Disease relevance of LanB2

• Gel-shift analyses showed that specific complexes were resolved using GC-containing oligonucleotides and Faza 567 hepatoma cells, which constitutively express laminin-gamma1 at a high level [1].
• The laminin-gamma1 chain is present in most basement membranes and is involved in various physiological and pathological processes, including carcinogenesis in the liver [1].
• Interaction of Bombyx mori nucleopolyhedrovirus BRO-A and host cell protein laminin [2].

High impact information on LanB2

• Attachment, spreading, and growth of myoblasts and neurons on the laminin substrate utilized different binding proteins and were independent of integrin [3].
• Transcripts of laminin B2 were detected in the RNA of male germ cells with the polymerase chain reaction and by in situ hybridization [4].
• Antigenic sites against laminin B2 were found in the lampbrush loops in primary spermatocyte nuclei, in nuclei of spermatids, and in heads of spermatozoa [4].
• We then describe the expression and tissue distribution of the three subunits of laminin during Drosophila embryogenesis using both in situ hybridization and immunolocalization techniques, with particular emphasis on its expression in and around the developing nervous system [5].
• This analysis revealed the similarity of Drosophila laminin with the mouse and human complexes in subunit composition, domain structure, and amino acid sequence [5].

Biological context of LanB2

• Drosophila laminin: sequence of B2 subunit and expression of all three subunits during embryogenesis [5].
• We show that laminin function is not required for the early phases of mesoderm patterning and morphogenesis in embryos at the extended germ band phase (stage 11) [6].
• In this report we describe the specific contribution of laminin to histogenesis and organogenesis during Drosophila embryogenesis [6].
• Large-scale culture of Drosophila Kc167 cells provided a sufficient amount of extracellular matrix (including laminin) for performing biochemical analysis on the signal transduction in BG2-c6 cells [7].
• This is due to a short, highly conserved sequence that occurs in both laminin gamma1 chains and which binds nidogen [8].

Anatomical context of LanB2

• Failure to down-regulate Dystroglycan disrupts apicobasal polarity in the PFC, which includes mislocalization of the extracellular matrix component Laminin [9].
• Laminin, a major component of basement membranes, is a large glycoprotein consisting of three disulfide-bonded subunits, A, B1, and B2 [10].
• Finally, during midgut formation, the endoderm fails to undergo the initial columnar polarization in the absence of functional laminin [6].
• Using several cell lines, the laminin alpha2 chain peptides showed cell attachment and/or spreading activities with cell type specificities [11].
• Cells from Drosophila embryos dissociated at the cellular blastoderm stage were grown in culture and some specific, differentiated cells synthesized laminin after several hours of culture as shown by immunofluorescence [12].

Associations of LanB2 with chemical compounds

• We conclude that laminin is not a ligand for integrin in this context [13].

Physical interactions of LanB2

• The amino acid composition and lectin-binding properties of Drosophila laminin are given [12].

Other interactions of LanB2

• Primary structure of the Drosophila laminin B2 chain and comparison with human, mouse, and Drosophila laminin B1 and B2 chains [10].
• In particular, the function of laminin during mesoderm development and morphogenesis was dissected by analyzing embryos deficient in laminin A chain alone or in both laminin A and B2 chains [6].
• Cloning and biological function of laminin in Hydra vulgaris [14].
• A family of laminin-related proteins controlling ectodermal differentiation in Drosophila [15].
• These results suggest that biologically active regions in the G domain are conserved in the laminin alpha1 and alpha2 chains, and that these regions in laminin play an important role in cell surface receptor interactions [11].

Analytical, diagnostic and therapeutic context of LanB2

• Cell culture consisting of Drosophila BG2-c6 cells and laminin revealed its value for the analysis of the integrin-mediated activity of extracellular matrix (Takagi, Y., et al. (1998) Neurosci. Lett. 244, 149-152) [7].

References