Disease relevance of Prph1

• In cultures of embryonic day 15 dorsal root ganglion neurons grown in the presence of nerve growth factor, peripherin and low-molecular-weight neurofilament messenger RNAs were expressed in all neurons, even after nine days in vitro, similar to embryonic dorsal root ganglia in vivo [1].

High impact information on Prph1

• We have cloned the rat gene encoding peripherin, a neuronal-specific intermediate filament protein that is NGF-regulated [2].
• The peripherin promoter contains sequences homologous to regions of other NGF-regulated promoters, which may function in peripherin induction by NGF [2].
• Together with protein sequence homologies, this conclusively demonstrates that peripherin is a type III intermediate filament protein [2].
• Nerve growth factor-induced derepression of peripherin gene expression is associated with alterations in proteins binding to a negative regulatory element [3].
• Transfection experiments using peripherin-chloramphenicol acetyltransferase constructs in which the footprinted sequence has been mutated confirm that the NRE has a functional, though not exclusive, role in repressing peripherin expression in undifferentiated and nonneuronal cells [3].

Chemical compound and disease context of Prph1

• Analysis of Triton X-100 extracts from okadaic acid-treated dorsal root ganglion cultures revealed that peripherin and alpha-internexin followed the same fragmentation pattern observed with NFs [4].

Biological context of Prph1

• We have isolated a full-length peripherin cDNA (designated as p61-11) from a rat brain cDNA library [5].
• In a previous study we described two distinct neuronal phenotypes in rat dorsal root ganglia based on immunocytochemical assays for the neuronal intermediate filament proteins, peripherin and low-molecular-weight neurofilaments [Goldstein M. E. et al. (1991) J. Neurosci. Res. 30, 92-104] [1].
• The developmental profile of the neurofilament (NF) triplet proteins, alpha-internexin and peripherin in cultured dorsal root ganglion neurons from gestation day 15 rat embryos was determined by Western blot analysis [4].

Anatomical context of Prph1

• Translation initiation and assembly of peripherin in cultured cells [5].
• After 24 h of traumatic damage induction, the injured spinal cord tissue up-regulated over 39 proteins including neurofilament light chain, annexin 5, heat shock protein, tubulin beta, peripherin, glial fibrillary acidic protein delta, peroxiredoxin 2, and apolipoprotein A [6].
• The results also show that peripherin is expressed more widely than has been previously observed and that this protein occurs in neuronal populations from different lineages (neural tube, neural crest, placodes) with different functions (motoneurons, sensory and autonomic neurons) [7].
• The common point of these neurons is that they all have axons lying, at least partly, at the outside of the axis constituted by the encephalon and the spinal medulla; this suggests that peripherin might play a role in the recognition of the axonal pathway through the intermediary of membrane proteins [7].
• Peripherin-like immunoreactivity in type II spiral ganglion cell body and projections [8].

Associations of Prph1 with chemical compounds

• Serotonin was present in trigeminal neurons containing CGRP, a potent vasoactive neuropeptide, peripherin, an intermediate filament present in neurons with unmyelinated axons, neurofilament H, which is present in neurons with myelinated axons, and in neurons binding IB4, a marker of nonpeptidergic nociceptors [9].
• Retinoic acid suppressed the synthesis of peripherin, an intermediate filament protein predominantly found in peripheral nerve cells, but a high level of simple keratins, normally found in simple epithelial cells, was present in retinoic acid-treated PC12 cells [10].
• After capsaicin treatment, a striking expansion in the latter population was seen (L2: 22.0%) together with a significant increase in size, restricted to the same population and the (remaining) peripherin-only immunoreactive neurons [11].

Other interactions of Prph1

• RNA blot analyses with total RNA obtained from DRGs at different postaxotomy times confirmed that NF-L mRNA levels were reduced in the DRG during the first 4 weeks after axotomy but, interestingly, failed to detect an increase in peripherin mRNA levels [12].
• In early embryonic stages (embryonic days 15-16), virtually all neurons were peripherin-immunoreactive and were positive for peripherin, alpha-tubulin and low-molecular-weight neuro-filament messenger RNAs, suggesting a homogeneous population [1].
• The few plectin positive neurons invariably also contain the neurofilament triplet proteins and peripherin, so that the ability of plectin to bind to the triplet proteins in vitro may reflect an in vivo interaction [13].
• Calcitonin gene-related peptide and peripherin immunoreactivity in nerve sheaths [14].

Analytical, diagnostic and therapeutic context of Prph1

• The results of quantitative analyses indicated that peripherin mRNA levels were significantly increased in large-sized (greater than 1000 microns 2) DRG neurons at 7, 14, and 28 days after axotomy while the mRNA levels for each of the NF triplet proteins were significantly decreased at these same time points [12].
• This difference concerning peripherin mRNA levels in axotomized preparations obtained by RNA blotting vs. in situ hybridization was attributed to the fact that RNA blots utilized total DRG RNA which includes mRNAs from both small and large-sized DRG neurons [12].
• The distribution of peripherin was studied in the adult rat cochlea using immunohistochemistry on whole mount material, in cryostat sections and sections of plastic embedded tissue [8].
• Double immunofluorescence labeling of the prenatal cochlea with peripherin and neurofilament (NF) antibodies revealed colocalization on the same structures [15].
• Northern blotting, in situ hybridization and immunocytochemistry were used to study the changes in levels of mRNA coding for peripherin and in immunoreactivity of peripherin, a type III neuronal intermediate filament, in rat spinal motor neurons following axotomy of the sciatic nerve [16].

References