The basic whey protein lactoferrin (LF) is a glycosaminoglycan (GAG)-binding protein that plays a role in innate immunity and is expected to be a potential biopharmaceutical because of its diverse functions. LF binds to heparan sulfate, a type of GAG on the cell surface, and is involved in neuroprotective and anti-cancer activities. Recently, it was found that human LF (hLF) binds to chondroitin sulfate E (CS-E), which inhibits neuronal axon outgrowth and neutralizes CS-E-induced axon outgrowth inhibition. LFs are potential therapeutic targets for GAG-related diseases, such as cancer, neurodegenerative diseases, and infectious diseases. This article outlines the general properties of LF and discusses the binding properties of hLF to CS-E and its application.

Gangliosides are glycosphingolipids containing one or more sialic acids, and abundantly exist in the central nervous system. They are fundamental components of cell membrane microdomains and interact laterally with membrane proteins, thereby regulating functions of transmembrane receptors such as epidermal growth factor receptor and insulin receptor. Studies using genetically engineered mice and neuronal cells for glycosyltransferase genes involved in glycosphingolipid synthesis provide insights into the roles of gangliosides in hypothalamic control of energy balance through leptin receptor signaling. This minireview summarizes current understanding of the mechanisms and discusses how ganglioside species regulate leptin receptor signaling.

In in vitro studies, chondroitin sulfate E (CSE) has been found to have various activities, suggesting its importance in the living body. However, the in vitro function of CSE has not been fully elucidated. Antibodies have been used as a tool for assessing the biological roles of sugar chains, but previously reported antibodies react not only with CSE but also with other CS isomers. If an antibody was highly specific and able to detect only CSE, it could be used to study the in vitro activities of CSE or as a probe for detecting diseases marked by abnormal expression or localization of CSE. This paper outlines the properties of antibodies that react with CSE.

The basic whey protein lactoferrin (LF) is a glycosaminoglycan (GAG)-binding protein that plays a role in innate immunity and is expected to be a potential biopharmaceutical because of its diverse functions. LF binds to heparan sulfate, a type of GAG on the cell surface, and is involved in neuroprotective and anti-cancer activities. Recently, it was found that human LF (hLF) binds to chondroitin sulfate E (CS-E), which inhibits neuronal axon outgrowth and neutralizes CS-E-induced axon outgrowth inhibition. LFs are potential therapeutic targets for GAG-related diseases, such as cancer, neurodegenerative diseases, and infectious diseases. This article outlines the general properties of LF and discusses the binding properties of hLF to CS-E and its application.

Gangliosides are glycosphingolipids containing one or more sialic acids, and abundantly exist in the central nervous system. They are fundamental components of cell membrane microdomains and interact laterally with membrane proteins, thereby regulating functions of transmembrane receptors such as epidermal growth factor receptor and insulin receptor. Studies using genetically engineered mice and neuronal cells for glycosyltransferase genes involved in glycosphingolipid synthesis provide insights into the roles of gangliosides in hypothalamic control of energy balance through leptin receptor signaling. This minireview summarizes current understanding of the mechanisms and discusses how ganglioside species regulate leptin receptor signaling.

In in vitro studies, chondroitin sulfate E (CSE) has been found to have various activities, suggesting its importance in the living body. However, the in vitro function of CSE has not been fully elucidated. Antibodies have been used as a tool for assessing the biological roles of sugar chains, but previously reported antibodies react not only with CSE but also with other CS isomers. If an antibody was highly specific and able to detect only CSE, it could be used to study the in vitro activities of CSE or as a probe for detecting diseases marked by abnormal expression or localization of CSE. This paper outlines the properties of antibodies that react with CSE.