Thyroid Carcinoma Glycoproteins Express Altered -Glycans with 3-O-Sulfated Galactose Residues.

Aberrant protein glycosylation is a hallmark alteration of cancer and is highly associated with cancer progression. Papillary thyroid cancer (PTC) is the most common type of thyroid cancer, but the -glycosylation of its glycoproteins has not been well characterized. In this work, we analyzed multiple freshly prepared PTC specimens along with paired normal tissue obtained from thyroidectomies.

Intact quantitation and evaluation of a PEG-glycosulfopeptide as a therapeutic P-selectin antagonist.

Peptide-based therapeutics are recognized as potent and selective molecules but are often limited by short circulating half-lives, instability towards enzymatic degradation, and immunogenicity. To address these limitations and improve their pharmacological properties, peptides are commonly modified by the covalent attachment of polyethylene glycol (PEG). However, the large molecular weight and polydispersity of PEG chains complicate the interpretation of the full structure of PEGylated peptide therapeutics using standard analytical techniques.

The restricted N-glycome of neurons is programmed during differentiation.

The protein glycome of individual cell types in the brain is unexplored, despite the critical function of these modifications in development and disease. In aggregate, the most abundant asparagine (N-) linked glycans in the adult brain are high mannose structures, and specifically ManGlcNAc (Man-5), which normally exits the ER for further processing in the Golgi. Mannose structures are uncommon in other organs and often overlooked or excluded in most studies.