High impact information on PTPRN

• While the function of ICA512 remains unknown, it is thought to link regulated neuropeptide and peptide hormone secretion with signal transduction pathways involving tyrosine phosphorylation/dephosphorylation [1].
• To characterize further its biochemical properties, we conducted studies in the bovine pituitary, an abundant source of native ICA512, as well as in fibroblasts transfected with various human ICA512 cDNA constructs [1].
• Post-translational modifications of ICA512, a receptor tyrosine phosphatase-like protein of secretory granules [1].
• Newly synthesized ICA512 appears first as a pro-protein of 110 kDa that is then converted by post-translational modifications into a 130-kDa species [1].
• ICA 512, a receptor tyrosine phosphatase-like protein, is concentrated in neurosecretory granule membranes [2].

Biological context of PTPRN

• Finally, the predicted N-terminal fragment of ICA512 resulting from this cleavage (amino acids 35-448) or parts thereof are present in the neurosecretosomes of posterior pituitary, raising the possibility that they may be secreted upon exocytosis of secretory granules [1].

Anatomical context of PTPRN

• Such processing ICA512 is not restricted to neuroendocrine cells, as it can also occur in transfected fibroblasts [1].

References