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J. Biol. Chem., Vol. 263, Issue 32, 16536-16544, Nov, 1988
M Sasaki, HK Kleinman, H Huber, R Deutzmann and Y Yamada
Laminin (Mr = 800,000) is a glycoprotein consisting of three chains, A, B1,
and B2, and has diverse biological activities. Previously we reported the
complete primary structure of the B1 and B2 chains of mouse laminin deduced
from cDNA sequence (Sasaki, M., Kohno, K., Kato, S., Martin, G. R., and
Yamada, Y. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 935-939; Sasaki, M.,
and Yamada, Y. (1988) J. Biol. Chem. 262, 17111-17117). Here we describe
the isolation, characterization, and sequence of cDNA clones spanning 9,520
bases which encode the entire A chain of mouse laminin. The nucleotide
sequence of the clones contains an open reading frame of 3,084 amino acids
including 24 amino acids of a signal peptide. The A chain contains some
eight distinct domains including alpha-helices, cysteine-rich repeats and
globules. There is considerable sequence and structural homology between
the A chain and the B1 and B2 chains. However, the A chain has a unique
globular structure containing homologous repeats at the carboxyl terminus
and constituting one third of the molecular mass of the chain. Furthermore,
the A chain contains three globules and three cysteine-rich domains at the
amino terminus, whereas the B1 and B2 chains have only two each of such
domains. The A chain shows homology to the basement membrane heparan
sulfate proteoglycan core protein and the extracellular domain of the
Drosophila neurogenic protein Notch. There is an RGD (Arg-Gly- Asp)
sequence in one of the cysteine-rich domains of the A chain. This potential
cell binding sequence could be active as another adhesion signal in
addition to the previously identified cell binding sequence YIGSR
(Tyr-Ile-Gly-Ser-Arg) of the B1 chain.
Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains
Laboratory of Developmental Biology and Anomalies, National Institute of Dental Research, Bethesda, Maryland 20892.
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