Laminin, alpha 5: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Laminin subunit alpha-5''' is a [[protein]] that in humans is encoded by the ''LAMA5'' [[gene]].<ref name="pmid9271224">{{cite journal | vauthors = Durkin ME, Loechel F, Mattei MG, Gilpin BJ, Albrechtsen R, Wewer UM | title = Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation | journal = FEBS Letters | volume = 411 | issue = 2-3 | pages = 296–300 | date = Jul 1997 | pmid = 9271224 | pmc =  | doi = 10.1016/S0014-5793(97)00686-8 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LAMA5 laminin, alpha 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3911| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Laminin, alpha 5
| HGNCid = 6485
| Symbol = LAMA5
| AltSymbols =; KIAA1907
| OMIM = 601033
| ECnumber = 
| Homologene = 4060
| MGIid = 105382
| GeneAtlas_image1 = PBB_GE_LAMA5_210150_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005605 |text = basal lamina}} {{GNF_GO|id=GO:0005606 |text = laminin-1 complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0030155 |text = regulation of cell adhesion}} {{GNF_GO|id=GO:0030334 |text = regulation of cell migration}} {{GNF_GO|id=GO:0045995 |text = regulation of embryonic development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3911
    | Hs_Ensembl = ENSG00000130702
    | Hs_RefseqProtein = NP_005551
    | Hs_RefseqmRNA = NM_005560
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 60317510
    | Hs_GenLoc_end = 60375763
    | Hs_Uniprot = O15230
    | Mm_EntrezGene = 16776
    | Mm_Ensembl = ENSMUSG00000015647
    | Mm_RefseqmRNA = XM_203796
    | Mm_RefseqProtein = XP_203796
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 180105782
    | Mm_GenLoc_end = 180155210
    | Mm_Uniprot = Q3TZ05
  }}
}}
'''Laminin, alpha 5''', also known as '''LAMA5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMA5 laminin, alpha 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3911| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Components of the extracellular matrix exert myriad effects on tissues throughout the body. In particular, the laminins, a family of heterotrimeric extracellular glycoproteins, affect tissue development and integrity in such diverse organs as the kidney, lung, skin, and nervous system. It is thought that laminins mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Laminins function as heterotrimeric complexes of alpha, beta, and gamma chains, with each chain type representing a different subfamily of proteins. The protein encoded by this gene belongs to the alpha subfamily of laminin chains and is a major component of basement membranes. Two transcript variants encoding different isoforms have been found for this gene, but the full-length nature of one of them has not been determined.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Components of the extracellular matrix exert myriad effects on tissues throughout the body. In particular, the laminins, a family of heterotrimeric extracellular glycoproteins, affect tissue development and integrity in such diverse organs as the kidney, lung, skin, and nervous system. It is thought that laminins mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Laminins function as heterotrimeric complexes of alpha, beta, and gamma chains, with each chain type representing a different subfamily of proteins. The protein encoded by this gene belongs to the alpha subfamily of laminin chains and is a major component of basement membranes. Two transcript variants encoding different isoforms have been found for this gene, but the full-length nature of one of them has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: LAMA5 laminin, alpha 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3911| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
Laminin, alpha 5 has been shown to [[Protein-protein interaction|interact]] with [[BCAM]].<ref name=pmid11133776>{{cite journal | vauthors = Parsons SF, Lee G, Spring FA, Willig TN, Peters LL, Gimm JA, Tanner MJ, Mohandas N, Anstee DJ, Chasis JA | title = Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity | journal = Blood | volume = 97 | issue = 1 | pages = 312–20 | date = Jan 2001 | pmid = 11133776 | doi = 10.1182/blood.V97.1.312 }}</ref><ref name=pmid12244066>{{cite journal | vauthors = Kikkawa Y, Moulson CL, Virtanen I, Miner JH | title = Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo | journal = The Journal of Biological Chemistry | volume = 277 | issue = 47 | pages = 44864–9 | date = Nov 2002 | pmid = 12244066 | doi = 10.1074/jbc.M208731200 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Utani A, Nomizu M, Yamada Y | title = Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences | journal = The Journal of Biological Chemistry | volume = 272 | issue = 5 | pages = 2814–20 | date = Jan 1997 | pmid = 9006922 | doi = 10.1074/jbc.272.5.2814 }}
| citations =
* {{cite journal | vauthors = Rousselle P, Keene DR, Ruggiero F, Champliaud MF, Rest M, Burgeson RE | title = Laminin 5 binds the NC-1 domain of type VII collagen | journal = The Journal of Cell Biology | volume = 138 | issue = 3 | pages = 719–28 | date = Aug 1997 | pmid = 9245798 | pmc = 2141627 | doi = 10.1083/jcb.138.3.719 }}
*{{cite journal | author=Utani A, Nomizu M, Yamada Y |title=Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 2814-20 |year= 1997 |pmid= 9006922 |doi= }}
* {{cite journal | vauthors = Tiger CF, Champliaud MF, Pedrosa-Domellof F, Thornell LE, Ekblom P, Gullberg D | title = Presence of laminin alpha5 chain and lack of laminin alpha1 chain during human muscle development and in muscular dystrophies | journal = The Journal of Biological Chemistry | volume = 272 | issue = 45 | pages = 28590–5 | date = Nov 1997 | pmid = 9353324 | doi = 10.1074/jbc.272.45.28590 }}
*{{cite journal | author=Rousselle P, Keene DR, Ruggiero F, ''et al.'' |title=Laminin 5 binds the NC-1 domain of type VII collagen. |journal=J. Cell Biol. |volume=138 |issue= 3 |pages= 719-28 |year= 1997 |pmid= 9245798 |doi= }}
* {{cite journal | vauthors = Mrowiec T, Melchar C, Górski A | title = HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium | journal = Archivum Immunologiae et Therapiae Experimentalis | volume = 45 | issue = 2-3 | pages = 255–9 | year = 1998 | pmid = 9597096 | doi =  }}
*{{cite journal | author=Durkin ME, Loechel F, Mattei MG, ''et al.'' |title=Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation. |journal=FEBS Lett. |volume=411 |issue= 2-3 |pages= 296-300 |year= 1997 |pmid= 9271224 |doi= }}
* {{cite journal | vauthors = Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro | journal = DNA Research | volume = 5 | issue = 1 | pages = 31–9 | date = Feb 1998 | pmid = 9628581 | doi = 10.1093/dnares/5.1.31 }}
*{{cite journal | author=Tiger CF, Champliaud MF, Pedrosa-Domellof F, ''et al.'' |title=Presence of laminin alpha5 chain and lack of laminin alpha1 chain during human muscle development and in muscular dystrophies. |journal=J. Biol. Chem. |volume=272 |issue= 45 |pages= 28590-5 |year= 1997 |pmid= 9353324 |doi=  }}
* {{cite journal | vauthors = Shimizu H, Hosokawa H, Ninomiya H, Miner JH, Masaki T | title = Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan | journal = The Journal of Biological Chemistry | volume = 274 | issue = 17 | pages = 11995–2000 | date = Apr 1999 | pmid = 10207021 | doi = 10.1074/jbc.274.17.11995 }}
*{{cite journal | author=Mrowiec T, Melchar C, Górski A |title=HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=45 |issue= 2-3 |pages= 255-9 |year= 1998 |pmid= 9597096 |doi= }}
* {{cite journal | vauthors = Son YJ, Scranton TW, Sunderland WJ, Baek SJ, Miner JH, Sanes JR, Carlson SS | title = The synaptic vesicle protein SV2 is complexed with an alpha5-containing laminin on the nerve terminal surface | journal = The Journal of Biological Chemistry | volume = 275 | issue = 1 | pages = 451–60 | date = Jan 2000 | pmid = 10617638 | doi = 10.1074/jbc.275.1.451 }}
*{{cite journal | author=Nagase T, Ishikawa K, Miyajima N, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 1 |pages= 31-9 |year= 1998 |pmid= 9628581 |doi= }}
* {{cite journal | vauthors = Köhler D, Kruse M, Stöcker W, Sterchi EE | title = Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro | journal = FEBS Letters | volume = 465 | issue = 1 | pages = 2–7 | date = Jan 2000 | pmid = 10620696 | doi = 10.1016/S0014-5793(99)01712-3 }}
*{{cite journal | author=Shimizu H, Hosokawa H, Ninomiya H, ''et al.'' |title=Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan. |journal=J. Biol. Chem. |volume=274 |issue= 17 |pages= 11995-2000 |year= 1999 |pmid= 10207021 |doi= }}
* {{cite journal | vauthors = Kikkawa Y, Sanzen N, Fujiwara H, Sonnenberg A, Sekiguchi K | title = Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins | journal = Journal of Cell Science | volume = 113 ( Pt 5) | issue = 5 | pages = 869–76 | date = Mar 2000 | pmid = 10671376 | doi =  }}
*{{cite journal | author=Son YJ, Scranton TW, Sunderland WJ, ''et al.'' |title=The synaptic vesicle protein SV2 is complexed with an alpha5-containing laminin on the nerve terminal surface. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 451-60 |year= 2000 |pmid= 10617638 |doi= }}
* {{cite journal | vauthors = Champliaud MF, Virtanen I, Tiger CF, Korhonen M, Burgeson R, Gullberg D | title = Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta | journal = Experimental Cell Research | volume = 259 | issue = 2 | pages = 326–35 | date = Sep 2000 | pmid = 10964500 | doi = 10.1006/excr.2000.4980 }}
*{{cite journal | author=Köhler D, Kruse M, Stöcker W, Sterchi EE |title=Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro. |journal=FEBS Lett. |volume=465 |issue= 1 |pages= 2-7 |year= 2000 |pmid= 10620696 |doi=  }}
* {{cite journal | vauthors = Libby RT, Champliaud MF, Claudepierre T, Xu Y, Gibbons EP, Koch M, Burgeson RE, Hunter DD, Brunken WJ | title = Laminin expression in adult and developing retinae: evidence of two novel CNS laminins | journal = The Journal of Neuroscience | volume = 20 | issue = 17 | pages = 6517–28 | date = Sep 2000 | pmid = 10964957 | pmc = 2924637 | doi = }}
*{{cite journal | author=Kikkawa Y, Sanzen N, Fujiwara H, ''et al.'' |title=Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins. |journal=J. Cell. Sci. |volume=113 ( Pt 5) |issue= |pages= 869-76 |year= 2000 |pmid= 10671376 |doi= }}
* {{cite journal | vauthors = Pierce RA, Griffin GL, Miner JH, Senior RM | title = Expression patterns of laminin alpha1 and alpha5 in human lung during development | journal = American Journal of Respiratory Cell and Molecular Biology | volume = 23 | issue = 6 | pages = 742–7 | date = Dec 2000 | pmid = 11104726 | doi = 10.1165/ajrcmb.23.6.4202 }}
*{{cite journal | author=Champliaud MF, Virtanen I, Tiger CF, ''et al.'' |title=Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 326-35 |year= 2000 |pmid= 10964500 |doi= 10.1006/excr.2000.4980 }}
* {{cite journal | vauthors = Parsons SF, Lee G, Spring FA, Willig TN, Peters LL, Gimm JA, Tanner MJ, Mohandas N, Anstee DJ, Chasis JA | title = Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity | journal = Blood | volume = 97 | issue = 1 | pages = 312–20 | date = Jan 2001 | pmid = 11133776 | doi = 10.1182/blood.V97.1.312 }}
*{{cite journal | author=Libby RT, Champliaud MF, Claudepierre T, ''et al.'' |title=Laminin expression in adult and developing retinae: evidence of two novel CNS laminins. |journal=J. Neurosci. |volume=20 |issue= 17 |pages= 6517-28 |year= 2000 |pmid= 10964957 |doi= }}
* {{cite journal | vauthors = Saghizadeh M, Brown DJ, Castellon R, Chwa M, Huang GH, Ljubimova JY, Rosenberg S, Spirin KS, Stolitenko RB, Adachi W, Kinoshita S, Murphy G, Windsor LJ, Kenney MC, Ljubimov AV | title = Overexpression of matrix metalloproteinase-10 and matrix metalloproteinase-3 in human diabetic corneas: a possible mechanism of basement membrane and integrin alterations | journal = The American Journal of Pathology | volume = 158 | issue = 2 | pages = 723–34 | date = Feb 2001 | pmid = 11159210 | pmc = 1850323 | doi = 10.1016/S0002-9440(10)64015-1 }}
*{{cite journal | author=Pierce RA, Griffin GL, Miner JH, Senior RM |title=Expression patterns of laminin alpha1 and alpha5 in human lung during development. |journal=Am. J. Respir. Cell Mol. Biol. |volume=23 |issue= 6 |pages= 742-7 |year= 2001 |pmid= 11104726 |doi= }}
* {{cite journal | vauthors = McArthur CP, Wang Y, Heruth D, Gustafson S | title = Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53 | journal = Archives of Oral Biology | volume = 46 | issue = 6 | pages = 545–55 | date = Jun 2001 | pmid = 11311202 | doi = 10.1016/S0003-9969(01)00014-0 }}
*{{cite journal | author=Parsons SF, Lee G, Spring FA, ''et al.'' |title=Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. |journal=Blood |volume=97 |issue= 1 |pages= 312-20 |year= 2001 |pmid= 11133776 |doi= }}
* {{cite journal | vauthors = Gagnoux-Palacios L, Allegra M, Spirito F, Pommeret O, Romero C, Ortonne JP, Meneguzzi G | title = The short arm of the laminin gamma2 chain plays a pivotal role in the incorporation of laminin 5 into the extracellular matrix and in cell adhesion | journal = The Journal of Cell Biology | volume = 153 | issue = 4 | pages = 835–50 | date = May 2001 | pmid = 11352943 | pmc = 2192378 | doi = 10.1083/jcb.153.4.835 }}
*{{cite journal | author=Saghizadeh M, Brown DJ, Castellon R, ''et al.'' |title=Overexpression of matrix metalloproteinase-10 and matrix metalloproteinase-3 in human diabetic corneas: a possible mechanism of basement membrane and integrin alterations. |journal=Am. J. Pathol. |volume=158 |issue= 2 |pages= 723-34 |year= 2001 |pmid= 11159210 |doi= }}
* {{cite journal | vauthors = Nagase T, Kikuno R, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins | journal = DNA Research | volume = 8 | issue = 4 | pages = 179–87 | date = Aug 2001 | pmid = 11572484 | doi = 10.1093/dnares/8.4.179 }}
*{{cite journal | author=McArthur CP, Wang Y, Heruth D, Gustafson S |title=Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53. |journal=Arch. Oral Biol. |volume=46 |issue= 6 |pages= 545-55 |year= 2001 |pmid= 11311202 |doi= }}
* {{cite journal | vauthors = Doi M, Thyboll J, Kortesmaa J, Jansson K, Iivanainen A, Parvardeh M, Timpl R, Hedin U, Swedenborg J, Tryggvason K | title = Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells | journal = The Journal of Biological Chemistry | volume = 277 | issue = 15 | pages = 12741–8 | date = Apr 2002 | pmid = 11821406 | doi = 10.1074/jbc.M111228200 }}
*{{cite journal | author=Gagnoux-Palacios L, Allegra M, Spirito F, ''et al.'' |title=The short arm of the laminin gamma2 chain plays a pivotal role in the incorporation of laminin 5 into the extracellular matrix and in cell adhesion. |journal=J. Cell Biol. |volume=153 |issue= 4 |pages= 835-50 |year= 2001 |pmid= 11352943 |doi= }}
*{{cite journal | author=Nagase T, Kikuno R, Ohara O |title=Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins. |journal=DNA Res. |volume=8 |issue= 4 |pages= 179-87 |year= 2002 |pmid= 11572484 |doi=  }}
*{{cite journal  | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal  | author=Doi M, Thyboll J, Kortesmaa J, ''et al.'' |title=Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 12741-8 |year= 2002 |pmid= 11821406 |doi= 10.1074/jbc.M111228200 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Fibrous proteins}}
{{WikiDoc Sources}}
 
[[Category:Laminins]]
 
 
{{gene-20-stub}}

Latest revision as of 01:42, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Laminin subunit alpha-5 is a protein that in humans is encoded by the LAMA5 gene.[1][2]

Function

Components of the extracellular matrix exert myriad effects on tissues throughout the body. In particular, the laminins, a family of heterotrimeric extracellular glycoproteins, affect tissue development and integrity in such diverse organs as the kidney, lung, skin, and nervous system. It is thought that laminins mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Laminins function as heterotrimeric complexes of alpha, beta, and gamma chains, with each chain type representing a different subfamily of proteins. The protein encoded by this gene belongs to the alpha subfamily of laminin chains and is a major component of basement membranes. Two transcript variants encoding different isoforms have been found for this gene, but the full-length nature of one of them has not been determined.[2]

Interactions

Laminin, alpha 5 has been shown to interact with BCAM.[3][4]

References

  1. ↑ Durkin ME, Loechel F, Mattei MG, Gilpin BJ, Albrechtsen R, Wewer UM (Jul 1997). "Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation". FEBS Letters. 411 (2–3): 296–300. doi:10.1016/S0014-5793(97)00686-8. PMID 9271224.
  2. ↑ 2.0 2.1 "Entrez Gene: LAMA5 laminin, alpha 5".
  3. ↑ Parsons SF, Lee G, Spring FA, Willig TN, Peters LL, Gimm JA, Tanner MJ, Mohandas N, Anstee DJ, Chasis JA (Jan 2001). "Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity". Blood. 97 (1): 312–20. doi:10.1182/blood.V97.1.312. PMID 11133776.
  4. ↑ Kikkawa Y, Moulson CL, Virtanen I, Miner JH (Nov 2002). "Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo". The Journal of Biological Chemistry. 277 (47): 44864–9. doi:10.1074/jbc.M208731200. PMID 12244066.

Further reading


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