecules are cross-linked together with the help of microfibrils to form a stretchy network.
Elastic fibers are composed of an amorphous core of cross-linked elastin surrounded by microfibrils. Microfibrils, which are primarily made of fibrillin-1 and associated proteins, serve as a scaffold for elastin deposition and are a cornerstone of the extracellular matrix. The assembly process involves secretion of tropoelastin, its alignment on microfibrils, and subsequent cross-linking by lysyl oxidase enzymes. This supramolecular organization confers the ability to recoil after transient stretching, as defined by GO:0030023.
Role of Fibrillins and Fibulins
In simple terms: Fibrillins and fibulins are proteins that help build and stabilize the elastic fiber network.
Fibrillins are large glycoproteins that polymerize into microfibrils and provide a template for elastin deposition. Mutations in fibrillin-1 cause Marfan syndrome, highlighting the importance of these proteins in elastic fiber function. Fibulins are another family of microfibril-associated proteins that contribute to elastic fiber integrity and are implicated in various connective tissue disorders. Together, these proteins ensure that the ECM can withstand repeated cycles of stretch and recoil.
Cross-linking and Maturation
In simple terms: Cross-links between elastin molecules make the network durable and elastic.
After deposition, tropoelastin monomers are cross-linked by lysyl oxidase to form a stable, insoluble network. This cross-linking is essential for the elastic properties of the matrix. Defects in cross-linking lead to fragile elastic fibers and impaired recoil, as seen in conditions like cutis laxa. The maturation of elastic fibers also involves interactions with other ECM components, such as proteoglycans, which can modulate fiber assembly and stability.
Regulation by Mechanical Forces
In simple terms: Cells sense mechanical forces and adjust elastic fiber production accordingly.
Mechanical stretch can influence the expression of elastin and microfibril genes through mechanotransduction pathways. For example, cyclic stretch in vascular smooth muscle cells upregulates elastin synthesis, helping to maintain tissue elasticity. This feedback loop ensures that elastic fiber assembly is matched to the mechanical demands of the tissue. Dysregulation of this process contributes to pathological remodeling in diseases such as hypertension and aneurysm.
Key Genes Involved in GO:0030023 extracellular matrix constituent conferring elasticity
The following genes encode proteins that are directly involved in the structure, assembly, or regulation of elastic fibers and thus contribute to the molecular function defined by GO:0030023.
| Gene | Major Role | Research Relevance |
|---|---|---|
| ELN | Elastin, the core component of elastic fibers | Mutations cause supravalvular aortic stenosis and cutis laxa; key for elastic fiber research |
| FBN1 | Fibrillin-1, major microfibril component | Mutations cause Marfan syndrome; central to elastic fiber assembly |
| FBN2 | Fibrillin-2, microfibril component | Mutations cause congenital contractural arachnodactyly; involved in early elastic fiber development |
| FBLN5 | Fibulin-5, microfibril-associated protein | Mutations cause cutis laxa; important for elastic fiber integrity |
| FBLN4 | Fibulin-4, microfibril-associated protein | Mutations cause cutis laxa and aortic aneurysm; critical for elastic fiber assembly |
| LOX | Lysyl oxidase, cross-links elastin and collagen | Defects lead to connective tissue disorders; target for studying cross-linking |
| LTBP1 | Latent TGF-beta binding protein 1 | Regulates TGF-beta signaling and elastic fiber assembly |
| LTBP4 | Latent TGF-beta binding protein 4 | Mutations cause cutis laxa; links elastic fibers to TGF-beta signaling |
| MFAP5 | Microfibril-associated protein 5 | Regulates elastic fiber assembly; potential biomarker in cancer |
| EMILIN1 | Elastin microfibril interface-located protein 1 | Stabilizes elastic fibers; involved in vascular biology |
| TGFBR1 | TGF-beta receptor 1 | Signaling receptor that modulates ECM production; relevant to Marfan syndrome |
| TGFBR2 | TGF-beta receptor 2 | Mutations cause Loeys-Dietz syndrome; affects elastic fiber homeostasis |
| SMAD3 | TGF-beta signaling effector | Mutations cause aneurysm-osteoarthritis syndrome; links signaling to ECM |
| ACTA2 | Smooth muscle actin | Mutations cause aortic aneurysm; affects mechanical forces on ECM |
| COL3A1 | Type III collagen | Mutations cause Ehlers-Danlos syndrome; interacts with elastic fibers |
| ADAMTS2 | Procollagen N-proteinase | Mutations cause dermatosparaxis; affects collagen and elastic fiber cross-linking |
| BGN | Biglycan, proteoglycan | Modulates elastic fiber assembly; involved in connective tissue disorders |
How Is extracellular matrix constituent conferring elasticity Regulated?
The expression and assembly of elastic fiber components are regulated at multiple levels. Transcriptional regulation by growth factors such as TGF-beta and mechanical stretch influences elastin and fibrillin synthesis. Post-translational modifications, including cross-linking by lysyl oxidase, are critical for fiber maturation. Additionally, microfibril-associated proteins like fibulins and LTBP proteins modulate assembly and stability. Dysregulation of these pathways contributes to connective tissue diseases, making them important targets for research.
extracellular matrix constituent conferring elasticity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| FBN1 | Marfan syndrome | Knock-in mouse models with patient mutations; iPSC-derived vascular smooth muscle cells |
| ELN | Supravalvular aortic stenosis, cutis laxa | Elastin knockout mice; overexpression in fibroblasts |
| FBLN5 | Cutis laxa | Knockout mice; point mutations in elastic fiber assembly domains |
| LTBP4 | Cutis laxa | Knock-in models; TGF-beta signaling assays |
| COL3A1 | Ehlers-Danlos syndrome | Knockout mice; collagen and elastic fiber co-culture systems |
Marfan Syndrome and Related Disorders
Marfan syndrome is caused by mutations in FBN1, which encodes fibrillin-1, a key component of elastic fibers. The disease affects the cardiovascular, skeletal, and ocular systems, with aortic aneurysm being a major cause of morbidity. Defects in elastic fiber assembly lead to weakened connective tissue and impaired mechanical properties. Studying GO:0030023 helps elucidate the molecular basis of Marfan syndrome and related disorders such as Loeys-Dietz syndrome.
Cutis Laxa and Skin Elasticity Disorders
Cutis laxa is a group of disorders characterized by loose, sagging skin due to defective elastic fibers. Mutations in ELN, FBLN4, FBLN5, and LTBP4 have been implicated in different forms of cutis laxa. These conditions highlight the importance of elastic fiber components in maintaining skin integrity. Research into GO:0030023 provides insights into the molecular mechanisms of skin aging and potential therapeutic targets.
Vascular Diseases and Aneurysms
Elastic fibers are abundant in large arteries, where they provide resilience to pulsatile blood flow. Defects in elastin or microfibril proteins lead to aortic aneurysms and dissections, as seen in Marfan syndrome and other connective tissue disorders. The TGF-beta signaling pathway, which interacts with elastic fiber components, plays a crucial role in vascular pathology. Targeting elastic fiber assembly may offer new strategies for treating vascular diseases.
From extracellular matrix constituent conferring elasticity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| What is the role of ELN in elastic fiber assembly? | ELN knockout cell lines and mice |
| How do FBN1 mutations affect microfibril formation? | Point-mutation knock-in models |
| Can overexpression of FBLN5 rescue elastic fiber defects? | Overexpression cell models |
| What is the interactome of fibrillin-1? | Tagged knock-in for affinity purification |
| How does mechanical stretch regulate elastin expression? | In vitro stretch systems with reporter cells |
| What are the downstream signaling effects of elastic fiber disruption? | Knockout models combined with transcriptomics |
How to Study the extracellular matrix constituent conferring elasticity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| RNA-seq | Gene expression levels | Profiling elastic fiber gene networks |
| Proteomics | Protein composition and modifications | Identifying elastic fiber components |
| Immunofluorescence | Protein localization and fiber morphology | Visualizing elastic fibers in tissues |
| Biomechanical testing | Tissue elasticity and recoil | Assessing functional impact of mutations |
| CRISPR knockout | Loss-of-function effects | Determining gene necessity for elastic fibers |
| CRISPR knock-in | Precise mutation introduction | Modeling patient-specific mutations |
| Overexpression | Gain-of-function effects | Testing sufficiency of candidate genes |
| CRISPR library screening | High-throughput gene function | Discovering novel elastic fiber regulators |
Genomic and Transcriptomic Approaches
RNA-seq and single-cell RNA-seq can profile the expression of elastic fiber genes across tissues and developmental stages. These methods help identify co-regulated gene networks and splicing variants relevant to GO:0030023. CRISPR screens can systematically test the contribution of candidate genes to elastic fiber assembly.
Proteomic and Biochemical Assays
Mass spectrometry-based proteomics can characterize the composition of elastic fibers and identify post-translational modifications such as cross-links. Western blotting and immunostaining are used to detect elastin, fibrillins, and fibulins in cell and tissue samples. Cross-linking assays measure lysyl oxidase activity.
Imaging and Biomechanics
Electron microscopy and immunofluorescence can visualize elastic fiber ultrastructure and localization. Biomechanical testing, such as tensile strength and stress-strain measurements, quantifies tissue elasticity and recoil. These methods directly assess the functional outcome of GO:0030023.
CRISPR-Based Functional Genomics
CRISPR knockout, knock-in, and overexpression models enable precise manipulation of elastic fiber genes. Pooled CRISPR screens can identify novel regulators of elastic fiber assembly. These approaches are essential for establishing causal relationships between genes and the elastic recoil function.
How CRISPR Can Be Used to Study GO:0030023 extracellular matrix constituent conferring elasticity
Knockout
CRISPR knockout of elastic fiber genes such as ELN or FBN1 in cell lines and animal models can reveal their essential roles in matrix assembly and recoil. These models help determine whether a gene is required for the molecular function defined by GO:0030023.
Point Mutation
Introducing specific point mutations found in patients (e.g., in FBN1) allows researchers to study the precise molecular defects that impair elastic fiber function. This approach bridges genotype to phenotype in diseases like Marfan syndrome.
Knock-in
Knock-in of tagged versions of elastic fiber proteins (e.g., GFP-ELN) enables live-cell imaging and proteomic analysis of assembly dynamics. Knock-in models can also humanize specific gene regions for drug testing.
Overexpression
Overexpression of candidate genes like FBLN5 or ELN can test whether increased levels enhance or rescue elastic fiber formation. This is useful for identifying rate-limiting components and potential therapeutic targets.
How EDITGENE Supports extracellular matrix constituent conferring elasticity Research
Researchers studying extracellular matrix constituent conferring elasticity-related genes often need to determine whether a candidate gene is causally involved in elastic fiber assembly, how specific mutations affect protein function, and what downstream pathways are perturbed. EDITGENE provides a comprehensive suite of CRISPR-based services to address these questions with precision and scale.
Contact EDITGENE today to design your custom CRISPR model for extracellular matrix constituent conferring elasticity research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| FBN1 Knockout HEK293 Cell Line | EDJ-KQ376 | Human | 2200 | Details Get a Quote |
| LAMC1 Knockout HEK293 Cell Line | EDJ-KQ830 | Human | 3915 | Details Get a Quote |
| FBN2 Knockout HEK293 Cell Line | EDJ-KQ2572 | Human | 2201 | Details Get a Quote |
| ELN Knockout HEK293 Cell Line | EDJ-KQ3563 | Human | 2006 | Details Get a Quote |
| FBLN2 Knockout HEK293 Cell Line | EDJ-KQ4578 | Human | 2199 | Details Get a Quote |
| FBLN5 Knockout HEK293 Cell Line | EDJ-KQ7074 | Human | 10516 | Details Get a Quote |
| EMILIN1 Knockout HEK293 Cell Line | EDJ-KQ7291 | Human | 11117 | Details Get a Quote |
| EMILIN3 Knockout HEK293 Cell Line | EDJ-KQ9857 | Human | 90187 | Details Get a Quote |
| EMILIN2 Knockout HEK293 Cell Line | EDJ-KQ9957 | Human | 84034 | Details Get a Quote |
| FBN3 Knockout HEK293 Cell Line | EDJ-KQ10098 | Human | 84467 | Details Get a Quote |
| FBN1 Knockout HeLa Cell Line | EDJ-KQ17981 | Human | 2200 | Details Get a Quote |
| LAMC1 Knockout HCT 116 Cell Line | EDJ-KQ18151 | Human | 3915 | Details Get a Quote |
| FBN3 Knockout HCT 116 Cell Line | EDJ-KQ37178 | Human | 84467 | Details Get a Quote |
| FBN1 Knockout A-549 Cell Line | EDJ-KQ18581 | Human | 2200 | Details Get a Quote |
| FBN1 Knockout HCT 116 Cell Line | EDJ-KQ18582 | Human | 2200 | Details Get a Quote |
Displaying Records 1 To 15 Of 40 Records
- 1
- 2
- Next Page »
Frequently Asked Questions About extracellular matrix constituent conferring elasticity
What is GO:0030023?
GO:0030023 is a Gene Ontology molecular function term that describes a component of the extracellular matrix that enables the matrix to recoil after transient stretching.
What genes are involved in extracellular matrix constituent conferring elasticity?
Key genes include ELN, FBN1, FBN2, FBLN4, FBLN5, LOX, and others encoding elastic fiber components.
What diseases are associated with defects in elastic fibers?
Marfan syndrome, cutis laxa, supravalvular aortic stenosis, and Ehlers-Danlos syndrome are linked to elastic fiber defects.
How can CRISPR be used to study elastic fiber genes?
CRISPR knockout, knock-in, point mutation, and overexpression models allow precise manipulation of genes to study their roles in elastic fiber assembly and function.
What is the role of fibrillin-1 in elastic fibers?
Fibrillin-1 is a major component of microfibrils that serve as a scaffold for elastin deposition; mutations cause Marfan syndrome.
What are microfibrils?
Microfibrils are extracellular matrix structures primarily composed of fibrillins that provide a template for elastin assembly and are a cornerstone of the ECM.
How is elastic fiber assembly regulated?
It is regulated by TGF-beta signaling, mechanical stretch, and post-translational cross-linking by lysyl oxidase.
What methods are used to study ECM elasticity?
Methods include RNA-seq, proteomics, immunofluorescence, biomechanical testing, and CRISPR screens.
What is the difference between elastin and microfibrils?
Elastin is the amorphous core protein that provides elasticity, while microfibrils are fibrillin-rich structures that guide elastin assembly.
Can EDITGENE help with CRISPR models for elastic fiber research?
Yes, EDITGENE offers knockout, point mutation, knock-in, overexpression, library screening, and bioinformatics services for ECM research.
Conclusion
GO:0030023, extracellular matrix constituent conferring elasticity, defines a critical molecular function that underpins the mechanical resilience of dynamic tissues. Elastin and associated microfibrillar proteins form complex supramolecular networks whose dysfunction leads to a spectrum of connective tissue diseases. Understanding the genes, mechanisms, and regulatory pathways involved is essential for developing therapeutic strategies. CRISPR-based models and advanced omics technologies provide powerful tools to dissect this function and translate findings into clinical benefit.
References
- 1. Bonetti MI. 2009. Microfibrils: a cornerstone of extracellular matrix and a key to understand Marfan syndrome.. Ital J Anat Embryol 114(4):201-24 PMID: 20578676
