Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2017 Mar;74(6):1095-1115.
doi: 10.1007/s00018-016-2381-0. Epub 2016 Oct 1.

Laminin: loss-of-function studies

Affiliations
Review

Laminin: loss-of-function studies

Yao Yao. Cell Mol Life Sci. 2017 Mar.

Abstract

Laminin, one of the most widely expressed extracellular matrix proteins, exerts many important functions in multiple organs/systems and at various developmental stages. Although its critical roles in embryonic development have been demonstrated, laminin's functions at later stages remain largely unknown, mainly due to its intrinsic complexity and lack of research tools (most laminin mutants are embryonic lethal). With the advance of genetic and molecular techniques, many new laminin mutants have been generated recently. These new mutants usually have a longer lifespan and show previously unidentified phenotypes. Not only do these studies suggest novel functions of laminin, but also they provide invaluable animal models that allow investigation of laminin's functions at late stages. Here, I first briefly introduce the nomenclature, structure, and biochemistry of laminin in general. Next, all the loss-of-function mutants/models for each laminin chain are discussed and their phenotypes compared. I hope to provide a comprehensive review on laminin functions and its loss-of-function models, which could serve as a reference for future research in this understudied field.

Keywords: Animal model; Basement membrane; Knockout; Laminin; Loss-of-function.

PubMed Disclaimer

Conflict of interest statement

The author declares no competing interests.

Figures

Fig. 1
Fig. 1
General structure of laminins. Laminin-111 is used as an example in this figure

Similar articles

Cited by

References

    1. Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, Engel J, Engvall E, Hohenester E, Jones JC, Kleinman HK, Marinkovich MP, Martin GR, Mayer U, Meneguzzi G, Miner JH, Miyazaki K, Patarroyo M, Paulsson M, Quaranta V, Sanes JR, Sasaki T, Sekiguchi K, Sorokin LM, Talts JF, Tryggvason K, Uitto J, Virtanen I, von der Mark K, Wewer UM, Yamada Y, Yurchenco PD. A simplified laminin nomenclature. Matrix Biol. 2005;24(5):326–332. doi: 10.1016/j.matbio.2005.05.006. - DOI - PubMed
    1. Aumailley M. The laminin family. Cell Adhes Migration. 2013;7(1):48–55. doi: 10.4161/cam.22826. - DOI - PMC - PubMed
    1. Durbeej M. Laminins. Cell Tissue Res. 2010;339(1):259–268. doi: 10.1007/s00441-009-0838-2. - DOI - PubMed
    1. Burgeson RE, Chiquet M, Deutzmann R, Ekblom P, Engel J, Kleinman H, Martin GR, Meneguzzi G, Paulsson M, Sanes J, et al. A new nomenclature for the laminins. Matrix Biol. 1994;14(3):209–211. doi: 10.1016/0945-053X(94)90184-8. - DOI - PubMed
    1. Ferrigno O, Virolle T, Galliano MF, Chauvin N, Ortonne JP, Meneguzzi G, Aberdam D. Murine laminin alpha3A and alpha3B isoform chains are generated by usage of two promoters and alternative splicing. J Biol Chem. 1997;272(33):20502–20507. doi: 10.1074/jbc.272.33.20502. - DOI - PubMed

Publication types

LinkOut - more resources