| Citation |
Kusche-Gullberg, M., Garrison, K., MacKrell, A.J., Fessler, L.I., Fessler, J.H. (1992). Laminin A chain: expression during Drosophila development and genomic sequence. EMBO J. 11: 4519--4527.
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| PubMed Abstract |
A Drosophila laminin A chain gene was characterized as a 14 kb genomic nucleotide sequence which encodes an open reading frame
of 3712 amino acids in 15 exons. Overall, this A chain is similar to its vertebrate counterparts, especially in its N- and
C-terminal globular domains, but the sequence that forms the laminin A short arm is quite different and larger. Laminin messages
appear in newly formed mesoderm and are later prominently expressed in hemocytes, which also synthesize basement membrane
collagen IV. The composition of Drosophila basement membranes changes with development. A novel method of tandemly fused RNA
probes showed that developmental increases of laminin mRNAs were primarily associated with periods of morphogenesis, and preceded
those of collagen IV, a protein strongly expressed during growth. The ratio of A:B1:B2 mRNAs varied little during embryogenesis,
with less mRNA for A than B chains. Staining of embryos with antibodies confirmed and extended the information provided by
in situ hybridization. Homologs of the G-subdomains of this A chain, which occur in interacting regions of agrin, perlecan,
laminin and sex steroid binding protein, may be involved in protein associations.
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