Laminina, alfa 1


La laminina, subunitat alfa-1 és una proteïna que en els humans és codificada pel gen LAMA1.[1][2]

Laminina, alfa 1
Símbols LAMA1 ; LAMA
Identif. externs OMIM150320 MGI99892 HomoloGene21146 GeneCards: LAMA1 Gene
Patró d'expressió d'ARN
PBB GE LAMA1 gnf1h03218 at tn.png
PBB GE LAMA1 gnf1h07866 at tn.png
More reference expression data
Espècies Humans Ratolins
Entrez 284217 16772
Ensembl ENSG00000101680 ENSMUSG00000032796
UniProt P25391 P19137
RefSeq (ARNm) XM_001130075 NM_008480
RefSeq (proteïna) XP_001130075 NP_032506
Localitz. (UCSC) Chr 18:
6.93 – 7.11 Mb
Chr 17:
67.6 – 67.73 Mb
Cerca al PubMed [1] [2]


La laminina, alfa 1 ha mostrat interaccionar amb la FBLN2.[3][4]


  1. Nagayoshi T, Mattei MG, Passage E, Knowlton R, Chu ML, Uitto J «Human laminin A chain (LAMA) gene: chromosomal mapping to locus 18p11.3». Genomics, 5, 4, Jan 1990, pàg. 932-5. PMID: 2591971.
  2. «Entrez Gene: LAMA1 laminin, alpha 1».
  3. Utani, A; Nomizu M, Yamada Y «Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences». J. Biol. Chem. [UNITED STATES], 272, 5, Jan. 1997, pàg. 2814-20. ISSN: 0021-9258. PMID: 9006922.
  4. Talts, J F; Sasaki T, Miosge N, Göhring W, Mann K, Mayne R, Timpl R «Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues». J. Biol. Chem. [UNITED STATES], 275, 45, Nov. 2000, pàg. 35192-9. DOI: 10.1074/jbc.M003261200. ISSN: 0021-9258. PMID: 10934193.

Bibliografia relacionadaModifica

  • Haaparanta T, Uitto J, Ruoslahti E, Engvall E «Molecular cloning of the cDNA encoding human laminin A chain.». Matrix, 11, 3, 1991, pàg. 151–60. PMID: 1714537.
  • Nissinen M, Vuolteenaho R, Boot-Handford R, et al. «Primary structure of the human laminin A chain. Limited expression in human tissues.». Biochem. J., 276 ( Pt 2), 1991, pàg. 369–79. PMID: 2049067.
  • Taraboletti G, Rao CN, Krutzsch HC, et al. «Sulfatide-binding domain of the laminin A chain.». J. Biol. Chem., 265, 21, 1990, pàg. 12253–8. PMID: 2373692.
  • Olsen D, Nagayoshi T, Fazio M, et al. «Human laminin: cloning and sequence analysis of cDNAs encoding A, B1 and B2 chains, and expression of the corresponding genes in human skin and cultured cells.». Lab. Invest., 60, 6, 1989, pàg. 772–82. PMID: 2733383.
  • Leivo I, Engvall E «C3d fragment of complement interacts with laminin and binds to basement membranes of glomerulus and trophoblast.». J. Cell Biol., 103, 3, 1986, pàg. 1091–100. DOI: 10.1083/jcb.103.3.1091. PMID: 3488995.
  • Wewer UM, Gerecke DR, Durkin ME, et al. «Human beta 2 chain of laminin (formerly S chain): cDNA cloning, chromosomal localization, and expression in carcinomas.». Genomics, 24, 2, 1995, pàg. 243–52. DOI: 10.1006/geno.1994.1612. PMID: 7698745.
  • Yamada H, Shimizu T, Tanaka T, et al. «Dystroglycan is a binding protein of laminin and merosin in peripheral nerve.». FEBS Lett., 352, 1, 1994, pàg. 49–53. DOI: 10.1016/0014-5793(94)00917-1. PMID: 7925941.
  • Moser TL, Enghild JJ, Pizzo SV, Stack MS «The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator.». J. Biol. Chem., 268, 25, 1993, pàg. 18917–23. PMID: 8360181.
  • Yurchenco PD, Sung U, Ward MD, et al. «Recombinant laminin G domain mediates myoblast adhesion and heparin binding.». J. Biol. Chem., 268, 11, 1993, pàg. 8356–65. PMID: 8463343.
  • Ancsin JB, Kisilevsky R «Characterization of high affinity binding between laminin and the acute-phase protein, serum amyloid A.». J. Biol. Chem., 272, 1, 1997, pàg. 406–13. DOI: 10.1074/jbc.272.1.406. PMID: 8995276.
  • Zahedi K «Characterization of the binding of serum amyloid P to laminin.». J. Biol. Chem., 272, 4, 1997, pàg. 2143–8. PMID: 8999915.
  • Utani A, Nomizu M, Yamada Y «Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences.». J. Biol. Chem., 272, 5, 1997, pàg. 2814–20. DOI: 10.1074/jbc.272.5.2814. PMID: 9006922.
  • Cáceres J, Brandan E «Interaction between Alzheimer's disease beta A4 precursor protein (APP) and the extracellular matrix: evidence for the participation of heparan sulfate proteoglycans.». J. Cell. Biochem., 65, 2, 1997, pàg. 145–58. DOI: 10.1002/(SICI)1097-4644(199705)65:2<145::AID-JCB2>3.0.CO;2-U. PMID: 9136074.
  • Chen M, Marinkovich MP, Veis A, et al. «Interactions of the amino-terminal noncollagenous (NC1) domain of type VII collagen with extracellular matrix components. A potential role in epidermal-dermal adherence in human skin.». J. Biol. Chem., 272, 23, 1997, pàg. 14516–22. DOI: 10.1074/jbc.272.23.14516. PMID: 9169408.
  • Schuger L, Skubitz AP, Zhang J, et al. «Laminin alpha1 chain synthesis in the mouse developing lung: requirement for epithelial-mesenchymal contact and possible role in bronchial smooth muscle development.». J. Cell Biol., 139, 2, 1997, pàg. 553–62. DOI: 10.1083/jcb.139.2.553. PMID: 9334356.
  • Mrowiec T, Melchar C, Górski A «HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium.». Arch. Immunol. Ther. Exp. (Warsz.), 45, 2-3, 1998, pàg. 255–9. PMID: 9597096.
  • O'Grady P, Thai TC, Saito H «The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR.». J. Cell Biol., 141, 7, 1998, pàg. 1675–84. DOI: 10.1083/jcb.141.7.1675. PMID: 9647658.
  • Ettner N, Göhring W, Sasaki T, et al. «The N-terminal globular domain of the laminin alpha1 chain binds to alpha1beta1 and alpha2beta1 integrins and to the heparan sulfate-containing domains of perlecan.». FEBS Lett., 430, 3, 1998, pàg. 217–21. DOI: 10.1016/S0014-5793(98)00601-2. PMID: 9688542.
  • Ludwig HC, Rausch S, Schallock K, Markakis E «Expression of CD 73 (ecto-5'-nucleotidase) in 165 glioblastomas by immunohistochemistry and electronmicroscopic histochemistry.». Anticancer Res., 19, 3A, 1999, pàg. 1747–52. PMID: 10470109.