Disease relevance of Rtn1

• Neurodegeneration was evaluated by fluoro-jade, neuronal loss by Nissl, reactive gliosis by glial fibrillary acidic protein staining, and differentiation by neuroendocrine-specific protein C immunoreactivity [1].

High impact information on Rtn1

• The prohormone convertase PC2, which is thought to mediate the proteolytic conversion of many peptide hormones, has recently been shown to interact with the neuroendocrine-specific polypeptide 7B2 in Xenopus intermediate lobe (Braks, J. A. M., and G. J. M. Martens. Cell. 78:263. 1994) [2].
• Using a subtractive hybridization technique directed to cloning transcripts with compartmentalized distributions within cerebral cortex neurons, we have isolated rat s-rex mRNAs that are analogues of the human neuroendocrine-specific NSP gene transcripts [3].
• Unexpectedly, one of the largest RGC clusters, RESP18, corresponded to a neuroendocrine-specific gene preferentially expressed in the hypothalamus [4].
• It is surprising that hybrid cells created by fusing normal PC12 cells with A35C cells exhibited the variant phenotype, suggesting that A35C cells express an inhibitory factor that represses neuroendocrine-specific gene expression [5].
• Among the prohormone convertases, PC2 is unique in that it specifically binds to the neuroendocrine-specific protein 7B2 in the endoplasmic reticulum (ER) and is activated late in the regulated secretory pathway of neuroendocrine cells [6].

Anatomical context of Rtn1

• Molecular analysis of expression in rat brain of NSP-A, a novel neuroendocrine-specific protein of the endoplasmic reticulum [7].
• Previous studies have established that the novel neuroendocrine-specific NSP gene encodes three carboxy-terminally overlapping proteins, NSP-A, NSP-B and NSP-C which are anchored to membranes of the endoplasmic reticulum [7].
• Expression of PAM along with a neuroendocrine-specific endoprotease liberates a soluble monooxygenase domain, yielding regulated secretion of both the monooxygenase and the prohormone convertase from large dense core vesicles [8].
• Cloning and characterization of a 22 kDa protein from rat adipocytes: a new member of the reticulon family [9].
• This protein is homologous to known members of the reticulon protein family. vp20 has two hydrophobic stretches of about 35 amino acids that could be membrane spanning domains and an ER retention motif at its carboxy-terminus. vp20 was most abundant in the high density microsome fraction of adipocytes, which is the fraction most enriched in ER [9].

Associations of Rtn1 with chemical compounds

• Among them was Neuroendocrine-Specific Protein-A (NSP-A), which is known to be affected by thyroid hormone in the cortex at this developmental time [10].

Regulatory relationships of Rtn1

• These cells secrete mainly prolactin and also express the neuroendocrine-specific protein secretogranin II, which is considered a peptide precursor [11].

Other interactions of Rtn1

• In addition, we present evidence that these cells also contain small neuroendocrine-specific vesicles, as evidenced by the expression of the neuroendocrine-specific vesicle proteins synaptophysin and S.V [12].

Analytical, diagnostic and therapeutic context of Rtn1

• Using in situ hybridization, we confirmed that the cortical expression of both neuroendocrine-specific protein (NSP) and Oct-1 was affected by changes in maternal thyroid status [13].

References