Abstract

Basement membrane is the first extracellular matrix produced during development and provides a physical support of a variety of cells. Basement membrane consists of a unique set of proteins which have various biological activities including cell migration, adhesion, differentiation, and growth. We have been studying molecular basis of the expression and function of basement membrane components as well as their receptors. Recombinant DNA techniques have been used to prepare molecular clones for various basement membrane components. The primary structure of most of these components has been determined by cDNA sequencing. We have identified some of regulatory DNA elements of basement membrane genes. Several nuclear protein factors have been identified and characterized. Relationships between the structure and function of the proteins have been studied using synthetic peptides and expressing exogenous genes in a variety of cell cultures. We have identified a new laminin receptor of Mr=67 which interacts with the IKVAV site of laminin. We have also isolated a mouse genomic clone which codes for a sequence homologous to the laminin A chain.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Intramural Research (Z01)
Project #
1Z01DE000485-03
Application #
3854229
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
3
Fiscal Year
1991
Total Cost
Indirect Cost

  Institution

Name
National Institute of Dental & Craniofacial Research
Department
Type
DUNS #
City
State
Country
United States
Zip Code

  Publications

Sarangi, Pranita P; Chakraborty, Papiya; Dash, Shiba Prasad et al. (2018) Cell adhesion protein fibulin-7 and its C-terminal fragment negatively regulate monocyte and macrophage migration and functions in vitro and in vivo. FASEB J 32:4889-4898
de Vega, S; Iwamoto, T; Yamada, Y (2009) Fibulins: multiple roles in matrix structures and tissue functions. Cell Mol Life Sci 66:1890-902
Ichikawa, Naoki; Iwabuchi, Kazuhisa; Kurihara, Hidetake et al. (2009) Binding of laminin-1 to monosialoganglioside GM1 in lipid rafts is crucial for neurite outgrowth. J Cell Sci 122:289-99
Kasai, Shingo; Urushibata, Shunsuke; Hozumi, Kentaro et al. (2007) Identification of multiple amyloidogenic sequences in laminin-1. Biochemistry 46:3966-74
Mochizuki, Mayumi; Philp, Deborah; Hozumi, Kentaro et al. (2007) Angiogenic activity of syndecan-binding laminin peptide AG73 (RKRLQVQLSIRT). Arch Biochem Biophys 459:249-55
Kato-Takagaki, Kozue; Suzuki, Nobuharu; Yokoyama, Fumiharu et al. (2007) Cyclic peptide analysis of the biologically active loop region in the laminin alpha3 chain LG4 module demonstrates the importance of peptide conformation on biological activity. Biochemistry 46:1952-60
Hozumi, Kentaro; Suzuki, Nobuharu; Nielsen, Peter K et al. (2006) Laminin alpha1 chain LG4 module promotes cell attachment through syndecans and cell spreading through integrin alpha2beta1. J Biol Chem 281:32929-40
Fukumoto, Satoshi; Miner, Jeffrey H; Ida, Hiroko et al. (2006) Laminin alpha5 is required for dental epithelium growth and polarity and the development of tooth bud and shape. J Biol Chem 281:5008-16
Aumailley, Monique; Bruckner-Tuderman, Leena; Carter, William G et al. (2005) A simplified laminin nomenclature. Matrix Biol 24:326-32
Vikramadithyan, Reeba K; Kako, Yuko; Chen, Guangping et al. (2004) Atherosclerosis in perlecan heterozygous mice. J Lipid Res 45:1806-12

Showing the most recent 10 out of 12 publications