Worm Breeder's Gazette 11(3): 31
These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.
Laminin is a large glycoprotein of the extracellular matrix. The comparison of laminins isolated from different species and tissues has demonstrated that a variety of laminin structures may exist and that the expression of different isoforms of laminin may be important for several developmental processes. Laminin is composed of three chains, A, B1, and B2, with possible variants of each chain. In our lab we have been studying structure/function relationships of the B2 chain gene (unc-6). Several other laminin or laminin-related genes from C. elegans have been reported (see Yochem & Greenwald, WBG 11(2) and Rogalski & Moerman, this issue). The sequence of the N-terminal domain (V1) is highly conserved in all three chains. We have been searching for other laminin chain genes by low stringency hybridization using probes derived from this region of the B2 chain. Several genomic clones, distinct from the unc- 6 B2 chain, have been isolated. Currently we are analyzing these clones to determine if any contain new laminin sequences. Using degenerate primers designed for a highly conserved region of domain V1 of the B1 chain, we have amplified and cloned a fragment of a C. elegans B1 chain by PCR. The sequence from this clone is aligned below with other sequenced B1 and B2 chain genes. [See Figure 1]