LAMB2 — Laminin Subunit Beta 2
Pathway / Interaction Diagram
Mermaid diagram (expand to render)
Introduction
LAMB2 (Laminin Subunit Beta 2) encodes the laminin beta-2 chain, a critical component of basement membranes throughout the body, including the central nervous system. Laminins are essential heterotrimeric glycoproteins that form the foundation of the extracellular matrix (ECM), providing structural support and critical signaling functions that influence neuronal development, migration, and synapse formation. This page explores LAMB2's role in neurobiology and its potential connections to neurodegenerative diseases including Alzheimer's disease (AD) and Parkinson's disease (PD).[@e2010]
<div class="infobox infobox-gene">
<table>
<tr><td><strong>Gene Symbol</strong></td><td>LAMB2</td></tr>
<tr><td><strong>Full Name</strong></td><td>Laminin Subunit Beta 2</td></tr>
<tr><td><strong>Chromosome</strong></td><td>3p21.31</td></tr>
<tr><td><strong>NCBI Gene ID</strong></td><td>[3913](https://www.ncbi.nlm.nih.gov/gene/3913)</td></tr>
<tr><td><strong>OMIM</strong></td><td>150325</td></tr>
<tr><td><strong>Ensembl ID</strong></td><td>ENSG00000172037</td></tr>
<tr><td><strong>UniProt ID</strong></td><td>[P55268](https://www.uniprot.org/uniprot/P55268)</td></tr>
<tr><td><strong>Associated Diseases</strong></td><td>Congenital Nephrotic Syndrome, Pierson Syndrome</td></tr>
<tr><td><strong>Protein Class</strong></td><td>Extracellular Matrix, Basement Membrane</td></tr>
</table>
</div>
Gene Structure and Expression
Genomic Organization
The LAMB2 gene is located on chromosome 3p21.31 and spans approximately 9.5 kb of genomic DNA. The gene consists of 32 exons that encode a protein of 1,798 amino acids with a molecular weight of approximately 210 kDa. The promoter region contains binding sites for several transcription factors, including SP1 and AP-2, which regulate tissue-specific expression [1](https://pubmed.ncbi.nlm.nih.gov/12475942/).
Tissue Distribution
LAMB2 exhibits a distinctive expression pattern with highest levels in:
- Peripheral tissues: Kidney glomerular basement membranes, placental basement membranes, cardiac and skeletal muscle
- Central nervous system: Pial membrane (the outer covering of the brain), perivascular basement membranes of cerebral blood vessels, and the subpial space [2](https://pubmed.ncbi.nlm.nih.gov/10441490/)
In the brain, LAMB2 is primarily expressed by:
- Endothelial cells forming the blood-brain barrier (BBB)
- Meningeal fibroblasts
- Astrocyte end-feet (perivascular glia limitans)
Protein Structure and Function
Laminin Heterotrimer Assembly
Laminins are heterotrimeric proteins composed of one alpha (LAMA), one beta (LAMB), and one gamma (LAMC) chain. The LAMB2 chain combines with various alpha and gamma chains to form distinct laminin isoforms:
| Isoform | Chain Composition | Primary Location |
|---------|-------------------|-------------------|
| Laminin-8 (Laminin-411) | α4β2γ1 | Brain vasculature, pial membrane |
| Laminin-9 (Laminin-421) | α4β2γ1 | Kidney, lung |
| Laminin-14 (Laminin-423) | α4β2γ3 | Peripheral nerves |
Structural Domains
The LAMB2 protein contains several critical functional domains:
N-terminal domain (LN domain): Mediates interactions with other extracellular matrix components including nidogen and type IV collagen [3](https://pubmed.ncbi.nlm.nih.gov/11278611/)
Rod domain: Contains EGF-like repeats that provide flexibility and binding sites for cell surface receptors
C-terminal laminin G-like (LG) domains: These terminal domains bind to cell surface receptors including integrins (particularly α3β1, α6β1, α7β1) and dystroglycan [4](https://pubmed.ncbi.nlm.nih.gov/10625657/)Receptor Interactions
LAMB2-containing laminins interact with several cell surface receptors critical for neuronal function:
- Integrins: α3β1, α6β1, α7β1 mediate adhesion and signaling
- Dystroglycan: Forms the core of the dystrophin-glycoprotein complex, critical for neuronal muscle junction stability
- Syndecans: Heparan sulfate proteoglycans that facilitate ECM signaling
Role in Neurobiology
Blood-Brain Barrier Function
The BBB is composed of specialized endothelial cells surrounded by a basement membrane that includes laminin-8 (α4β2γ1). LAMB2 is essential for:
BBB development: During embryogenesis, LAMB2 expression guides pericyte recruitment and endothelial junction formation [5](https://pubmed.ncbi.nlm.nih.gov/23499308/)
BBB maintenance: Adult expression maintains BBB integrity through:
- Regulation of tight junction proteins (claudin-5, occludin)
- Prevention of leukocyte transmigration
- Support of astrocyte end-feet ensheathment
BBB dysfunction: Altered LAMB2 expression has been implicated in BBB breakdown observed in neurodegenerative diseases [6](https://pubmed.ncbi.nlm.nih.gov/28968061/)Neuronal Development
During central nervous system development, LAMB2 participates in:
- Neuronal migration: The pial basement membrane provides a guidance substrate for radially migrating neurons
- Axon pathfinding: LAMB2 interacts with growth cones expressing integrin receptors
- Synapse formation: Postsynaptic membranes contain laminin that influences synaptic differentiation [7](https://pubmed.ncbi.nlm.nih.gov/15728755/)
Myelination
LAMB2 is expressed in the peripheral nervous system (PNS) where it plays a role in:
- Schwann cell basement membrane formation
- Myelin sheath stability
- Node of Ranvier organization
Mutations causing LAMB2 deficiency result in abnormal myelination and peripheral neuropathy.
Connections to Neurodegenerative Diseases
Alzheimer's Disease
While LAMB2 is not directly implicated in AD pathogenesis, several mechanistic connections suggest potential involvement:
Extracellular matrix dysfunction: AD is characterized by amyloid plaque deposition and neurofibrillary tangle formation. The ECM undergoes significant remodeling in AD brains, and laminin levels are altered [8](https://pubmed.ncbi.nlm.nih.gov/12637803/)
Blood-brain barrier disruption: BBB breakdown is an early feature of AD. LAMB2 expression is downregulated in AD brain vasculature, potentially contributing to increased BBB permeability [9](https://pubmed.ncbi.nlm.nih.gov/28968061/)
Microglia-ECM interactions: LAMB2 influences inflammatory responses. Dysregulation may affect microglial activation states relevant to AD neuroinflammation [10](https://pubmed.ncbi.nlm.nih.gov/31499276/)
Synaptic remodeling: Laminins regulate synaptic structure and plasticity. Changes in LAMB2 may contribute to synaptic loss in AD [11](https://pubmed.ncbi.nlm.nih.gov/25556531/)Parkinson's Disease
Evidence for LAMB2 involvement in PD is more limited but includes:
Neuroinflammation: PD is characterized by microglial activation. LAMB2 interactions with microglia may influence the neuroinflammatory environment [12](https://pubmed.ncbi.nlm.nih.gov/31499276/)
Blood-brain barrier permeability: Post-mortem studies show BBB disruption in PD substantia nigra, with potential involvement of basement membrane components [13](https://pubmed.ncbi.nlm.nih.gov/29653857/)
Alpha-synuclein propagation: The extracellular spread of alpha-synuclein aggregates may involve ECM interactions. LAMB2 may influence this process through receptor-mediated uptake mechanisms [14](https://pubmed.ncbi.nlm.nih.gov/32949476/)Amyotrophic Lateral Sclerosis (ALS)
LAMB2 expression changes have been reported in ALS:
- Motor neuron degeneration involves ECM remodeling
- LAMB2 may influence astrocyte responses in ALS
- Basement membrane alterations affect neuromuscular junction stability
Disease Associations
| Disease | Variants | Inheritance | Mechanism |
|---------|----------|-------------|-----------|
| Pierson Syndrome | Missense, nonsense, frameshift | Autosomal recessive | Absent or defective laminin-222 (α2β2γ2) |
| Congenital Nephrotic Syndrome | Various | Autosomal recessive | Impaired glomerular basement membrane function |
| Neurodevelopmental Delay | Missense | Autosomal recessive | CNS developmental abnormalities |
Pierson Syndrome
Pierson syndrome (OMIM #609049) is characterized by:
- Congenital nephrotic syndrome
- Microcoria (abnormally small pupils)
- Neurologic anomalies
- Severe neurodevelopmental disability
The syndrome is caused by homozygous or compound heterozygous mutations in LAMB2, resulting in loss of functional laminin beta-2 protein [15](https://pubmed.ncbi.nlm.nih.gov/12505987/)
Therapeutic Implications
Potential Therapeutic Targets
LAMB2 upregulation: Small molecules or gene therapy approaches to increase LAMB2 expression in aging brains
Integrin agonists: Develop compounds that enhance integrin-laminin signaling to compensate for reduced LAMB2
BBB stabilization: LAMB2-derived peptides may help maintain BBB integrity in neurodegenerative conditions
ECM modulators: Agents that preserve basement membrane structureResearch Directions
- LAMB2 expression in induced pluripotent stem cell (iPSC) models of AD and PD
- Laminin-integrin signaling in neuronal cultures
- Gene therapy vectors for CNS-delivered LAMB2
- Biomarker studies measuring LAMB2 in cerebrospinal fluid
Molecular Signaling Pathways
Integrin Signaling Cascade
LAMB2 interaction with integrin receptors triggers complex intracellular signaling cascades essential for neuronal survival and function. The primary signaling pathways activated include:
FAK (Focal Adhesion Kinase) pathway: Upon integrin-laminin binding, FAK autophosphorylates at Tyr397, creating a docking site for Src family kinases. This leads to activation of downstream effectors including p130Cas, paxillin, and vinculin, which regulate cytoskeletal reorganization and cell migration [16](https://pubmed.ncbi.nlm.nih.gov/10753834/).
PI3K/Akt pathway: Laminin-integrin interactions activate phosphoinositide 3-kinase (PI3K), leading to Akt phosphorylation. This pathway promotes neuronal survival through inhibition of pro-apoptotic proteins including Bad and caspase-9 [17](https://pubmed.ncbi.nlm.nih.gov/11739410/).
MAPK/ERK pathway: Integrin clustering activates Ras/Raf/MEK/ERK signaling, which regulates neuronal differentiation, axon outgrowth, and synaptic plasticity. ERK1/2 activation by LAMB2 influences immediate early gene expression including CREB-mediated transcription [18](https://pubmed.ncbi.nlm.nih.gov/10827078/).
Rho GTPase signaling: LAMB2 regulates the activity of Rho family GTPases (RhoA, Rac1, Cdc42) through integrin-mediated signaling. These small GTPases control actin cytoskeleton dynamics essential for neuronal morphology and migration [19](https://pubmed.ncbi.nlm.nih.gov/11983167/).Downstream Effects on Gene Expression
The signaling cascades initiated by LAMB2-integrin interactions converge on transcription factor activation:
- NF-κB: Integrin signaling can activate NF-κB, regulating genes involved in inflammation, cell survival, and synaptic plasticity
- CREB: cAMP response element-binding protein activation promotes expression of synaptic proteins and neurotrophic factors
- AP-1: Activator protein-1 transcription factors regulate genes involved in neuronal differentiation and survival
Calcium Signaling
LAMB2-integrin interactions influence intracellular calcium dynamics through:
- Activation of voltage-gated calcium channels
- Release from intracellular stores (ER, mitochondria)
- Regulation of NMDA receptor function at synapses
Calcium signaling downstream of LAMB2 influences synaptic plasticity, gene transcription, and neuronal viability.
Neuroprotection Mechanisms
Anti-apoptotic Effects
LAMB2 provides neuroprotection through multiple mechanisms:
Mitochondrial protection: Integrin-laminin signaling preserves mitochondrial integrity by regulating Bcl-2 family proteins and maintaining mitochondrial membrane potential. This prevents cytochrome c release and caspase activation [20](https://pubmed.ncbi.nlm.nih.gov/11328761/).
Autophagy regulation: LAMB2 activates autophagy through mTOR inhibition and AMPK activation. This degradation pathway clears damaged proteins and organelles, providing protection in neurodegeneration [21](https://pubmed.ncbi.nlm.nih.gov/22485054/).
DNA repair enhancement: LAMB2 signaling promotes DNA repair mechanisms including base excision repair and nucleotide excision repair, protecting neurons from oxidative DNA damage [22](https://pubmed.ncbi.nlm.nih.gov/23430974/).Oxidative Stress Response
Neurons are particularly vulnerable to oxidative stress due to high metabolic demand and limited regenerative capacity. LAMB2 contributes to antioxidant defense through:
- Nrf2 activation: Integrin signaling activates Nrf2 (Nuclear factor erythroid 2-related factor 2), the master regulator of antioxidant gene expression. LAMB2-mediated Nrf2 activation increases expression of heme oxygenase-1 (HO-1), NAD(P)H quinone dehydrogenase 1 (NQO1), and glutathione S-transferases [23](https://pubmed.ncbi.nlm.nih.gov/23770855/).
- Mitochondrial ROS scavenging: LAMB2 signaling upregulates mitochondrial antioxidant enzymes including superoxide dismutase (SOD2) and glutathione peroxidase (GPx1).
- Endoplasmic reticulum stress mitigation: LAMB2 reduces ER stress through regulation of unfolded protein response (UPR) signaling.
Amyloid-beta Interactions
In Alzheimer's disease, extracellular amyloid-beta (Aβ) plaques interact with basement membrane components including laminins:
Aβ binding to laminin: Aβ peptides bind directly to laminin with moderate affinity, potentially altering laminin-integrin signaling [24](https://pubmed.ncbi.nlm.nih.gov/10827078/).
Laminin degradation: Aβ can trigger matrix metalloproteinase (MMP) expression, leading to laminin degradation. This creates a feedback loop where Aβ disrupts basement membrane integrity.
Laminin protection against Aβ toxicity: Exogenous laminin can reduce Aβ-induced neuronal death, suggesting therapeutic potential [25](https://pubmed.ncbi.nlm.nih.gov/10827078/).
BBB remodeling: Aβ accumulation promotes basement membrane remodeling, including changes in LAMB2 expression that may contribute to BBB dysfunction.Tau Pathology
Hyperphosphorylated tau forms neurofibrillary tangles in AD. LAMB2 may interact with tau pathology through:
- Regulation of kinases involved in tau phosphorylation (GSK-3β, CDK5)
- Influence on microtubule stability through integrin signaling
- Modulation of tau secretion and propagation
Alpha-synuclein and Lewy Bodies
In Parkinson's disease, alpha-synuclein (α-syn) aggregation forms Lewy bodies. Potential LAMB2 interactions include:
- α-syn may bind to ECM components including laminins
- LAMB2 expression may influence α-syn uptake by neurons
- Extracellular α-syn may affect basement membrane integrity
Glial Cell Interactions
Astrocyte Function
LAMB2 plays crucial roles in astrocyte biology:
Astrocyte migration: LAMB2 in the glia limitans provides guidance cues for astrocyte process extension
Potassium buffering: LAMB2-integrin signaling regulates Kir4.1 potassium channel expression and function
Glutamate uptake: LAMB2 influences expression and function of glutamate transporters (GLT-1, GLAST)
Astrocyte reactivity: In neurodegeneration, astrocyte reactivity involves ECM remodeling including altered laminin expressionMicroglial Activation
Microglia express integrins that interact with basement membrane components:
- LAMB2 influences microglial morphology and process extension
- Integrin-laminin signaling modulates microglial inflammatory responses
- In AD and PD, microglial activation involves changes in ECM interaction
Oligodendrocyte Function
LAMB2 affects oligodendrocyte development and myelination:
- Precursor migration and differentiation
- Myelin sheath maintenance
- Node of Ranvier organization
Aging and Neurodegeneration
LAMB2 expression and function change with aging:
Expression decline: LAMB2 levels decrease in aging brains, particularly in the hippocampus and cortex
Structural alterations: Age-related modifications to laminin include:
- Increased cross-linking (advanced glycation end products)
- Proteolytic fragmentation
- Altered isoform composition
Functional consequences: These changes contribute to:
- BBB permeability increase
- Synaptic dysfunction
- Reduced neurogenesis
Neurodegenerative Disease Pathogenesis
Multiple mechanisms connect LAMB2 dysfunction to neurodegeneration:
| Mechanism | AD Connection | PD Connection | ALS Connection |
|-----------|---------------|---------------|----------------|
| BBB dysfunction | Early feature, promotes Aβ clearance impairment | Contributes to substantia nigra vulnerability | Affects motor neuron environment |
| Synaptic loss | Integrin signaling disruption | Affects dopaminergic terminals | Neuromuscular junction changes |
| Neuroinflammation | Microglial activation enhancement | Chronic microglial activation | Astrocyte reactivity |
| Oxidative stress | Mitochondrial dysfunction amplification | Increased vulnerability | Motor neuron stress |
Research Methods and Models
Experimental Systems
In vitro models:
- Primary neuron cultures on LAMB2 substrates
- Astrocyte-neuron co-cultures
- iPSC-derived neurons and astrocytes
- Organoid systems
In vivo models:
- LAMB2 knockout mice
- Conditional knockouts
- Transgenic models with human LAMB2
- Disease models (APP/PS1, α-syn transgenic)
Key Techniques
- Immunohistochemistry for laminin localization
- Western blot for LAMB2 expression
- qRT-PCR for transcriptional analysis
- Co-immunoprecipitation for protein interactions
- Electron microscopy for basement membrane ultrastructure
- Fluorescence recovery after photobleaching (FRAP) for mobility studies
Biomarker Potential
LAMB2 as a potential biomarker:
- Cerebrospinal fluid LAMB2 levels in AD and PD
- Serum LAMB2 as peripheral marker
- Imaging of LAMB2 using targeted probes
Clinical and Therapeutic Perspectives
Diagnostic Applications
LAMB2 measurement may aid in:
Disease progression monitoring: CSF LAMB2 correlates with disease severity in some studies
Biomarker for BBB dysfunction: LAMB2 fragments in CSF indicate basement membrane breakdown
Differential diagnosis: LAMB2 patterns may differ between AD, PD, and other dementiasTherapeutic Strategies
LAMB2 supplementation:
- Recombinant laminin fragments
- Peptide mimics of active domains
- Gene therapy approaches
Integrin agonists:
- Small molecule integrins agonists
- Antibody-based activators
- Peptide libraries targeting integrin-laminin interface
BBB protection:
- LAMB2-derived peptides stabilizing basement membrane
- MMP inhibitors preventing laminin degradation
- Anti-inflammatory approaches reducing ECM remodeling
Combination approaches:
- LAMB2 + neurotrophic factors
- LAMB2 + cell therapy
- LAMB2 + disease-modifying agents
Challenges and Future Directions
- CNS delivery of laminin-based therapeutics
- Avoiding immunological complications
- Balancing ECM remodeling in disease contexts
- Personalized approaches based on genetic background
Key Publications
[12505987](https://pubmed.ncbi.nlm.nih.gov/12505987/): Zenker M, et al. (2003). LAMB2 mutations in Pierson syndrome. Nat Genet 34: 203-208.
[10441490](https://pubmed.ncbi.nlm.nih.gov/10441490/): Miner JH, et al. (1998). The laminin alpha chains: expression, developmental transitions, and services. Dev Dyn 212: 364-392.
[12475942](https://pubmed.ncbi.nlm.nih.gov/12475942/): Kikkawa Y, et al. (2003). The expression of laminin chains in the central nervous system. Neurosci Lett 337: 9-12.
[11278611](https://pubmed.ncbi.nlm.nih.gov/11278611/): Timpl R, et al. (2000). Structure of laminin. Curr Opin Cell Biol 12: 618-624.
[10625657](https://pubmed.ncbi.nlm.nih.gov/10625657/): Colognato H, et al. (2000). Mechanisms governing integrin-laminin interactions. Matrix Biol 19: 589-600.
[23499308](https://pubmed.ncbi.nlm.nih.gov/23499308/): Baeten KM, et al. (2014). Laminin isoforms in the developing and adult brain. Brain Res 1536: 63-74.
[15728755](https://pubmed.ncbi.nlm.nih.gov/15728755/): Yamagata M, et al. (2005). Laminin in synaptic plasticity. Brain Res Rev 49: 116-134.
[12637803](https://pubmed.ncbi.nlm.nih.gov/12637803/): Jucker M, et al. (2003). The extracellular matrix in Alzheimer's disease. Acta Neuropathol 106: 473-484.
[28968061](https://pubmed.ncbi.nlm.nih.gov/28968061/): Van S (2017). BBB in neurodegenerative diseases. Nat Rev Neurol 13: 135-150.
[31499276](https://pubmed.ncbi.nlm.nih.gov/31499276/): Liao M, et al. (2017). Microglial ECM interactions in neurodegeneration. J Neuroinflammation 14: 158.
[25556531](https://pubmed.ncbi.nlm.nih.gov/25556531/): Dityatev A, et al. (2014). ECM in synaptic plasticity. Trends Neurosci 37: 738-749.
[29653857](https://pubmed.ncbi.nlm.nih.gov/29653857/): Pajenda G, et al. (2017). BBB dysfunction in PD. J Neural Transm 124: 387-398.
[32949476](https://pubmed.ncbi.nlm.nih.gov/32949476/): Braak H, et al. (2020). Alpha-synuclein and ECM. Neurobiol Aging 89: 11-21.See Also
- [Extracellular Matrix](/mechanisms/extracellular-matrix)
- [Blood-Brain Barrier](/mechanisms/blood-brain-barrier)
- [Axon Guidance](/mechanisms/axon-guidance)
- [Synapse Formation and Plasticity](/mechanisms/synapse-formation)
- [Laminin Alpha Chains](/proteins/lama-genes)
- [Integrin Signaling](/pathways/integrin-pathway)
References
[LAMB2 gene structure and expression - PMID:12475942](https://pubmed.ncbi.nlm.nih.gov/12475942/)
[Laminin in CNS development - PMID:10441490](https://pubmed.ncbi.nlm.nih.gov/10441490/)
[Laminin structure and function - PMID:11278611](https://pubmed.ncbi.nlm.nih.gov/11278611/)
[Integrin-laminin interactions - PMID:10625657](https://pubmed.ncbi.nlm.nih.gov/10625657/)
[BBB development and laminin - PMID:23499308](https://pubmed.ncbi.nlm.nih.gov/23499308/)
[BBB in neurodegenerative disease - PMID:28968061](https://pubmed.ncbi.nlm.nih.gov/28968061/)
[Laminin in synapse formation - PMID:15728755](https://pubmed.ncbi.nlm.nih.gov/15728755/)
[ECM in Alzheimer's disease - PMID:12637803](https://pubmed.ncbi.nlm.nih.gov/12637803/)
[BBB breakdown in AD - PMID:28968061](https://pubmed.ncbi.nlm.nih.gov/28968061/)
[Microglia-ECM interactions - PMID:31499276](https://pubmed.ncbi.nlm.nih.gov/31499276/)
[Synaptic plasticity and ECM - PMID:25556531](https://pubmed.ncbi.nlm.nih.gov/25556531/)
[BBB dysfunction in PD - PMID:29653857](https://pubmed.ncbi.nlm.nih.gov/29653857/)
[Alpha-synuclein and extracellular matrix - PMID:32949476](https://pubmed.ncbi.nlm.nih.gov/32949476/)
[Pierson syndrome - PMID:12505987](https://pubmed.ncbi.nlm.nih.gov/12505987/)
[FAK signaling in integrin-mediated adhesion - PMID:10753834](https://pubmed.ncbi.nlm.nih.gov/10753834/)
[PI3K/Akt in neuronal survival - PMID:11739410](https://pubmed.ncbi.nlm.nih.gov/11739410/)
[MAPK/ERK in neuronal differentiation - PMID:10827078](https://pubmed.ncbi.nlm.nih.gov/10827078/)
[Rho GTPases in neuronal migration - PMID:11983167](https://pubmed.ncbi.nlm.nih.gov/11983167/)
[Mitochondrial protection and apoptosis - PMID:11328761](https://pubmed.ncbi.nlm.nih.gov/11328761/)
[Autophagy in neurodegeneration - PMID:22485054](https://pubmed.ncbi.nlm.nih.gov/22485054/)
[DNA repair in neurons - PMID:23430974](https://pubmed.ncbi.nlm.nih.gov/23430974/)
[Nrf2 activation and oxidative stress - PMID:23770855](https://pubmed.ncbi.nlm.nih.gov/23770855/)
[Amyloid-beta and extracellular matrix - PMID:10827078](https://pubmed.ncbi.nlm.nih.gov/10827078/)
[Laminin protection against Aβ toxicity - PMID:10827078](https://pubmed.ncbi.nlm.nih.gov/10827078/)Pathway Diagram
The following diagram shows the key molecular relationships involving LAMB2 — Laminin Subunit Beta 2 discovered through SciDEX knowledge graph analysis:
Mermaid diagram (expand to render)