Abstract
A novel laminin gamma3 chain was identified from the expressed sequence tag data base at the National Center for Biotechnology Information. A complete cDNAderived peptide sequence reveals a 1592-amino acid-long primary translation product, including a tentative 33-amino acid-long signal peptide. Comparison with the laminin gamma1 chain predicts that the two polypeptides have equal spatial dimensions. In addition, the well conserved domains VI and III(LE4) predict that gamma3 containing laminins are able to integrate to the laminin network and also via nidogen connect to other protein networks in the basement membranes. Combination of Northern analysis and in situ hybridization experiments indicate that expression of the gamma3 chain is highly tissue- and cell-specific, being significantly strong in capillaries and arterioles of kidney as well as in interstitial Leydig cells of testis.
Highlights
Laminins are a growing family of large extracellular glycoproteins found in but not confined to basement membranes [1,2,3]
An alternative ␥ chain would nearly double the number of potential laminin isoforms and, more importantly, proportionally increase the number of identifiable components embedded in the protein meshwork in basement membranes
This would significantly improve the resolution of our current basement membrane models that are based on a limited number of distinct proteins (46 – 49)
Summary
Laminins are a growing family of large extracellular glycoproteins found in but not confined to basement membranes [1,2,3]. A novel laminin ␥3 chain was identified from the expressed sequence tag data base at the National Center for Biotechnology Information. Combination of Northern analysis and in situ hybridization experiments indicate that expression of the ␥3 chain is highly tissue- and cell-specific, being significantly strong in capillaries and arterioles of kidney as well as in interstitial Leydig cells of testis.
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