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The most straightforward applications of proteomics database searching involve intracellular proteins. While intracellular gene products number in the thousands, their well-defined post-translational modifications (PTMs) makes database searching practical. By contrast, cell surface and extracellular matrisome proteins pass through the secretory pathway where many become glycosylated, modulating their physicochemical properties, adhesive interactions, and diversifying their functions. Despite that matrisome proteins number only a few hundred, their high degree of complex glycosylation multiplies the number of theoretical proteoforms by orders of magnitude. Given that extracellular networks that mediate cell-cell and cell-pathogen interactions in physiology depend on glycosylation, it is important to characterize the proteomes, glycomes and glycoproteomes of matrisome molecules that exist in a given biological context. In this presentation, I will summarize proteomics approaches for characterizing matrisome molecules, with an emphasis on applications to brain diseases.