Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (688 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Glycoprotein GP-2; Glycoprotein GP 2; Laminin M; Laminin M Chain; Chain, Laminin M; M Chain, Laminin; Merosin.
Where it fits in the MeSH classification
- Broader topics
- Membrane Glycoproteins; Extracellular Matrix Proteins
- Narrower topics
- Kalinin
- See also
- Receptors, Laminin
Research landscape
PubMed indexes 16,750 records tagged with the MeSH heading “Laminin” (counts retrieved 2026-10-31). 1,466 of them (8.8%) were published from 2020 onward, and the busiest period so far is through 1999 with 6,364 records.
Reviews account for 854 records (5.1%) and meta-analyses for 7. Randomized controlled trials number 24 (0.1%) as a share of all records on the topic. Randomized trials make up only a small share of this literature, so much of what is known comes from laboratory, observational or descriptive work.
Show the data
| Period | Records |
|---|---|
| through 1999 | 6,364 |
| 2000-2009 | 5,082 |
| 2010-2019 | 3,838 |
| 2020 onward | 1,466 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 854 | 5.1% |
| Meta-analyses | 7 | 0.0% |
| Randomized controlled trials | 24 | 0.1% |
Method: PubMed query "Laminin"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-31.
Reading the evidence in drugs and chemicals
Studies of a chemical or drug can answer very different questions: what it is and how it behaves in cells and animals, how the body handles it, and whether it changes outcomes in people. Laboratory and animal findings often do not carry over to patients, and observational studies of exposures are confounded by who uses a substance and why. Nothing on this page is a recommendation to use, avoid, start or stop any substance or medicine; talk to a qualified clinician or pharmacist about your own situation. Check the dose, the species, the comparison group and whether a patient-relevant outcome was measured.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| Towards organoid culture without Matrigel | 2021 | Review article Design not recorded in structured metadata | 321 | cc by PMID 34893703 · DOI · PMC8664924 |
| A new cell-laden 3D Alginate-Matrigel hydrogel resembles human breast cancer cell malignant morphology, spread and invasion capability observed "in vivo" | 2018 | Research article Design not recorded in structured metadata | 107 | cc by PMID 29593247 · DOI · PMC5871779 |
| Structural mechanism of laminin recognition by integrin | 2021 | Research article Design not recorded in structured metadata | 100 | cc by PMID 34188035 · DOI · PMC8241838 |
| Scalable Matrigel-Free Suspension Culture for Generating High-Quality Human Liver Ductal Organoids | 2025 | Research article Design not recorded in structured metadata | 7 | cc by PMID 40166955 · DOI · PMC12414634 |
Towards organoid culture without Matrigel [1]
Abstract reading summary — source excerpts
- Opening excerpt
- Organoids-cellular aggregates derived from stem or progenitor cells that recapitulate organ function in miniature-are of growing interest in developmental biology and medicine.
- Closing excerpt
- In this review, we discuss promising Matrigel-free methods for the generation and maintenance of organoids that use decellularized extracellular matrix (ECM), synthetic hydrogels, or gel-forming recombinant proteins.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (127 words)
Organoids-cellular aggregates derived from stem or progenitor cells that recapitulate organ function in miniature-are of growing interest in developmental biology and medicine. Organoids have been developed for organs and tissues such as the liver, gut, brain, and pancreas; they are used as organ surrogates to study a wide range of questions in basic and developmental biology, genetic disorders, and therapies. However, many organoids reported to date have been cultured in Matrigel, which is prepared from the secretion of Engelbreth-Holm-Swarm mouse sarcoma cells; Matrigel is complex and poorly defined. This complexity makes it difficult to elucidate Matrigel-specific factors governing organoid development. In this review, we discuss promising Matrigel-free methods for the generation and maintenance of organoids that use decellularized extracellular matrix (ECM), synthetic hydrogels, or gel-forming recombinant proteins.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 34893703 · DOI · PMC8664924
A new cell-laden 3D Alginate-Matrigel hydrogel resembles human breast cancer cell malignant morphology, spread and invasion capability observed "in vivo" [2]
Abstract reading summary — source excerpts
- Opening excerpt
- Purpose of this study was the development of a 3D material to be used as substrate for breast cancer cell culture.
- Closing excerpt
- cells were able to migrate through the gels and attach to an engineered membrane mimicking the vascular walls hosted within bioreactor, providing a completely new 3D in vitro model of the very precursor steps of metastasis.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (169 words)
Purpose of this study was the development of a 3D material to be used as substrate for breast cancer cell culture. We developed composite gels constituted by different concentrations of Alginate (A) and Matrigel (M) to obtain a structurally stable-in-time and biologically active substrate. Human aggressive breast cancer cells (i.e. MDA-MB-231) were cultured within the gels. Known the link between cell morphology and malignancy, cells were morphologically characterized and their invasiveness correlated through an innovative bioreactor-based invasion assay. A particular type of gel (i.e. 50% Alginate, 50% Matrigel) emerged thanks to a series of significant results: 1. cells exhibited peculiar cytoskeleton shapes and nuclear fragmentation characteristic of their malignancy; 2. cells expressed the formation of the so-called invadopodia, actin-based protrusion of the plasma membrane through which cells anchor to the extracellular matrix; 3. cells were able to migrate through the gels and attach to an engineered membrane mimicking the vascular walls hosted within bioreactor, providing a completely new 3D in vitro model of the very precursor steps of metastasis.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 29593247 · DOI · PMC5871779
Structural mechanism of laminin recognition by integrin [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Recognition of laminin by integrin receptors is central to the epithelial cell adhesion to basement membrane, but the structural background of this molecular interaction remained elusive.
- Closing excerpt
- The propeller sheet corresponding to this region shows unusually high mobility, suggesting its unique role in ligand capture.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (149 words)
Recognition of laminin by integrin receptors is central to the epithelial cell adhesion to basement membrane, but the structural background of this molecular interaction remained elusive. Here, we report the structures of the prototypic laminin receptor α6β1 integrin alone and in complex with three-chain laminin-511 fragment determined via crystallography and cryo-electron microscopy, respectively. The laminin-integrin interface is made up of several binding sites located on all five subunits, with the laminin γ1 chain C-terminal portion providing focal interaction using two carboxylate anchor points to bridge metal-ion dependent adhesion site of integrin β1 subunit and Asn189 of integrin α6 subunit. Laminin α5 chain also contributes to the affinity and specificity by making electrostatic interactions with large surface on the β-propeller domain of α6, part of which comprises an alternatively spliced X1 region. The propeller sheet corresponding to this region shows unusually high mobility, suggesting its unique role in ligand capture.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 34188035 · DOI · PMC8241838
Scalable Matrigel-Free Suspension Culture for Generating High-Quality Human Liver Ductal Organoids [4]
Abstract reading summary — source excerpts
- Opening excerpt
- Liver transplantation is currently the sole definitive treatment option for end-stage liver failure.
- Closing excerpt
- Finally, animal experiments indicated that the transplantation of liver ductal organoids harvested from suspension culture can effectively alleviate liver injury and inflammation, demonstrating the feasibility of large-scale production of liver ductal organoids cultivated in suspension culture with an improved extracellular matrix environment.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (243 words)
Liver transplantation is currently the sole definitive treatment option for end-stage liver failure. However, a significant shortage of donors prevails due to high clinical demands. Recently, human liver organoids have shown significant potential in regenerative medicine for liver diseases. Nevertheless, current static cultures of organoids grown in well-plates heavily rely on extracellular matrix hydrogels (Matrigel), thereby limiting both the scalability and quantity of organoid culture. In this study, we present a groundbreaking culture mode that eliminates all reliance on extracellular matrix hydrogels, enabling the successful preparation of functional human liver ductal organoids (LDOs) based on the cell suspension culture mode in a mechanically stirred bioreactor. Initially, the developed suspension culture in a 6-well plate without matrigel was proven to support robust growth of liver ductal organoids with an average size 2.6 times larger than those obtained in static culture, and with a high organoid survival rate exceeding 90%. Also, the transcriptome profile reveals that suspension culture activates the phosphatidylinositol 3-kinase (PI3K) signalling pathway through mechanical signal transduction, thereby promoting hepatobiliary characteristics. Then, a controllable and scalable bioprocess for liver ductal organoid culture was developed and successfully scaled up to a 50 mL flask bioreactor with a working volume of 15 mL. Finally, animal experiments indicated that the transplantation of liver ductal organoids harvested from suspension culture can effectively alleviate liver injury and inflammation, demonstrating the feasibility of large-scale production of liver ductal organoids cultivated in suspension culture with an improved extracellular matrix environment.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 40166955 · DOI · PMC12414634
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Matrigel: basement membrane matrix with biological activity [5]
- Research article Form and function: the laminin family of heterotrimers [6]
- Research article A simplified laminin nomenclature [7]
- Research article Laminin and other basement membrane components [8]
- Research article Structure and function of laminin: anatomy of a multidomain glycoprotein [9]
- Research article Laminin functions in tissue morphogenesis [10]
References
- Kozlowski MT, Crook CJ, Ku HT. Towards organoid culture without Matrigel. . 2021. PMID 34893703 · DOI · PMC8664924
- Cavo M, Caria M, Pulsoni I, Beltrame F, Fato M, Scaglione S. A new cell-laden 3D Alginate-Matrigel hydrogel resembles human breast cancer cell malignant morphology, spread and invasion capability observed "in vivo". . 2018. PMID 29593247 · DOI · PMC5871779
- Arimori T, Miyazaki N, Mihara E, Takizawa M, Taniguchi Y, Cabañas C, et al.. Structural mechanism of laminin recognition by integrin. . 2021. PMID 34188035 · DOI · PMC8241838
- Gong S, He K, Liu Y, Luo X, Ashraf K, He J, et al.. Scalable Matrigel-Free Suspension Culture for Generating High-Quality Human Liver Ductal Organoids. . 2025. PMID 40166955 · DOI · PMC12414634
- Kleinman HK, Martin GR. Matrigel: basement membrane matrix with biological activity. Semin Cancer Biol. 2005. PMID 15975825 · DOI
- Colognato H, Yurchenco PD. Form and function: the laminin family of heterotrimers. Dev Dyn. 2000. PMID 10842354 · DOI
- Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, et al.. A simplified laminin nomenclature. Matrix Biol. 2005. PMID 15979864 · DOI
- Martin GR, Timpl R. Laminin and other basement membrane components. Annu Rev Cell Biol. 1987. PMID 3318883 · DOI
- Beck K, Hunter I, Engel J. Structure and function of laminin: anatomy of a multidomain glycoprotein. FASEB J. 1990. PMID 2404817 · DOI
- Miner JH, Yurchenco PD. Laminin functions in tissue morphogenesis. Annu Rev Cell Dev Biol. 2004. PMID 15473841 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-31.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.