Laminin, alpha 3: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Laminin subunit alpha-3''' is a [[protein]] that in humans is encoded by the ''LAMA3'' [[gene]].<ref name="pmid8077230">{{cite journal | vauthors = Ryan MC, Tizard R, VanDevanter DR, Carter WG | title = Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair | journal = J Biol Chem | volume = 269 | issue = 36 | pages = 22779–87 | date = Oct 1994 | pmid = 8077230 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LAMA3 laminin, alpha 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3909| 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 3
| HGNCid = 6483
| Symbol = LAMA3
| AltSymbols =; E170; LAMNA; LOCS; lama3a
| OMIM = 600805
| ECnumber = 
| Homologene = 18279
| MGIid = 99909
| GeneAtlas_image1 = PBB_GE_LAMA3_203726_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_LAMA3_gnf1h02350_at_tn.png
| GeneAtlas_image3 = PBB_GE_LAMA3_gnf1h02351_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005606 |text = laminin-1 complex}}
| Process = {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{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 = 3909
    | Hs_Ensembl = ENSG00000053747
    | Hs_RefseqProtein = NP_000218
    | Hs_RefseqmRNA = NM_000227
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 18
    | Hs_GenLoc_start = 19523560
    | Hs_GenLoc_end = 19789025
    | Hs_Uniprot = Q16787
    | Mm_EntrezGene = 16774
    | Mm_Ensembl = ENSMUSG00000024421
    | Mm_RefseqmRNA = XM_140451
    | Mm_RefseqProtein = XP_140451
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 12477560
    | Mm_GenLoc_end = 12725832
    | Mm_Uniprot = Q3UU65
  }}
}}
'''Laminin, alpha 3''', also known as '''LAMA3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMA3 laminin, alpha 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3909| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Laminins are basement membrane components thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. The protein encoded by this gene is the alpha-3 chain of laminin 5, which is a complex glycoprotein composed of three subunits (alpha, beta, and gamma). Alternatively spliced transcript variants encoding different isoforms have been identified.  
{{PBB_Summary
| section_title =
| summary_text = Laminins are basement membrane components thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. The protein encoded by this gene is the alpha-3 chain of laminin 5, which is a complex glycoprotein composed of three subunits (alpha, beta, and gamma). Laminin 5 is thought to be involved in cell adhesion, signal transduction and differentiation of keratinocytes. Mutations in this gene have been identified as the cause of Herlitz type junctional epidermolysis bullosa. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: LAMA3 laminin, alpha 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3909| accessdate = }}</ref>
}}


==References==
Laminin 5 is thought to be involved in cell adhesion, signal transduction and differentiation of keratinocytes.<ref name="entrez" />
{{reflist|2}}
 
==Further reading==
==Clinical significance==
{{refbegin | 2}}
Mutations in this gene have been identified as the cause of Herlitz type [[Junctional epidermolysis bullosa (medicine)|junctional epidermolysis bullosa]]. <ref name="entrez" />
{{PBB_Further_reading
 
| citations =  
It may be associated with [[Laryngoonychocutaneous syndrome]].<ref name="pmid12915477">{{cite journal | vauthors = McLean WH, Irvine AD, Hamill KJ, Whittock NV, Coleman-Campbell CM, Mellerio JE, Ashton GS, Dopping-Hepenstal PJ, Eady RA, Jamil T, Phillips R, Shabbir SG, Haroon TS, Khurshid K, Moore JE, Page B, Darling J, Atherton DJ, Van Steensel MA, Munro CS, Smith FJ, McGrath JA, Phillips RJ | title = An unusual N-terminal deletion of the laminin alpha3a isoform leads to the chronic granulation tissue disorder laryngo-onycho-cutaneous syndrome | journal = Hum. Mol. Genet. | volume = 12 | issue = 18 | pages = 2395–409 | date = September 2003 | pmid = 12915477 | doi = 10.1093/hmg/ddg234 | url = http://hmg.oxfordjournals.org/cgi/pmidlookup?view=long&pmid=12915477 }}</ref>
*{{cite journal | author=Timpl R |title=Macromolecular organization of basement membranes. |journal=Curr. Opin. Cell Biol. |volume=8 |issue= 5 |pages= 618-24 |year= 1997 |pmid= 8939648 |doi= }}
 
*{{cite journal  | author=Kivirikko S, McGrath JA, Baudoin C, ''et al.'' |title=A homozygous nonsense mutation in the alpha 3 chain gene of laminin 5 (LAMA3) in lethal (Herlitz) junctional epidermolysis bullosa. |journal=Hum. Mol. Genet. |volume=4 |issue= 5 |pages= 959-62 |year= 1995 |pmid= 7633458 |doi= }}
== Interactions ==
*{{cite journal  | author=Rousselle P, Golbik R, van der Rest M, Aumailley M |title=Structural requirement for cell adhesion to kalinin (laminin-5). |journal=J. Biol. Chem. |volume=270 |issue= 23 |pages= 13766-70 |year= 1995 |pmid= 7775432 |doi= }}
 
*{{cite journal | author=Burgeson RE, Chiquet M, Deutzmann R, ''et al.'' |title=A new nomenclature for the laminins. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 209-11 |year= 1994 |pmid= 7921537 |doi= }}
Laminin, alpha 3 has been shown to [[Protein-protein interaction|interact]] with [[SDC2]].<ref name=pmid11373281>{{cite journal | vauthors = Utani A, Nomizu M, Matsuura H, Kato K, Kobayashi T, Takeda U, Aota S, Nielsen PK, Shinkai H | title = A unique sequence of the laminin alpha 3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4  | journal = J. Biol. Chem. | volume = 276 | issue = 31 | pages = 28779–88 | date = Aug 2001 | pmid = 11373281 | doi = 10.1074/jbc.M101420200 }}</ref>
*{{cite journal | author=Ryan MC, Tizard R, VanDevanter DR, Carter WG |title=Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair. |journal=J. Biol. Chem. |volume=269 |issue= 36 |pages= 22779-87 |year= 1994 |pmid= 8077230 |doi= }}
 
*{{cite journal | author=Vidal F, Baudoin C, Miquel C, ''et al.'' |title=Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with Herlitz junctional epidermolysis bullosa. |journal=Genomics |volume=30 |issue= 2 |pages= 273-80 |year= 1996 |pmid= 8586427 |doi= 10.1006/geno.1995.9877 }}
== References ==
*{{cite journal | author=McGrath JA, Kivirikko S, Ciatti S, ''et al.'' |title=A recurrent homozygous nonsense mutation within the LAMA3 gene as a cause of Herlitz junctional epidermolysis bullosa in patients of Pakistani ancestry: evidence for a founder effect. |journal=J. Invest. Dermatol. |volume=106 |issue= 4 |pages= 781-4 |year= 1996 |pmid= 8618022 |doi= }}
{{reflist}}
*{{cite journal | author=Mizushima H, Miyagi Y, Kikkawa Y, ''et al.'' |title=Differential expression of laminin-5/ladsin subunits in human tissues and cancer cell lines and their induction by tumor promoter and growth factors. |journal=J. Biochem. |volume=120 |issue= 6 |pages= 1196-202 |year= 1997 |pmid= 9010770 |doi= }}
 
*{{cite journal | author=Miner JH, Patton BL, Lentz SI, ''et al.'' |title=The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform. |journal=J. Cell Biol. |volume=137 |issue= 3 |pages= 685-701 |year= 1997 |pmid= 9151674 |doi= }}
== Further reading ==
*{{cite journal | author=Doliana R, Bellina I, Bucciotti F, ''et al.'' |title=The human alpha3b is a 'full-sized' laminin chain variant with a more widespread tissue expression than the truncated alpha3a. |journal=FEBS Lett. |volume=417 |issue= 1 |pages= 65-70 |year= 1998 |pmid= 9395076 |doi= }}
{{refbegin|35em}}
*{{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 = Timpl R | title = Macromolecular organization of basement membranes | journal = Curr. Opin. Cell Biol. | volume = 8 | issue = 5 | pages = 618–24 | year = 1997 | pmid = 8939648 | doi = 10.1016/S0955-0674(96)80102-5 }}
*{{cite journal | author=Pulkkinen L, Cserhalmi-Friedman PB, Tang M, ''et al.'' |title=Molecular analysis of the human laminin alpha3a chain gene (LAMA3a): a strategy for mutation identification and DNA-based prenatal diagnosis in Herlitz junctional epidermolysis bullosa. |journal=Lab. Invest. |volume=78 |issue= 9 |pages= 1067-76 |year= 1998 |pmid= 9759651 |doi=  }}
* {{cite journal | vauthors = Kivirikko S, McGrath JA, Baudoin C, Aberdam D, Ciatti S, Dunnill MG, McMillan JR, Eady RA, Ortonne JP, Meneguzzi G | title = A homozygous nonsense mutation in the alpha 3 chain gene of laminin 5 (LAMA3) in lethal (Herlitz) junctional epidermolysis bullosa | journal = Hum. Mol. Genet. | volume = 4 | issue = 5 | pages = 959–62 | year = 1995 | pmid = 7633458 | doi = 10.1093/hmg/4.5.959 }}
*{{cite journal | author=Gonzales M, Haan K, Baker SE, ''et al.'' |title=A cell signal pathway involving laminin-5, alpha3beta1 integrin, and mitogen-activated protein kinase can regulate epithelial cell proliferation. |journal=Mol. Biol. Cell |volume=10 |issue= 2 |pages= 259-70 |year= 1999 |pmid= 9950675 |doi=  }}
* {{cite journal | vauthors = Rousselle P, Golbik R, van der Rest M, Aumailley M | title = Structural requirement for cell adhesion to kalinin (laminin-5) | journal = J. Biol. Chem. | volume = 270 | issue = 23 | pages = 13766–70 | year = 1995 | pmid = 7775432 | doi = 10.1074/jbc.270.23.13766 }}
*{{cite journal | author=Hirosaki T, Mizushima H, Tsubota Y, ''et al.'' |title=Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22495-502 |year= 2000 |pmid= 10801807 |doi= 10.1074/jbc.M001326200 }}
* {{cite journal | vauthors = Burgeson RE, Chiquet M, Deutzmann R, Ekblom P, Engel J, Kleinman H, Martin GR, Meneguzzi G, Paulsson M, Sanes J | title = A new nomenclature for the laminins | journal = Matrix Biol. | volume = 14 | issue = 3 | pages = 209–11 | year = 1994 | pmid = 7921537 | doi = 10.1016/0945-053X(94)90184-8 }}
*{{cite journal | author=Amano S, Scott IC, Takahara K, ''et al.'' |title=Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 22728-35 |year= 2000 |pmid= 10806203 |doi= 10.1074/jbc.M002345200 }}
* {{cite journal | vauthors = Vidal F, Baudoin C, Miquel C, Galliano MF, Christiano AM, Uitto J, Ortonne JP, Meneguzzi G | title = Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with Herlitz junctional epidermolysis bullosa | journal = Genomics | volume = 30 | issue = 2 | pages = 273–80 | year = 1996 | pmid = 8586427 | doi = 10.1006/geno.1995.9877 }}
*{{cite journal | author=Goldfinger LE, Jiang L, Hopkinson SB, ''et al.'' |title=Spatial regulation and activity modulation of plasmin by high affinity binding to the G domain of the alpha 3 subunit of laminin-5. |journal=J. Biol. Chem. |volume=275 |issue= 45 |pages= 34887-93 |year= 2001 |pmid= 10956663 |doi= 10.1074/jbc.M006652200 }}
* {{cite journal | vauthors = McGrath JA, Kivirikko S, Ciatti S, Moss C, Christiano AM, Uitto J | title = A recurrent homozygous nonsense mutation within the LAMA3 gene as a cause of Herlitz junctional epidermolysis bullosa in patients of Pakistani ancestry: evidence for a founder effect | journal = J. Invest. Dermatol. | volume = 106 | issue = 4 | pages = 781–4 | year = 1996 | pmid = 8618022 | doi = 10.1111/1523-1747.ep12346349 }}
*{{cite journal | author=Fujiwara H, Kikkawa Y, Sanzen N, Sekiguchi K |title=Purification and characterization of human laminin-8. Laminin-8 stimulates cell adhesion and migration through alpha3beta1 and alpha6beta1 integrins. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17550-8 |year= 2001 |pmid= 11278628 |doi= 10.1074/jbc.M010155200 }}
* {{cite journal | vauthors = Mizushima H, Miyagi Y, Kikkawa Y, Yamanaka N, Yasumitsu H, Misugi K, Miyazaki K | title = Differential expression of laminin-5/ladsin subunits in human tissues and cancer cell lines and their induction by tumor promoter and growth factors | journal = J. Biochem. | volume = 120 | issue = 6 | pages = 1196–202 | year = 1997 | pmid = 9010770 | doi = 10.1093/oxfordjournals.jbchem.a021541 }}
*{{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 = Miner JH, Patton BL, Lentz SI, Gilbert DJ, Snider WD, Jenkins NA, Copeland NG, Sanes JR | title = The Laminin α Chains: Expression, Developmental Transitions, and Chromosomal Locations of α1-5, Identification of Heterotrimeric Laminins 8–11, and Cloning of a Novel α3 Isoform | journal = J. Cell Biol. | volume = 137 | issue = 3 | pages = 685–701 | year = 1997 | pmid = 9151674 | pmc = 2139892 | doi = 10.1083/jcb.137.3.685 }}
*{{cite journal  | author=Utani A, Nomizu M, Matsuura H, ''et al.'' |title=A unique sequence of the laminin alpha 3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 28779-88 |year= 2001 |pmid= 11373281 |doi= 10.1074/jbc.M101420200 }}
* {{cite journal | vauthors = Doliana R, Bellina I, Bucciotti F, Mongiat M, Perris R, Colombatti A | title = The human alpha3b is a 'full-sized' laminin chain variant with a more widespread tissue expression than the truncated alpha3a | journal = FEBS Lett. | volume = 417 | issue = 1 | pages = 65–70 | year = 1998 | pmid = 9395076 | doi = 10.1016/S0014-5793(97)01251-9 }}
}}
* {{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 = Arch. Immunol. Ther. Exp. (Warsz.) | volume = 45 | issue = 2–3 | pages = 255–9 | year = 1998 | pmid = 9597096 | doi =  }}
* {{cite journal | vauthors = Pulkkinen L, Cserhalmi-Friedman PB, Tang M, Ryan MC, Uitto J, Christiano AM | title = Molecular analysis of the human laminin alpha3a chain gene (LAMA3a): a strategy for mutation identification and DNA-based prenatal diagnosis in Herlitz junctional epidermolysis bullosa | journal = Lab. Invest. | volume = 78 | issue = 9 | pages = 1067–76 | year = 1998 | pmid = 9759651 | doi =  }}
* {{cite journal | vauthors = Gonzales M, Haan K, Baker SE, Fitchmun M, Todorov I, Weitzman S, Jones JC | title = A Cell Signal Pathway Involving Laminin-5, α3β1 Integrin, and Mitogen-activated Protein Kinase Can Regulate Epithelial Cell Proliferation | journal = Mol. Biol. Cell | volume = 10 | issue = 2 | pages = 259–70 | year = 1999 | pmid = 9950675 | pmc = 25167 | doi = 10.1091/mbc.10.2.259 }}
* {{cite journal | vauthors = Hirosaki T, Mizushima H, Tsubota Y, Moriyama K, Miyazaki K | title = Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5 | journal = J. Biol. Chem. | volume = 275 | issue = 29 | pages = 22495–502 | year = 2000 | pmid = 10801807 | doi = 10.1074/jbc.M001326200 }}
* {{cite journal | vauthors = Amano S, Scott IC, Takahara K, Koch M, Champliaud MF, Gerecke DR, Keene DR, Hudson DL, Nishiyama T, Lee S, Greenspan DS, Burgeson RE | title = Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain | journal = J. Biol. Chem. | volume = 275 | issue = 30 | pages = 22728–35 | year = 2000 | pmid = 10806203 | doi = 10.1074/jbc.M002345200 }}
* {{cite journal | vauthors = Goldfinger LE, Jiang L, Hopkinson SB, Stack MS, Jones JC | title = Spatial regulation and activity modulation of plasmin by high affinity binding to the G domain of the alpha 3 subunit of laminin-5 | journal = J. Biol. Chem. | volume = 275 | issue = 45 | pages = 34887–93 | year = 2001 | pmid = 10956663 | doi = 10.1074/jbc.M006652200 }}
* {{cite journal | vauthors = Fujiwara H, Kikkawa Y, Sanzen N, Sekiguchi K | title = Purification and characterization of human laminin-8. Laminin-8 stimulates cell adhesion and migration through alpha3beta1 and alpha6beta1 integrins | journal = J. Biol. Chem. | volume = 276 | issue = 20 | pages = 17550–8 | year = 2001 | pmid = 11278628 | doi = 10.1074/jbc.M010155200 }}
* {{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 = Arch. Oral Biol. | volume = 46 | issue = 6 | pages = 545–55 | year = 2001 | pmid = 11311202 | doi = 10.1016/S0003-9969(01)00014-0 }}
* {{cite journal | vauthors = Utani A, Nomizu M, Matsuura H, Kato K, Kobayashi T, Takeda U, Aota S, Nielsen PK, Shinkai H | title = A unique sequence of the laminin alpha 3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4 | journal = J. Biol. Chem. | volume = 276 | issue = 31 | pages = 28779–88 | year = 2001 | pmid = 11373281 | doi = 10.1074/jbc.M101420200 }}
{{refend}}
{{refend}}


{{protein-stub}}
{{Fibrous proteins}}
{{WikiDoc Sources}}
 
[[Category:Laminins]]
 
 
{{gene-18-stub}}

Latest revision as of 01:47, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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

Laminin subunit alpha-3 is a protein that in humans is encoded by the LAMA3 gene.[1][2]

Function

Laminins are basement membrane components thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. The protein encoded by this gene is the alpha-3 chain of laminin 5, which is a complex glycoprotein composed of three subunits (alpha, beta, and gamma). Alternatively spliced transcript variants encoding different isoforms have been identified.

Laminin 5 is thought to be involved in cell adhesion, signal transduction and differentiation of keratinocytes.[2]

Clinical significance

Mutations in this gene have been identified as the cause of Herlitz type junctional epidermolysis bullosa. [2]

It may be associated with Laryngoonychocutaneous syndrome.[3]

Interactions

Laminin, alpha 3 has been shown to interact with SDC2.[4]

References

  1. ↑ Ryan MC, Tizard R, VanDevanter DR, Carter WG (Oct 1994). "Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair". J Biol Chem. 269 (36): 22779–87. PMID 8077230.
  2. ↑ 2.0 2.1 2.2 "Entrez Gene: LAMA3 laminin, alpha 3".
  3. ↑ McLean WH, Irvine AD, Hamill KJ, Whittock NV, Coleman-Campbell CM, Mellerio JE, Ashton GS, Dopping-Hepenstal PJ, Eady RA, Jamil T, Phillips R, Shabbir SG, Haroon TS, Khurshid K, Moore JE, Page B, Darling J, Atherton DJ, Van Steensel MA, Munro CS, Smith FJ, McGrath JA, Phillips RJ (September 2003). "An unusual N-terminal deletion of the laminin alpha3a isoform leads to the chronic granulation tissue disorder laryngo-onycho-cutaneous syndrome". Hum. Mol. Genet. 12 (18): 2395–409. doi:10.1093/hmg/ddg234. PMID 12915477.
  4. ↑ Utani A, Nomizu M, Matsuura H, Kato K, Kobayashi T, Takeda U, Aota S, Nielsen PK, Shinkai H (Aug 2001). "A unique sequence of the laminin alpha 3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4". J. Biol. Chem. 276 (31): 28779–88. doi:10.1074/jbc.M101420200. PMID 11373281.

Further reading

  • Timpl R (1997). "Macromolecular organization of basement membranes". Curr. Opin. Cell Biol. 8 (5): 618–24. doi:10.1016/S0955-0674(96)80102-5. PMID 8939648.
  • Kivirikko S, McGrath JA, Baudoin C, Aberdam D, Ciatti S, Dunnill MG, McMillan JR, Eady RA, Ortonne JP, Meneguzzi G (1995). "A homozygous nonsense mutation in the alpha 3 chain gene of laminin 5 (LAMA3) in lethal (Herlitz) junctional epidermolysis bullosa". Hum. Mol. Genet. 4 (5): 959–62. doi:10.1093/hmg/4.5.959. PMID 7633458.
  • Rousselle P, Golbik R, van der Rest M, Aumailley M (1995). "Structural requirement for cell adhesion to kalinin (laminin-5)". J. Biol. Chem. 270 (23): 13766–70. doi:10.1074/jbc.270.23.13766. PMID 7775432.
  • Burgeson RE, Chiquet M, Deutzmann R, Ekblom P, Engel J, Kleinman H, Martin GR, Meneguzzi G, Paulsson M, Sanes J (1994). "A new nomenclature for the laminins". Matrix Biol. 14 (3): 209–11. doi:10.1016/0945-053X(94)90184-8. PMID 7921537.
  • Vidal F, Baudoin C, Miquel C, Galliano MF, Christiano AM, Uitto J, Ortonne JP, Meneguzzi G (1996). "Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with Herlitz junctional epidermolysis bullosa". Genomics. 30 (2): 273–80. doi:10.1006/geno.1995.9877. PMID 8586427.
  • McGrath JA, Kivirikko S, Ciatti S, Moss C, Christiano AM, Uitto J (1996). "A recurrent homozygous nonsense mutation within the LAMA3 gene as a cause of Herlitz junctional epidermolysis bullosa in patients of Pakistani ancestry: evidence for a founder effect". J. Invest. Dermatol. 106 (4): 781–4. doi:10.1111/1523-1747.ep12346349. PMID 8618022.
  • Mizushima H, Miyagi Y, Kikkawa Y, Yamanaka N, Yasumitsu H, Misugi K, Miyazaki K (1997). "Differential expression of laminin-5/ladsin subunits in human tissues and cancer cell lines and their induction by tumor promoter and growth factors". J. Biochem. 120 (6): 1196–202. doi:10.1093/oxfordjournals.jbchem.a021541. PMID 9010770.
  • Miner JH, Patton BL, Lentz SI, Gilbert DJ, Snider WD, Jenkins NA, Copeland NG, Sanes JR (1997). "The Laminin α Chains: Expression, Developmental Transitions, and Chromosomal Locations of α1-5, Identification of Heterotrimeric Laminins 8–11, and Cloning of a Novel α3 Isoform". J. Cell Biol. 137 (3): 685–701. doi:10.1083/jcb.137.3.685. PMC 2139892. PMID 9151674.
  • Doliana R, Bellina I, Bucciotti F, Mongiat M, Perris R, Colombatti A (1998). "The human alpha3b is a 'full-sized' laminin chain variant with a more widespread tissue expression than the truncated alpha3a". FEBS Lett. 417 (1): 65–70. doi:10.1016/S0014-5793(97)01251-9. PMID 9395076.
  • Mrowiec T, Melchar C, Górski A (1998). "HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium". Arch. Immunol. Ther. Exp. (Warsz.). 45 (2–3): 255–9. PMID 9597096.
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