Laminin, a major structural glycoprotein complex of basement membranes has been found to be modulated by angiotensin II in vitro and in vivo. In cultures of aortic organoids and vascular smooth muscle cells, expression of laminin was stimulated by exogenous vasoconstrictor peptide. Stimulation of laminin protein and mRNA expression was observed for both laminin B1/ B2-chains and an unknown laminin heavy chain. Compared with PYS-2 cells, a mouse teratocarcinoma cell line which constitutively expresses a 10-kb mRNA transcript for ‘classical’ laminin A-chain, cultured vascular smooth muscle cells (VSMC) did not express a corresponding mRNA. However, cultured VSMC were found to express laminin A-chain-related mRNAs of ≈1.8 kb and ≈3.8kb, respectively. The 1.8-kb species of transcript was expressed in a constitutive manner, whereas the 3.8-kb mRNA was found to be regulated by angiotensin II. Laminin complexes secreted by cultured cells contained a ≈300 kD heavy chain which did not immunoreact with immuno-reagents raised against either the classical laminin complex secreted by EHS tumor cells or the merosin heavy chain. The putative A-chain analogue possibly represents a new form of a tissue-specific laminin heavy chain, distinct from the A- and M-chains thus far described. Translation products encoded by the A-chain-related transcripts of cultured smooth muscle cells could not be specified using currently available antibodies. The putative protein(s) is speculated to contain the biological features of the N-terminus of the laminin A-chain, namely self-assembly and association with collagen type IV.