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Laminin Database


NAR Molecular Biology Database Collection entry number 1419
Daiane C. F. Golbert, Leandra Linhares-Lacerda, Luiz G. Almeida, Eliane Correa-de-Santana, Alice R. de Oliveira, Alex S. Mundstein, Wilson Savino and Ana T. R. de Vasconcelos
Contact lm@lncc.br

Database Description

Laminins (LM) correspond to a large number of heretotrimeric glycoproteins, playing and a major role in several cell functions, including differentiation, proliferation, adhesion, and migration [1-3]. In addition to binding to other extracellular matrix proteins, laminins bind specific cell membrane receptors, several of them are integrins, such as α3β1, α6β1, α6β4 and α7β1 [2, 4].
For example, laminin-mediated interactions are relevant for the entrance of T cell precursors into the thymus [5, 6], the migration of developing thymocytes, both in mice and humans [7, 8 , 9], as well as in peripheral lymphoid organs [10, 11]. Also, activated T cells use laminin receptors to migrate across endothelial barriers, as exemplified by the role of laminin isoforms in leukocyte extravasation in the central nervous system [12, 13].

Moreover, the effector immune function in rejection of heart grafts can be abrogated by blocking laminin- α6β1 interaction with antibodies specific for the ligand or the corresponding receptor [14, 15]. In fact, blockade of the α6β1 receptor also prevents neutrophils to cross basement lamina [16]. Lastly, laminins are presently demonstrated to be involved in pathophysiology and/or pathogenesis in neuromuscular and neurodegenerative diseases [17, 18, 19, 20].

Taking together, one can easily realize the high degree of biological complexity in laminin-mediated interactions, in both health and disease. The Laminin Database provides a comprehensive repository for public data concerning laminins and related proteins, which is collected and manually curated and annotated, allowing the user to easily retrieve highthroughput data available, but so far dispersed in the net. Further, external links are provided underlying data infrastructure for services such as Ensembl, UniProt and NCBI. The LM Database includes the 16 known laminins, 10 integrin type receptors, 9 non integrin type receptors and 6 extracellular laminin-binding proteins.

For each protein provided at the database, the following items are stored: summary, information concerning protein details, gene structure, gene expression and tissue distribution, therapy and reference(s) to relevant paper(s). The information can be retrieved for three particular organisms, Homo sapiens, Mus musculus and Ratus novergicus. The database is available on line at http://www.lm.lncc.br.

If you wish to make contributions to or comment on the database, please contact lm@lncc.br

References

[1] Timpl R, Rohde H, Robey PG, Rennard SI, Foidart JM, Martin GR. (1979). Laminin--a glycoprotein from basement membranes. J Biol Chem. 254(19):9933-7.

[2] Durbeej M. (2010). Laminins. Cell Tissue Res. 339(1):259-68.

[3] Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, et al. (2005). A simplified laminin nomenclature. Matrix Biol. 24(5):326-32.

[4] Barczyk M, Carracedo S, Gullberg D. Integrins. (2010). Cell Tissue Res. 339(1):269-80.

[5] Savino W, Mendes-Da-Cruz DA, Smaniotto S, Silva-Monteiro E, Villa-Verde DM. (2004). Molecular mechanisms governing thymocyte migration: combined role of chemokines and extracellular matrix. J Leukoc Biol. 75(6):951-61.

[6] Stimamiglio MA, Jiménez E, Silva-Barbosa SD, Alfaro D, García-Ceca JJ, Muñoz JJ, Cejalvo T, Savino W, Zapata A. (2010). EphB2-mediated interactions are essential for proper migration of T cell progenitors during fetal thymus colonization. J Leukoc Biol. 88(3):483-94.

[7] Vivinus-Nebot M, Rousselle P, Breittmayer JP, Cenciarini C, Berrih-Aknin S, Spong S, Nokelainen P, Cottrez F, Marinkovich MP, Bernard A. (2004). Mature human thymocytes migrate on laminin-5 with activation of metalloproteinase-14 and cleavage of CD44. J Immunol. 172(3):1397-406.

[8] Drumea-Mirancea M, Wessels JT, Müller CA, Essl M, Eble JA, Tolosa E, Koch M, Reinhardt DP, Sixt M, Sorokin L, Stierhof YD, Schwarz H, Klein G. (2006). Characterization of a conduit system containing laminin-5 in the human thymus: a potential transport system for small molecules. J Cell Sci. 119(Pt 7):1396-405.

[9] Ocampo JS, de Brito JM, Corrêa-de-Santana E, Borojevic R, Villa-Verde DM, Savino W. (2008). Laminin-211 controls thymocyte--thymic epithelial cell interactions. Cell Immunol. 254(1):1-9.

[10] Gorfu G, Virtanen I, Hukkanen M, Lehto VP, Rousselle P, Kenne E, Lindbom L, Kramer R, Tryggvason K, Patarroyo M. (2008). Laminin isoforms of lymph nodes and predominant role of alpha5-laminin(s) in adhesion and migration of blood lymphocytes. J Leukoc Biol. 84(3):701-12.

[11] Smaniotto S, Mendes-da-Cruz DA, Carvalho-Pinto CE, Araujo LM, Dardenne M, Savino W. (2010). Combined role of extracellular matrix and chemokines on peripheral lymphocyte migration in growth hormone transgenic mice. Brain Behav Immun. 24(3):451-61.

[12] Wu C, Ivars F, Anderson P, Hallmann R, Vestweber D, Nilsson P, Robenek H, Tryggvason K, Song J, Korpos E, Loser K, Beissert S, Georges-Labouesse E, Sorokin LM. (2009). Endothelial basement membrane laminin alpha5 selectively inhibits T lymphocyte extravasation into the brain. Nat Med. 15(5):519-27.

[13] Sorokin L. (2010). The impact of the extracellular matrix on inflammation. Nat Rev Immunol. 10(10):712-23.

[14] Silva-Barbosa SD, Cotta-de-Almeida V, Riederer I, De Meis J, Dardenne M, Bonomo A, Savino W. (1997). Involvement of laminin and its receptor in abrogation of heart graft rejection by autoreactive T cells from Trypanosoma cruzi-infected mice. J Immunol. 159(2):997-1003.

[15] Riederer I, Silva-Barbosa SD, Rodrigues ML, Savino W. (2002). Local antilaminin antibody treatment alters the rejection pattern of murine cardiac allografts: correlation between cellular infiltration and extracellular matrix. Transplantation. 74(11):1515-22.

[16] Dangerfield J, Larbi KY, Huang MT, Dewar A, Nourshargh S. (2002). PECAM-1 (CD31) homophilic interaction up-regulates alpha6beta1 on transmigrated neutrophils in vivo and plays a functional role in the ability of alpha6 integrins to mediate leukocyte migration through the perivascular basement membrane. J Exp Med. 196(9):1201-11.

[17] Patton BL. (2000). Laminins of the neuromuscular system. Microsc Res Tech. 51(3):247-61.

[18] Carmignac V, Durbeej M. (2012). Cell-matrix interactions in muscle disease. J Pathol. 226(2):200-18.

[19] Kittur SD, Adler WH, Martin GR, Schapiro MB, Rapoport SI, Gunzler V. (1993). Laminin concentrations in serum and cerebrospinal fluid in aging and Alzheimer's disease. Int J Dev Neurosci. 11(1):95-9.

[20] Drouet B, Pinçon-Raymond M, Chambaz J, Pillot T. (1999). Laminin 1 attenuates beta-amyloid peptide Abeta(1-40) neurotoxicity of cultured fetal rat cortical neurons. J Neurochem. 73(2):742-9.



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