Laminin

Not to be confused with Lamin.

Illustration of the laminin-111 complex depicting the domain organization.

Laminins are a family of glycoproteins of the extracellular matrix of all animals. They are major constituents of the basement membrane, namely the basal lamina (the protein network foundation for most cells and organs). Laminins are vital to biological activity, influencing cell differentiation, migration, and adhesion. ^{[1] [2]}

Laminins are heterotrimeric proteins with a high molecular mass (~400 to ~900 kDa) and possess three different chains (α, β, and γ) encoded by five, four, and three paralogous genes in humans, respectively. The laminin molecules are named according to their chain composition, e.g. laminin-511 contains α5, β1, and γ1 chains. ^[3] Fourteen other chain combinations have been identified in vivo . The trimeric proteins intersect, composing a cruciform structure that is able to bind to other molecules of the extracellular matrix and cell membrane. ^[4] The three short arms have an affinity for binding to other laminin molecules, conducing sheet formation. The long arm is capable of binding to cells and helps anchor organized tissue cells to the basement membrane.

Laminins are integral to the structural scaffolding of almost every tissue of an organism—secreted and incorporated into cell-associated extracellular matrices. These glycoproteins are imperative to the maintenance and vitality of tissues; defective laminins can cause muscles to form improperly, leading to a form of muscular dystrophy, lethal skin blistering disease (junctional epidermolysis bullosa), and/or defects of the kidney filter (nephrotic syndrome). ^[5]

Types

In humans, fifteen laminin trimers have been identified. The laminins are combinations of different alpha-, beta-, and gamma-chains. ^[6]

• Five alpha-chain isoforms: LAMA1, LAMA2, LAMA3 (which has three splice forms), LAMA4, LAMA5
• Four beta-chain isoforms: LAMB1, LAMB2, LAMB3, LAMB4 (note that no known laminin trimer incorporates LAMB4 and its function remains poorly understood).
• Three gamma-chain isoforms: LAMC1, LAMC2, LAMC3

Laminins were previously numbered as they were discovered, i.e., laminin-1, laminin-2, laminin-3, etc., but the nomenclature was changed to describe which chains are present in each isoform (laminin-111, laminin-211, etc.). ^[3] In addition, many laminins had common names before either laminin nomenclature was in place. ^{[7] [8]}

Old nomenclature	Old synonyms	Chain composition	New nomenclature
Laminin-1	EHS laminin	α1β1γ1	Laminin-111
Laminin-2	Merosin	α2β1γ1	Laminin-211
Laminin-3	S-laminin	α1β2γ1	Laminin-121
Laminin-4	S-merosin	α2β2γ1	Laminin-221
Laminin-5 / Laminin-5A	Kalinin, epiligrin, nicein, ladsin	α3Aβ3γ2	Laminin-332 / Laminin-3A32
Laminin-5B		α3Bβ3γ2	Laminin-3B32
Laminin-6 / Laminin-6A	K-laminin	α3Aβ1γ1	Laminin-311 / Laminin-3A11
Laminin-7 / Laminin-7A	KS-laminin	α3Aβ2γ1	Laminin-321 / Laminin-3A21
Laminin-8		α4β1γ1	Laminin-411
Laminin-9		α4β2γ1	Laminin-421
Laminin-10	Drosophila-like laminin	α5β1γ1	Laminin-511
Laminin-11		α5β2γ1	Laminin-521
Laminin-12		α2β1γ3	Laminin-213
Laminin-14		α4β2γ3	Laminin-423
		α5β2γ2	Laminin-522
Laminin-15		α5β2γ3	Laminin-523

Function

Laminins form independent networks and are associated with type IV collagen networks via entactin, ^[9] fibronectin, ^[10] and perlecan. The proteins also bind to cell membranes through integrins and other plasma membrane molecules, such as the dystroglycan glycoprotein complex and Lutheran blood group glycoprotein. ^[4] Through these interactions, laminins critically contribute to cell attachment and differentiation, cell shape and movement, maintenance of tissue phenotype, and promotion of tissue survival. ^{[4] [6]} Some of these biological functions of laminin have been associated with specific amino-acid sequences or fragments of laminin. ^[4] For example, the peptide sequence [GTFALRGDNGDNGQ], which is located on the alpha-chain of laminin, promotes the adhesion of endothelial cells. ^[11]

Laminin alpha4 is distributed in a variety of tissues, including peripheral nerves, dorsal root ganglion, skeletal muscle, and capillaries; in the neuromuscular junction, it is required for synaptic specialisation. ^[12] The structure of the laminin-G domain has been predicted to resemble that of pentraxin. ^[13]

Role in neural development

Laminin-111 is a major substrate along which nerve axons will grow, both in vivo and in vitro. For example, it lays down a path that developing retinal ganglion cells follow on their way from the retina to the tectum. It is also often used as a substrate in cell culture experiments. The presence of laminin-1 can influence how the growth cone responds to other cues. For example, growth cones are repelled by netrin when grown on laminin-111 but are attracted to netrin when grown on fibronectin.^{[ citation needed ]} This effect of laminin-111 probably occurs through a lowering of intracellular cyclic AMP.^{[ citation needed ]}

Role in peripheral nerve repair

Laminins are enriched at the lesion site after peripheral nerve injury and are secreted by Schwann cells. Neurons of the peripheral nervous system express integrin receptors that attach to laminins and promote neuroregeneration after injury. ^[14]

Pathology

Dysfunctional structure of one particular laminin, laminin-211, is the cause of one form of congenital muscular dystrophy. ^[15] Laminin-211 is composed of α2, β1, and γ1 chains. This laminin's distribution includes the brain and muscle fibers. In muscle, it binds to alpha-dystroglycan and integrin alpha7—beta1 via the G domain, and via the other end, it binds to the extracellular matrix.

Abnormal laminin-332, essential for epithelial cell adhesion to the basement membrane, leads to junctional epidermolysis bullosa, characterized by generalized blisters, exuberant granulation tissue of the skin and mucosa, and pitted teeth.

Malfunctional laminin-521 in the kidney filter causes leakage of protein into the urine and nephrotic syndrome. ^[5]

Role in cancer

Some of the laminin isoforms have been implicated in cancer pathophysiology. The majority of transcripts that harbor an internal ribosome entry site (IRES) are involved in cancer development via corresponding proteins. A crucial event in tumor progression, referred to as the epithelial-to-mesenchymal transition (EMT) allows carcinoma cells to acquire invasive properties. The translational activation of the extracellular matrix component laminin B1 (LAMB1) during EMT has been recently reported, suggesting an IRES-mediated mechanism. The IRES activity of LamB1 was determined by independent bicistronic reporter assays. Strong evidence excludes an impact of cryptic promoter or splice sites on IRES-driven translation of LamB1. Furthermore, no other LamB1 mRNA species arising from alternative transcription start sites or polyadenylation signals were detected that account for its translational control. Mapping of the LamB1 5'-untranslated region (UTR) revealed the minimal LamB1 IRES motif between -293 and -1 upstream of the start codon. RNA affinity purification demonstrated that the La protein interacts with the LamB1 IRES. This interaction and its regulation during EMT were confirmed by ribonucleoprotein immunoprecipitation. La is able to positively modulate LamB1 IRES translation, so LamB1 IRES is activated by binding to La which leads to translational upregulation during hepatocellular EMT. ^[16]

Use in cell culture

Together with other major components of the ECM, such as collagens and fibronectin, laminins have been used to enhance mammalian cell culture, especially in the case of pluripotent stem cells, as well as some primary cell cultures, which can be difficult to propagate on other substrates. Two types of naturally-sourced laminins are commercially available: Laminin-111, extracted from mouse sarcomas, and laminin mixtures from human placenta, which may primarily correspond to laminin-211, 411, or 511, depending on the provider. ^[17] The various laminin isoforms are practically impossible to isolate from tissues in pure form due to extensive cross-linking and the need for harsh extraction conditions, such as proteolytic enzymes or low pH, that cause degradation. Therefore, recombinant laminins have been produced since the year 2000. ^[18] This made it possible to test if laminins could have a significant role in vitro as they have in the human body. In 2008, two groups independently showed that mouse embryonic stem cells can be grown for months on top of recombinant laminin-511. ^{[19] [20]} Later, Rodin et al. showed that recombinant laminin-511 can be used to create a xeno-free and defined cell culture environment to culture human pluripotent ES cells and human iPS cells. ^[21]

Laminin domains

Laminin Domain I
Identifiers
Symbol	Laminin_I
Pfam	PF06008
InterPro	IPR009254
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Laminin Domain II
Identifiers
Symbol	Laminin_II
Pfam	PF06009
InterPro	IPR010307
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Laminin B (Domain IV)
Identifiers
Symbol	Laminin_B
Pfam	PF00052
InterPro	IPR000034
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Laminin EGF-like (Domains III and V)
crystal structure of three consecutive laminin-type epidermal growth factor-like (le) modules of laminin gamma1 chain harboring the nidogen binding site
Identifiers
Symbol	Laminin_EGF
Pfam	PF00053
Pfam clan	CL0001
InterPro	IPR002049
PROSITE	PDOC00021
SCOP2	1tle / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Laminin G domain
laminin alpha 2 chain lg4-5 domain pair, ca1 site mutant
Identifiers
Symbol	Laminin_G_1
Pfam	PF00054
Pfam clan	CL0004
InterPro	IPR012679
SCOP2	1qu0 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Laminin G domain
the structure of the ligand-binding domain of neurexin 1beta: regulation of lns domain function by alternative splicing
Identifiers
Symbol	Laminin_G_2
Pfam	PF02210
Pfam clan	CL0004
InterPro	IPR012680
SMART	TSPN
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Laminin N-terminal (Domain VI)
Identifiers
Symbol	Laminin_N
Pfam	PF00055
Pfam clan	CL0202
InterPro	IPR008211
SMART	LamNT
SCOP2	1klo / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Laminins contain several conserved protein domains.

Laminin I and Laminin II

Laminins are trimeric molecules; laminin-1 is an alpha1 beta1 gamma1 trimer. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure. ^[22]

Laminin B

The laminin B domain (also known as domain IV) is an extracellular module of unknown function. It is found in a number of different proteins that include, heparan sulphate proteoglycan from basement membrane, a laminin-like protein from Caenorhabditis elegans and laminin. Laminin IV domain is not found in short laminin chains (alpha4 or beta3).

Laminin EGF-like

Beside different types of globular domains each laminin subunit contains, in its first half, consecutive repeats of about 60 amino acids in length that include eight conserved cysteines. ^[23] The tertiary structure of this domain is remotely similar in its N-terminus to that of the EGF-like module. ^{[24] [25]} It is also known as a 'LE' or 'laminin-type EGF-like' domain. The number of copies of the laminin EGF-like domain in the different forms of laminins is highly variable; from 3 up to 22 copies have been found. In mouse laminin gamma-1 chain, the seventh LE domain has been shown to be the only one that binds with a high affinity to nidogen. ^[26] The binding-sites are located on the surface within the loops C1-C3 and C5-C6. ^{[24] [25]} Long consecutive arrays of laminin EGF-like domains in laminins form rod-like elements of limited flexibility, which determine the spacing in the formation of laminin networks of basement membranes. ^{[27] [28]}

Laminin G

The laminin globular (G) domain, also known as the LNS (Laminin-alpha, Neurexin and Sex hormone-binding globulin) domain, is on average 177 amino acids in length and can be found in one to six copies in various laminin family members as well as in a large number of other extracellular proteins. ^[29] For example, all laminin alpha-chains have five laminin G domains, all collagen family proteins have one laminin G domain, the CNTNAP proteins have four laminin G domains, while neurexin 1 and 2 each hold six laminin G domains. On average, approximately one quarter of the proteins that hold laminin G domains is taken up by these laminin G domains themselves. The smallest laminin G domain can be found in one of the collagen proteins (COL24A1; 77 AA) and the largest domain in TSPEAR (219 AA).

The exact function of the Laminin G domains has remained elusive, and a variety of binding functions has been ascribed to different Laminin G modules. For example, the laminin alpha1 and alpha2 chains each have five C-terminal laminin G domains, where only domains LG4 and LG5 contain binding sites for heparin, sulphatides and the cell surface receptor dystroglycan. ^[30] Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion, signalling, migration, assembly and differentiation.

Laminin N-terminal

Basement membrane assembly is a cooperative process in which laminins polymerise through their N-terminal domain (LN or domain VI) and anchor to the cell surface through their G domains. Netrins may also associate with this network through heterotypic LN domain interactions. ^[28] This leads to cell signalling through integrins and dystroglycan (and possibly other receptors) recruited to the adherent laminin. This LN domain-dependent self-assembly is considered to be crucial for the integrity of basement membranes, as highlighted by genetic forms of muscular dystrophy containing the deletion of the LN module from the alpha 2 laminin chain. ^[31] The laminin N-terminal domain is found in all laminin and netrin subunits except laminin alpha 3A, alpha 4 and gamma 2.

Human proteins containing laminin domains

• Laminin domain I: all laminin alpha chains (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5)
• Laminin domain II: all laminin alpha chains (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5)
• Laminin B (domain IV): all laminin alpha chains (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5), gamma chains (LAMC1, LAMC2, LAMC3), and perlecan (HSPG2)
• Laminin EGF-like (domains III and V): all laminin chains (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5, LAMB1, LAMB2, LAMB3, LAMB4, LAMC1, LAMC2, LAMC3), attractins (ATRN, ATRNL1), cadherin EGF LAG seven-pass G-type receptors (CELSR1, CELSR2, CELSR3), cysteine-rich with EGF-like domain proteins (CRELD1, CRELD2), multiple EGF-like domain proteins (MEGF6, MEGF8, MEGF9, MEGF10, PEAR1), most netrins (NTN1, NTN3, NTN4, NTNG1, NTNG2), mucins 3A and 3B (MUC3A, MUC3B), class F scavenger receptors (SCARF1, SCARF2), stabilins (STAB1, STAB2), agrin (AGRIN), angiopoietin-1 receptor (TEK), perlecan (HSPG2), tenascin N (TNN), and usherin (USH2A).
• Laminin G domain: all laminin alpha chains (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5), cadherin EGF LAG seven-pass G-type receptors (CELSR1, CELSR2, CELSR3), contactin-associated proteins (CNTNAP1, CNTNAP2, CNTNAP3, CNTNAP3B, CNTNAP4, CNTNAP5), some collagens (COL5A1, COL5A3, COL9A1, COL11A1, COL11A2, COL12A1, COL14A1, COL15A1, COL16A1, COL18A1, COL19A1, COL20A1, COL21A1, COL22A1, COL24A1, COL27A1), crumbs homologs 1 and 2 (CRB1, CRB2), fat homologs (FAT1, FAT2, FAT3, FAT4), NEL-like proteins (NELL1, NELL2), neurexins (NRXN1, NRXN2, NRXN3), slit homologs (SLIT1, SLIT2, SLIT3), thrombospondins (THBS1, THBS2, THBS3, THBS4, TSPEAR), agrin (AGRIN), chondroitin sulfate proteoglycan 4 (CSPG4), eyes shut homolog (EYS), growth arrest-specific protein 6 (GAS6), perlecan (HSPG2), pikachurin (EGFLAM), protein S (PROS1), sex hormone-binding globulin (SHBG) and usherin (USH2A)
• Laminin N-terminal (domain VI): most laminin chains (LAMA1, LAMA2, LAMA3, LAMA5, LAMB1, LAMB2, LAMB3, LAMB4, LAMC1, LAMC3), most netrins (NTN1, NTN3, NTN4, NTNG1, NTNG2), and usherin (USH2A)

See also

• Substrate adhesion molecules
• Laminin database
• List of target antigens in pemphigoid

References

1. Timpl R, Rohde H, Robey PG, Rennard SI, Foidart JM, Martin GR (October 1979). "Laminin--a glycoprotein from basement membranes". The Journal of Biological Chemistry. 254 (19): 9933–9937. doi: 10.1016/S0021-9258(19)83607-4 . PMID   114518.
2. Durbeej M (January 2010). "Laminins". Cell and Tissue Research. 339 (1): 259–268. doi:10.1007/s00441-009-0838-2. PMID   19693542.
3. Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, et al. (August 2005). "A simplified laminin nomenclature". Matrix Biology. 24 (5): 326–332. doi:10.1016/j.matbio.2005.05.006. PMID   15979864.
4. Haralson MA, Hassell JR (1995). Extracellular Matrix: A Practical Approach. IRL Press. ISBN   978-0-19-963220-6.^{[ page needed ]}
5. Yurchenco PD, Patton BL (2009). "Developmental and pathogenic mechanisms of basement membrane assembly". Current Pharmaceutical Design. 15 (12): 1277–1294. doi:10.2174/138161209787846766. PMC   2978668 . PMID   19355968.
6. Colognato H, Yurchenco PD (June 2000). "Form and function: the laminin family of heterotrimers". Developmental Dynamics. 218 (2): 213–234. doi: 10.1002/(SICI)1097-0177(200006)218:2<213::AID-DVDY1>3.0.CO;2-R . PMID   10842354.
7. von der Mark K, Sorokin L (2002). "Adhesive Glycoproteins". In Royce PM (ed.). Connective tissue and its heritable disorders: molecular, genetic, and medical aspects (2nd ed.). New York: Wiley-Liss. p. 306. ISBN   978-0-471-25185-9.
8. Kühn K (1997). "Extracellular matrix constituents as integrin ligands". In Elbe JA (ed.). Integrin-ligand interaction. New York: Chapman & Hall. p. 50. ISBN   978-0-412-13861-4.
9. Smith J, Ockleford CD (January 1994). "Laser scanning confocal examination and comparison of nidogen (entactin) with laminin in term human amniochorion". Placenta. 15 (1): 95–106. doi:10.1016/S0143-4004(05)80240-1. PMID   8208674.
10. Ockleford C, Bright N, Hubbard A, D'Lacey C, Smith J, Gardiner L, et al. (October 1993). "Micro-trabeculae, macro-plaques or mini-basement membranes in human term fetal membranes?". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 342 (1300): 121–136. doi:10.1098/rstb.1993.0142. PMID   7904354.
11. Beck et al., 1999.^{[ specify ]}
12. Ichikawa N, Kasai S, Suzuki N, Nishi N, Oishi S, Fujii N, et al. (April 2005). "Identification of neurite outgrowth active sites on the laminin alpha4 chain G domain". Biochemistry. 44 (15): 5755–5762. doi:10.1021/bi0476228. PMID   15823034.
13. Beckmann G, Hanke J, Bork P, Reich JG (February 1998). "Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins". Journal of Molecular Biology. 275 (5): 725–730. doi:10.1006/jmbi.1997.1510. PMID   9480764.
14. Nieuwenhuis B, Haenzi B, Andrews MR, Verhaagen J, Fawcett JW (August 2018). "Integrins promote axonal regeneration after injury of the nervous system". Biological Reviews of the Cambridge Philosophical Society. 93 (3): 1339–1362. doi:10.1111/brv.12398. PMC   6055631 . PMID   29446228.
15. Hall TE, Bryson-Richardson RJ, Berger S, Jacoby AS, Cole NJ, Hollway GE, et al. (April 2007). "The zebrafish candyfloss mutant implicates extracellular matrix adhesion failure in laminin alpha2-deficient congenital muscular dystrophy". Proceedings of the National Academy of Sciences of the United States of America. 104 (17): 7092–7097. Bibcode:2007PNAS..104.7092H. doi: 10.1073/pnas.0700942104 . PMC   1855385 . PMID   17438294.
16. Petz M, Them N, Huber H, Beug H, Mikulits W (January 2012). "La enhances IRES-mediated translation of laminin B1 during malignant epithelial to mesenchymal transition". Nucleic Acids Research. 40 (1): 290–302. doi:10.1093/nar/gkr717. PMC   3245933 . PMID   21896617.
17. Wondimu Z, Gorfu G, Kawataki T, Smirnov S, Yurchenco P, Tryggvason K, et al. (March 2006). "Characterization of commercial laminin preparations from human placenta in comparison to recombinant laminins 2 (α2β1γ1), 8 (α4β1γ1), 10 (α5β1γ1)". Matrix Biology. 25 (2): 89–93. doi:10.1016/j.matbio.2005.10.001. PMID   16289578.
18. Kortesmaa J, Yurchenco P, Tryggvason K (May 2000). "Recombinant Laminin-8 (α4β1γ1) Production, purification,and interactions with integrins". The Journal of Biological Chemistry. 275 (20): 14853–14859. doi: 10.1074/jbc.275.20.14853 . PMID   10809728.
19. Domogatskaya A, Rodin S, Boutaud A, Tryggvason K (November 2008). "Laminin-511 but not -332, -111, or -411 enables mouse embryonic stem cell self-renewal in vitro". Stem Cells. 26 (11): 2800–2809. doi: 10.1634/stemcells.2007-0389 . PMID   18757303.
20. Miyazaki T, Futaki S, Hasegawa K, Kawasaki M, Sanzen N, Hayashi M, et al. (October 2008). "Recombinant human laminin isoforms can support the undifferentiated growth of human embryonic stem cells". Biochemical and Biophysical Research Communications. 375 (1): 27–32. doi:10.1016/j.bbrc.2008.07.111. PMID   18675790.
21. Rodin S, Domogatskaya A, Ström S, Hansson EM, Chien KR, Inzunza J, et al. (June 2010). "Long-term self-renewal of human pluripotent stem cells on human recombinant laminin-511". Nature Biotechnology. 28 (6): 611–615. doi:10.1038/nbt.1620. hdl: 10616/40259 . PMID   20512123. S2CID   10801152.
22. Sasaki M, Kleinman HK, Huber H, Deutzmann R, Yamada Y (November 1988). "Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains". The Journal of Biological Chemistry. 263 (32): 16536–16544. doi: 10.1016/S0021-9258(18)37424-6 . PMID   3182802.
23. Engel J (July 1989). "EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation?". FEBS Letters. 251 (1–2): 1–7. doi: 10.1016/0014-5793(89)81417-6 . PMID   2666164. S2CID   36607427.
24. Stetefeld J, Mayer U, Timpl R, Huber R (April 1996). "Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site". Journal of Molecular Biology. 257 (3): 644–657. doi:10.1006/jmbi.1996.0191. PMID   8648630.
25. Baumgartner R, Czisch M, Mayer U, Pöschl E, Huber R, Timpl R, et al. (April 1996). "Structure of the nidogen binding LE module of the laminin gamma1 chain in solution". Journal of Molecular Biology. 257 (3): 658–668. doi:10.1006/jmbi.1996.0192. PMID   8648631.
26. Mayer U, Pöschl E, Gerecke DR, Wagman DW, Burgeson RE, Timpl R (May 1995). "Low nidogen affinity of laminin-5 can be attributed to two serine residues in EGF-like motif gamma 2III4". FEBS Letters. 365 (2–3): 129–132. doi: 10.1016/0014-5793(95)00438-F . PMID   7781764. S2CID   21559588.
27. Beck K, Hunter I, Engel J (February 1990). "Structure and function of laminin: anatomy of a multidomain glycoprotein". FASEB Journal. 4 (2): 148–160. doi: 10.1096/fasebj.4.2.2404817 . PMID   2404817.
28. Yurchenco PD, Cheng YS (August 1993). "Self-assembly and calcium-binding sites in laminin. A three-arm interaction model". The Journal of Biological Chemistry. 268 (23): 17286–17299. doi: 10.1016/S0021-9258(19)85334-6 . PMID   8349613.
29. "Laminin G domain". InterPro . European Bioinformatics Institute . Retrieved 22 February 2016.
30. Tisi D, Talts JF, Timpl R, Hohenester E (April 2000). "Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin". The EMBO Journal. 19 (7): 1432–1440. doi:10.1093/emboj/19.7.1432. PMC   310212 . PMID   10747011.
31. Xu H, Wu XR, Wewer UM, Engvall E (November 1994). "Murine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene". Nature Genetics. 8 (3): 297–302. doi:10.1038/ng1194-297. PMID   7874173. S2CID   21549628.

External links

• The Laminin Protein
• Laminin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Overview of all the structural information available in the PDB for UniProt : P19137 (Laminin subunit alpha-1) at the PDBe-KB .
• Overview of all the structural information available in the PDB for UniProt : P24043 (Laminin subunit alpha-2) at the PDBe-KB .
• Overview of all the structural information available in the PDB for UniProt : O15230 (Laminin subunit alpha-5) at the PDBe-KB .
• "How I learned to love laminin". YouTube. Imperial College London. April 13, 2011. (lecture by Professor Erhard Hoheneseter)

This article incorporates text from the public domain Pfam and InterPro:

• IPR002049
• IPR012679
• IPR012680
• IPR009254
• IPR010307
• IPR008211
• IPR000034