List of Proteins
Laminins correspond to a large number of heretotrimeric glycoproteins, playing and a major role in several cell functions, including differentiation, proliferation, adhesion, and migration. The first laminin, presently named laminin-111, was identified more than 30 years ago by Rupert Timpl in Germany (PMID: 114518). Since then a large number of isoforms have been described, with specificities in terms of tissue distribution as well as cellular functions (PMID: 19693542, PMID: 15979864). In addition to binging to other extracellular matrix proteins, laminins bind specific cell membrane receptors, several of them are integrins, such as Î±3Î²1, Î±6Î²1, Î±6Î²4 and Î±7Î²1 (PMID: 19693542, PMID: 19693543). Taking together, one can easily realize the high degree of biological complexity in laminin-mediated interactions, in both health and disease.
Worldwide research into many aspects of laminins is rapidly growing. Such a notion can be applied for the study of laminins in general, as well as more specifically when we evaluate the expression and role of laminins in the hemopoietic system. For example, laminin-mediated interactions are relevant for the entrance of T cell precursors into the thymus (PMID: 15020651, PMID: 20504947), the migration of developing thymocytes, both in mice and humans (PMID: 14734715, PMID: 16537647, PMID: 18644586), as well as in peripheral lymphoid organs (PMID: 18523231, PMID: 19948213). 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 (PMID: 19396173, PMID: 20865019).
Moreover, the effector immune function in rejection of heart grafts can be abrogated by blocking laminin- Î±6Î²1 interaction with antibodies specific for the ligand or the corresponding receptor (PMID: 9218622,PMID: 12490783). In fact, blockade of the Î±6Î²1 receptor also prevents neutrophils to cross basement lamina (PMID: 12417630). Lastly, it has recently been demonstrated that laminins are involved in pathophysiology and/or pathogenesis in neuromuscular and neurodegenetative diseases (PMID:11054875, PMID: 21989954, PMID: 19756756, PMID: 18219670, PMID: 9273822, PMID: 8488758, PMID: 10428072, PMID: 21069393, PMID: 18651950, PMID:12715073).
Currently, there is a considerable amount of information about these proteins, but the data are scattered in the literature and in several bioinformatic databases. The laminin (LM) database allows the user to easily retrieve highthroughput data available, but so far dispersed in the net. Moreover, relevant information in the database is carefully curated and annotated.
We expect that LM-database 2.0 will be a relevant tool for retrieving information of laminins in health and disease, particularly in relation to the physiology of the hemopoietic system and in pathological dysfunctions, including neuromuscular and neurodegenerative diseases.
The LM database was published in 2011 with the reference: Golbert DC, Linhares-Lacerda L, Almeida LG, Correa-de-Santana E, de Oliveira AR, Mundstein AS, Savino W, de Vasconcelos AT. Laminin database: a tool to retrieve high-throughput and curated data for studies on laminins. Nucl. Acids Res. 2011 Jan;39(Database issue):D320-3. doi: 10.1093/nar/gkq1055 and updated in 2013 with the reference Daiane C. F. Golbert; Eliane Santana-van-Vliet; Alex S. Mundstein; Vicente Calfo; Wilson Savino; Ana Tereza R. de Vasconcelos Laminin-database v.2.0: an update on laminins in health and neuromuscular disorders. Nucl. Acids Res. (1 January 2014); 42 (D1): D426-D429. doi:10.1093/nar/gkt901.First published online: October 7, 2013.If you wish to make contributions to or comment on the database, please contact firstname.lastname@example.org.