Laminin, alpha 3

LAMA3
Identifiers
Aliases	LAMA3 , BM600, E170, LAMNA, LOCS, lama3a, Laminin, alpha 3, laminin subunit alpha 3, JEB2B, JEB2A, JEB2C
External IDs	OMIM: 600805 MGI: 99909 HomoloGene: 18279 GeneCards: LAMA3
Gene location (Human)
Chr.	Chromosome 18 (human)
End	23,956,222 bp
Gene location (Mouse)
Chr.	Chromosome 18 (mouse)
End	12,716,070 bp
RNA expression pattern
	Top expressed in
	right lung; ; periodontal fiber; ; skin of abdomen; ; jejunal mucosa; ; sural nerve; ; upper lobe of left lung; ; minor salivary gland; ; hair follicle; ; vagina; ; pancreatic ductal cell;
	Top expressed in
	molar; ; corneal stroma; ; left lung lobe; ; right lung lobe; ; conjunctival fornix; ; left colon; ; ileum; ; skin of back; ; cervix; ; jejunum;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	signaling receptor binding ; structural molecule activity ; extracellular matrix structural constituent ; integrin binding ;
Cellular component	extracellular region ; basement membrane ; laminin-5 complex ; extracellular exosome ; extracellular matrix ; endoplasmic reticulum ; collagen-containing extracellular matrix ;
Biological process	hemidesmosome assembly ; cell adhesion ; extracellular matrix disassembly ; regulation of cell adhesion ; extracellular matrix organization ; regulation of cell migration ; endodermal cell differentiation ; regulation of embryonic development ; epidermis development ; morphogenesis of a polarized epithelium ; integrin-mediated signaling pathway ; animal organ morphogenesis ; tissue development ; cell migration ; cell-cell adhesion ;
	Sources:Amigo / QuickGO
Orthologs
	3909
	16774
	ENSG00000053747
	ENSMUSG00000024421
	Q16787
	Q61789
	NM_000227 ; NM_001127717 ; NM_001127718 ; NM_001302996 ; NM_198129 Contents Function ; Clinical significance ; Interactions ; References ; Further reading ;
	NM_010680 ; NM_001347461
	NP_000218 ; NP_001121189 ; NP_001121190 ; NP_001289925 ; NP_937762
	NP_001334390 ; NP_034810
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 15, 2023

Laminin subunit alpha-3 is a protein that in humans is encoded by the LAMA3 gene.^[5]^[6]

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.^[6]

Clinical significance

Mutations in this gene have been identified as the cause of Herlitz type junctional epidermolysis bullosa. ^[6]

It may be associated with Laryngoonychocutaneous syndrome.^[7]

Interactions

Laminin, alpha 3 has been shown to interact with SDC2.^[8]

Related Research Articles

Hemidesmosomes are very small stud-like structures found in keratinocytes of the epidermis of skin that attach to the extracellular matrix. They are similar in form to desmosomes when visualized by electron microscopy, however, desmosomes attach to adjacent cells. Hemidesmosomes are also comparable to focal adhesions, as they both attach cells to the extracellular matrix. Instead of desmogleins and desmocollins in the extracellular space, hemidesmosomes utilize integrins. Hemidesmosomes are found in epithelial cells connecting the basal epithelial cells to the lamina lucida, which is part of the basal lamina. Hemidesmosomes are also involved in signaling pathways, such as keratinocyte migration or carcinoma cell intrusion.

<span class="mw-page-title-main">Laminin</span> Protein in the extracellular matrix

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. Laminins are vital to biological activity, influencing cell differentiation, migration, and adhesion.

Integrin alpha-3 is a protein that in humans is encoded by the ITGA3 gene. ITGA3 is an integrin alpha subunit. Together with beta-1 subunit, it makes up half of the α3β1 integrin duplex that plays a role in neural migration and corticogenesis, acted upon by such factors as netrin-1 and reelin.

Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion, identified by Diaz and colleagues in 1990.

Collagen alpha-1(VII) chain is a protein that in humans is encoded by the COL7A1 gene. It is composed of a triple helical, collagenous domain flanked by two non-collagenous domains, and functions as an anchoring fibril between the dermal-epidermal junction in the basement membrane. Mutations in COL7A1 cause all types of dystrophic epidermolysis bullosa, and the exact mutations vary based on the specific type or subtype. It has been shown that interactions between the NC-1 domain of collagen VII and several other proteins, including laminin-5 and collagen IV, contribute greatly to the overall stability of the basement membrane.

Integrin, beta 4 (ITGB4) also known as CD104, is a human gene.

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

Laminin subunit gamma-2 is a protein that in humans is encoded by the LAMC2 gene.

Laminin subunit beta-3 is a protein that in humans is encoded by the LAMB3 gene.

Laminin subunit alpha-1 is a protein that in humans is encoded by the LAMA1 gene.

Laminin subunit beta-1 is a protein that in humans is encoded by the LAMB1 gene.

Collagen alpha-6(IV) chain is a protein that in humans is encoded by the COL4A6 gene.

Alpha-7 integrin is a protein that in humans is encoded by the ITGA7 gene. Alpha-7 integrin is critical for modulating cell-matrix interactions. Alpha-7 integrin is highly expressed in cardiac muscle, skeletal muscle and smooth muscle cells, and localizes to Z-disc and costamere structures. Mutations in ITGA7 have been associated with congenital myopathies and noncompaction cardiomyopathy, and altered expression levels of alpha-7 integrin have been identified in various forms of muscular dystrophy.

Laminin subunit alpha-4 is a protein that in humans is encoded by the LAMA4 gene.

Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.

Laminin subunit beta-2 is a protein that in humans is encoded by the LAMB2 gene.

Basal cell adhesion molecule, also known as Lutheran antigen, is a plasma membrane glycoprotein that in humans is encoded by the BCAM gene. BCAM has also recently been designated CD239.

Integrin alpha-9 is a protein that in humans is encoded by the ITGA9 gene. Cytogenetic location: 3p22.2

Laminin subunit gamma-3 also known as LAMC3 is a protein that in humans is encoded by the LAMC3 gene.

Junctional epidermolysis bullosa is a skin condition characterized by blister formation within the lamina lucida of the basement membrane zone.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000053747 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024421 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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. doi: 10.1016/S0021-9258(17)31713-1 . PMID 8077230.
1 2 3 "Entrez Gene: LAMA3 laminin, alpha 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.
↑ 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.

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. S2CID 85823519.
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.
Pulkkinen L, Cserhalmi-Friedman PB, Tang M, Ryan MC, Uitto J, Christiano AM (1998). "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". Lab. Invest. 78 (9): 1067–76. PMID 9759651.
Gonzales M, Haan K, Baker SE, Fitchmun M, Todorov I, Weitzman S, Jones JC (1999). "A Cell Signal Pathway Involving Laminin-5, α3β1 Integrin, and Mitogen-activated Protein Kinase Can Regulate Epithelial Cell Proliferation". Mol. Biol. Cell. 10 (2): 259–70. doi:10.1091/mbc.10.2.259. PMC 25167 . PMID 9950675.
Hirosaki T, Mizushima H, Tsubota Y, Moriyama K, Miyazaki K (2000). "Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5". J. Biol. Chem. 275 (29): 22495–502. doi: 10.1074/jbc.M001326200 . PMID 10801807.
Amano S, Scott IC, Takahara K, Koch M, Champliaud MF, Gerecke DR, Keene DR, Hudson DL, Nishiyama T, Lee S, Greenspan DS, Burgeson RE (2000). "Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain". J. Biol. Chem. 275 (30): 22728–35. doi: 10.1074/jbc.M002345200 . PMID 10806203.
Goldfinger LE, Jiang L, Hopkinson SB, Stack MS, Jones JC (2001). "Spatial regulation and activity modulation of plasmin by high affinity binding to the G domain of the alpha 3 subunit of laminin-5". J. Biol. Chem. 275 (45): 34887–93. doi: 10.1074/jbc.M006652200 . PMID 10956663.
Fujiwara H, Kikkawa Y, Sanzen N, Sekiguchi K (2001). "Purification and characterization of human laminin-8. Laminin-8 stimulates cell adhesion and migration through alpha3beta1 and alpha6beta1 integrins". J. Biol. Chem. 276 (20): 17550–8. doi: 10.1074/jbc.M010155200 . PMID 11278628.
McArthur CP, Wang Y, Heruth D, Gustafson S (2001). "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". Arch. Oral Biol. 46 (6): 545–55. doi:10.1016/S0003-9969(01)00014-0. PMID 11311202.
Utani A, Nomizu M, Matsuura H, Kato K, Kobayashi T, Takeda U, Aota S, Nielsen PK, Shinkai H (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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000053747 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024421 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8077230-5] 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. doi: 10.1016/S0021-9258(17)31713-1 . PMID 8077230.

[entrez-6] 1 2 3 "Entrez Gene: LAMA3 laminin, alpha 3".

[pmid12915477-7] 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.

[pmid11373281-8] 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.

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