The extracellular matrix (ECM) has been implicated in the primary developmental processes of many organisms. A family of secretory adhesive glycoproteins called substrate adhesion molecules (SAMs) is believed to confer these dynamic capabilities to the ECM in animals. In this paper, we report the existence of SAM-like genes and gene products in flowering plants. Hybridizations with a human vitronectin cDNA probe and genomic DNA from broad bean, soybean, and tomato revealed vitronectin-like sequences. Human vitronectin antibodies cross-react with a 55-kilodalton protein in leaf and root protein extracts from lily, broad bean, soybean, and tomato. In addition, immunocytochemical staining of frozen sections of lily leaf and broad bean gynoecium demonstrated that vitronectinlike proteins were localized to the ECM on the cell surface, with the most intense labeling residing in the transmitting tract of broad bean gynoecium.

Antiserum was raised in rabbits against a lily (Lilium longiflorum) anther-specific protein (LLA-15). Monospecific anti-LLA-15 antibodies were prepared to investigate the distribution of LLA-15 during anther development in a variety of flowering plants. Immunoblot analyses of total protein from floral and vegetative organs confirmed that LLA-15 or LLA-15-like proteins accumulated to detectable levels only in a discrete stage of anther development. In situ localization using anti-rabbit immunoglobulin G conjugated with gold particles confirmed that LLA-15 was specifically localized in the tapetal tissue of lily anthers. The maximal level of LLA-15 was strictly coincident with the peak of tapetal secretory functions.

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