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Evidence for receptors of PSA has so far been elusive. We now identified histone H1 as binding partner of PSA via a single-chain variable fragment antibody using an anti-idiotypic approach. Histone H1 directly binds to PSA as shown by ELISA. Surface biotinylation of cultured cerebellar neurons indicated an extracellular localization of histone H1. Immunostaining of live cerebellar neurons and Schwann cells confirmed that an extracellular pool of histone H1 colocalizes with PSA at the cell surface. Histone H1 was also detected in detergent-insoluble synaptosomal membrane subfractions and postsynaptic densities. When applied<jats:italic>in vitro<\/jats:italic>, histone H1 stimulated neuritogenesis, process formation and proliferation of Schwann cells, and migration of neural precursor cells via a PSA-dependent mechanism, further indicating that histone H1 is active extracellularly. These<jats:italic>in vitro<\/jats:italic>observations suggested an important functional role for the interaction between histone H1 and PSA not only for nervous system development but also for regeneration in the adult. Indeed, histone H1 improved functional recovery, axon regrowth, and precision of reinnervation of the motor branch in adult mice with femoral nerve injury. Our findings encourage investigations on the therapeutic potential of histone H1 in humans.<\/jats:p>","DOI":"10.1523\/jneurosci.6407-09.2010","type":"journal-article","created":{"date-parts":[[2010,9,15]],"date-time":"2010-09-15T16:44:02Z","timestamp":1284569042000},"page":"12400-12413","source":"Crossref","is-referenced-by-count":63,"title":["Functional Role of the Interaction between Polysialic Acid and Extracellular Histone H1"],"prefix":"10.1523","volume":"30","author":[{"given":"Bibhudatta","family":"Mishra","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maren","family":"von der 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