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PubMed1992

Peripherin and neurofilament protein coexist in spinal spheroids of motor neuron disease.

We have compared the immunolocalization of neurofilament protein (NF) with two other neuronal-specific intermediate filament proteins in large spinal axonal swellings (spheroids) of motor neuron disease and controls. All spheroids labeled each of the three different subunits of NF, the low, middle, and high molecular weight polypeptides. In doublelabel immunofluorescence, 300 axonal swellings were immunostained for NF, and 87% of them contained the intermediate protein peripherin. The pattern of immunostaining of NF and peripherin was indistinguishable at a high resolution viewed in 1 microns optical sections by confocal microscopy. A minority of the spheroids contained alpha-internexin, another intermediate protein, but it was weakly immunoreactive. The immunostaining of axonal swellings was similar for all epitopes tested in motor neuron disease and control subjects. The findings suggest that peripherin as well as neurofilament protein are major components of the proliferated intermediate filaments in spheroids.

Axons↗
PubMed1995

Calcitonin gene-related peptide and peripherin immunoreactivity in nerve sheaths.

The intrinsic innervation of rat sciatic nerve sheaths was studied by means of immunohistochemical labeling for calcitonin gene-related peptide (CGRP) and peripherin. CGRP immunoreactivity (CGRP-IR) and peripherin immunoreactivity (peripherin-IR) were found in fine nerve fibers independent of nerve sheath vasculature. These findings suggest that a subset of the nervi nervorum may have nociceptive functions, and that this subset is distinct from nerve fibers that innervate the blood vessels of the nerve sheaths.

Animals↗
PubMed1995

A point mutation in the RDS-peripherin gene in a Spanish family with central areolar choroidal dystrophy.

The RDS-peripherin gene encodes a photoreceptor-specific protein that is localized in the outer segment disc membranes of both rods and cones. We screened a Spanish family with central areolar choroidal dystrophy for mutations in candidate genes. A base substitution was identified in the RDS-peripherin gene of one patient and DNA sequencing revealed a C-to-T transition in codon 172, arginine being substituted by tryptophan. The mutation was also detected in two asymptomatic family members who showed irregular pigmentation in the retinal pigment epithelium (RPE). The phenotype is similar to other macular dystrophies caused by mutation in the RDS-peripherin gene.

Adult↗
PubMed1988

[Comparative expression of 2 intermediate filament proteins, peripherin and the 68 kDa neurofilament protein, during embryonal development of the rat].

Peripherin, an intermediate filament protein, was originally detected by biochemical methods in the neurons of the peripheral nervous system. We now studied its expression and cellular localization by immunocytochemical methods in the developing rat embryo, and compared them with the expression and localization of the 68 kDa neurofilament protein. It appears that peripherin is expressed not only in the neurons of the peripheral nervous system, but also in some well defined neuronal populations of the central nervous system. These results focus on the questions of the phylogenetic origin and of the function of peripherin.

Animals↗
PubMed1993

Peripherin and neurofilaments: expression and role during neural development.

This review focuses attention on the expression of peripherin and the low-molecular mass neurofilament protein during development, as well as on recent results concerning the roles of these neuronal proteins. Peripherin is the only type III intermediate filament that has been shown to be expressed in neurons but exclusively in motor, sensory and sympathetic neurons; moreover, it is co-expressed with neurofilament proteins (NFP). Clearly, peripherin is expressed concomitantly with axonal growth during development, and its synthesis appears necessary to axonal regeneration in the adult. As to NFP, they are presumed to maintain the axonal diameter and thereby ensure a normal conduction velocity. In many neuropathies, either occurring in man or provoked by different means in animals, the neurofilament network is disrupted thus giving rise to bundles of filaments in perikarya or along axons; consequently, the axonal transport is impaired. The possible significance of the overexpression of NFP is discussed.

Animals↗
PubMed1994

Substance P, neurofilament, peripherin and SSEA4 immunocytochemistry of human dorsal root ganglion neurons obtained from post-mortem tissue: a quantitative morphometric analysis.

Immunocytochemical studies on lumbar dorsal root ganglia obtained at routine postmortem 24-36 h after death were carried out, and neuronal cross-sectional areas measured. The subjects were elderly (76-81 years), of both sexes, had died from heart attack or haemorrhage, and had no clinical evidence of clinical neuropathy or of disease known to be associated with neuropathy. The data were consistent between ganglia from the three subjects. There were striking similarities with data from other species. Two populations of cell profiles with overlapping size distributions were distinguished with an anti-neurofilament antibody, neurofilament-rich (45% of cell profiles) with a large mean area and neurofilament-poor with a smaller mean area. Anti-substance P and anti-peripherin antibodies both labelled a population with a small mean area, with extensive co-localization between them. There were also some differences between these human dorsal root ganglia and dorsal root ganglia from some other species. More neuronal profiles were labelled for substance P in humans (44%) than in rat (20%). More neuronal profiles were labelled for SSEA4 (stage specific embryonic antigen 4) in human (40.5%) than in rat dorsal root ganglia (10%), and the SSEA4-positive profiles were relatively smaller in human than in rat. No selective accumulation of lipofusin in profiles of large cells was apparent. This study also shows that quantitative morphometric analysis of immunocytochemically labelled dorsal root ganglion neuronal profiles can be carried out successfully on human sensory ganglia obtained at post-mortem. This is the first demonstration of the two main subgroups of dorsal root ganglia neurones with neurofilament-rich and poor somata in human tissue. The size distributions of neurons with neurofilament, substance P and peripherin are consistent with these neuronal populations having similar functional properties to those described in other species. From the known sensory and fibre loss with aging, it is speculated that the loss of some large diameter neurones with myelinated fibres and low mechanical thresholds, might account for the high percentage of neurones expressing substance P.

Aged↗
PubMed1990

Neuronal intermediate filaments in rat dorsal root ganglia: differential distribution of peripherin and neurofilament protein immunoreactivity and effect of capsaicin.

Two major neuronal populations were revealed in rat dorsal root ganglia, immunoreactive for either peripherin, or neurofilament triplet proteins (adult L2 ganglia: 66.2% and 25.6%, mainly small and large diameter cells, respectively), together with a minor, double-immunostained population (L2: 8.1%, mainly intermediate-size neurons). 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. Calcitonin gene-related peptide (CGRP) immunoreactivity was revealed in neurons of all 3 groups, in both normal and capsaicin-treated rats.

Animals↗
PubMed1993

A subpopulation of chicken primary sensory neurons defined by complete co-localization of peripherin-and ovalbumin-immunoreactivities.

In a previous study, we have demonstrated that an ovalbumin-like antigen is present within approximately one-half of all neurons of chicken spinal ganglia. The current study demonstrates this antigen co-localizes absolutely with neural intermediate filament protein (Peripherin) in small to medium-sized neurons of spinal ganglia. While the function of ovalbumin in neurons is unknown, its precise co-localization with Peripherin suggests a functional role restricted to neurons of a defined phenotype.

Animals↗
PubMed1992

Structure of the mouse gene encoding peripherin: a neuronal intermediate filament protein.

The gene encoding mouse peripherin, a neuronal intermediate filament protein, has been cloned. Its sequence, through 1021 nucleotides composing the 5'-flanking region, nine exons, eight introns and 547 nucleotides of the 3'-flanking region, as well as its transcription initiation site have been determined. The amino acid coding sequence differs from that of the rat peripherin gene. The mouse gene has an additional histidine near the N-terminal end, and shows three conservative and two non-conservative changes. The promoter sequence, containing the binding sites for transcription factors as well as other sequences is homologous to promoter regions of other type III intermediate filament protein genes and other neuronal-specific genes.

Amino Acid Sequence↗
PubMed2006

Vestibular efferents contain peripherin.

Vestibular efferents have a common origin with the motoneurons of the facial nerve. In adults they share a number of common features, such as the same transmitter. Here we show using retrograde transport and immunohistochemistry, that the vestibular efferents, like facial motoneurons, contain peripherin. This supports the suggestion that peripherin-positive fibers at the apex of the cristae ampullaris are efferents.

Animals↗
PubMed2002

Molecular probes of the vestibular nerve. I. Peripheral termination patterns of calretinin, calbindin and peripherin containing fibers.

Vestibular afferents have different physiological properties that can be at least partially correlated with the morphology that the peripheral ending makes with type I and type II hair cells. If the location of the ending in the sensory epithelium is included, the correlations are further improved. It is also known that vestibular afferents can be immunohistochemically stained for a variety of different substances. We have concentrated on three of these markers, calretinin, calbindin and peripherin, because the sources of afferents to the vestibular nuclear complex that contain these substances are restricted, in two cases to the primary afferents. We demonstrate that calretinin is found only in the calyx-only afferents that are located at the apex of the cristae ampullaris and along the striola of the maculae. The area containing stained calyces is equal to or slightly smaller than the central zone of the cristae as defined by the Goldberg group [J. Neurophysiol. 60 (1988) 167]. Calbindin is also found in calyces at the apex of the cristae and along the striola of the otoliths. Examination of adjacent sections of all endorgans indicates that calbindin staining overlaps with calretinin, but is always several hair cells wider on each side. Peripherin also stains fibers in the neuroepithelium. The greatest density of staining is in the peripheral zone of the cristae, i.e. at the base and toward the planum semilunatum. We suggest that these substances are useful markers for specific sets of vestibular afferents.

Afferent Pathways↗
PubMed1999

Peripherin immunoreactivity labels small diameter vestibular 'bouton' afferents in rodents.

Recent morphophysiological studies have described three different subpopulations of vestibular afferents. The purpose of this study was to determine whether peripherin, a 56-kDa type III intermediate filament protein present in small sensory neurons in dorsal root ganglion and spiral ganglion cells, would also label thin vestibular afferents. Peripherin immunohistochemistry was done on vestibular sensory organs (cristae ampullares, utriculi and sacculi) of chinchillas, rats, and mice. In these sensory organs, immunoreactivity was confined to the extrastriolar region of the utriculus and the peripheral region of the crista. The labelled terminals were all boutons, except for an occasional calyx. In vestibular ganglia, immunoreactivity was restricted to small vestibular ganglion cells with thin axons. The immunoreactive central axons of vestibular ganglion cells form narrow bundles as they pass through the caudal spinal trigeminal tract. As they exit this tract, several bundles coalesce to form a single, narrow bundle passing caudally through the ventral part of the lateral vestibular nucleus. Finally, we conclude that all labelled axons and terminals were vestibular afferents rather than efferents, as no immunoreactivity in the vestibular efferent nucleus of the brainstem was observed.

Afferent Pathways↗
PubMed1992

Chromosomal localisation of the mouse and human peripherin genes.

Using a mouse cDNA probe encoding for the major part of peripherin, a type III intermediate filament protein, we have assigned, by in situ hybridization, the mouse and human peripherin genes, Prph, to the E-F region of chromosome 15 and to the q12-q13 region of chromosome 12, respectively. These regions are known as homologous chromosomal segments containing other intermediate filament genes (keratins) and also other genes which could be co-ordinately regulated.

Animals↗
PubMed1991

Origin of the beta cells of the islets of Langerhans is further questioned by the expression of neuronal intermediate filament proteins, peripherin and NF-L, in the rat insulinoma RIN5F cell line.

Intermediate filament proteins of the rat insulinoma RIN5F cell line were characterized. Two-dimensional gel analysis followed by immunostaining of proteins demonstrated that these cells express both peripherin and the low-molecular-mass neurofilament protein (NF-L); this was confirmed for peripherin by immunohistochemistry, peptide analysis and Northern blot. No expression of these proteins could be detected with these same methods either in the adult pancreas or in the tumor at the origin of the cell line, although such expression was apparent on sections of rat pancreas at embryonal day 16. These results were compared to those obtained on the rat pheochromocytoma PC12 cell line: expression in the adrenal medulla of the embryo, no expression either in the adult tissue or in the tumor, but solely in the derived cell line. The expression of neuronal intermediate filament proteins in the rat insulinoma RIN5F cell line is discussed in relation to its similarity in the rat pheochromocytoma PC12 cell line, and its meaning as to the developmental cell lineage; an ectodermal origin is suggested for the pancreatic islet cells.

Adrenal Medulla↗
PubMed1987

Peripherin. A rim-specific membrane protein of rod outer segment discs.

Monoclonal antibodies were used with radioimmune assays and immunocytochemical techniques to identify and localize membrane proteins in bovine rod outer segment (ROS) disc membranes. When ROS membrane proteins were separated by SDS-polyacrylamide gel electrophoresis in the presence of the sulfhydryl reducing agent, 2-mercaptoethanol, two monoclonal antibodies designated as 3B6 and 2B6 were found to bind to a polypeptide having an apparent molecular weight (Mr) of 33,000 daltons. In the absence of 2-mercaptoethanol, these monoclonal antibodies bound to a doublet having Mr of 67,000 and 69,000. Immunogold-dextran labeling of ROS sections embedded in Lowicryl resin indicated that this protein is localized around the periphery of the ROS organelle where the discs come in close contact to the ROS plasma membrane. Immunogold labeling of morphologically intact isolated discs prepared by mild trypsinization of ROS fragments confirmed that this disc membrane protein is localized along the rim region of discs. On the basis of these localization studies, the authors have named this protein peripherin. Immunogold-dextran markers were also used with previously characterized antirhodopsin monoclonal antibodies to visualize the distribution of rhodopsin on isolated discs. Dense labeling was observed along the lamellar region of the discs, but little if any labeling was observed on the extreme edges of the discs. These results are consistent with the view that the lamellar region of discs containing rhodopsin is a distinct membrane domain from the rim region which contains peripherin, a high Mr rim protein and possibly other proteins involved in disc-disc and disc-plasma membrane interactions.

Animals↗
PubMed1994

A Trk nerve growth factor (NGF) receptor point mutation affecting interaction with phospholipase C-gamma 1 abolishes NGF-promoted peripherin induction but not neurite outgrowth.

We analyzed the function of Trk nerve growth factor (NGF) receptors containing a point mutation (Tyr-->Phe) in a major autophosphorylation site (Tyr-785). Tyr-785 is required for phospholipase C-gamma 1 to interact with Trk and to become tyrosine-phosphorylated in response to NGF. The altered receptors were transfected into a mutant subline of PC12 rat pheochromocytoma cells (designated PC12nnr5) that, unlike wild-type PC12 cells, lack expression of endogenous Trk and responsiveness to NGF. PC12nnr5 cells permanently transfected with Trk Y785F exhibit NGF-dependent autophosphorylation and normal NGF binding and internalization. Moreover, Trk Y785F mediates NGF-stimulated neurite outgrowth as well as a variety of additional responses including induction of immediate-early and late genes. However, in contrast to cells expressing wild-type Trk, cells expressing Trk Y785F lack NGF-promoted elevation of peripherin intermediate filament mRNA and protein. These observations indicate that phospholipase C-gamma 1 activation or other signaling pathways dependent on Tyr-785 autophosphorylation are selectively required for regulation of peripherin expression by NGF, but not for many other functional NGF responses. This supports the presence of multiple and separable signaling pathways in the NGF mechanism of action.

Amino Acid Sequence↗
PubMed1996

Mutations and polymorphisms in the human peripherin-RDS gene and their involvement in inherited retinal degeneration.

The RDS gene codes for the protein peripherin-RDS, which is an integral membrane glycoprotein found in the outer segment of both rod and cone photoreceptor cells. It is thought to function as a structural protein involved in the maintenance of the flattened form of the disc lamellae. The RDS gene has been implicated in the mouse phenotype retinal degeneration slow, and mutations in the human homologue are now known to be associated with both central and peripheral retinal degenerations. In all, 43 sequence variants have been described in the human gene, including 30 missense mutations, two single base substitutions producing termination codons, 7 small in-frame deletions, and 4 insertion/ deletion events, which break the reading frame. Of these, 39 are associated with retinal phenotypes, which can be grouped into four broad categories: dominant retinitis pigmentosa, progressive macular degeneration, digenic RP, and pattern dystrophies. The mutations underlying dominant RP and severe macular degeneration are largely missense or small in-frame deletions in a large intradiscal loop between the third and fourth transmembrane domains. In contrast, those associated with the milder pattern phenotypes or with digenic RP are scattered more evenly through the gene and are often nonsense mutations. This observation correlates with the hypothesis that the large loop is an important site of interaction between RDS molecules and other protein components in the disc.

Animals↗
PubMed2006

RNAi-based suppression and replacement of rds-peripherin in retinal organotypic culture.

Extensive mutational heterogeneity presents a significant barrier to the development of therapeutics for RDS-peripherin-linked autosomal-dominant retinitis pigmentosa (RP), for which more than 50 disease-related mutations have been identified to date. Mutation-independent suppression, using RNA interference (RNAi), together with simultaneous expression of a replacement rds gene (r-rds, which has been altered to escape suppression but nevertheless encodes wild-type protein) has been explored in COS-7 cells and mouse retinal explants. The efficacy of small interfering and short hairpin RNAs (si/shRNAs) silencing mouse rds, and the function of r-rds (containing degenerate substitutions in the RNAi target sequence) were analyzed at transcript (RT-PCR) and protein (ELISA) levels in COS-7 cells. "Dual-" and "triple-expression" constructs carrying the shRNA suppressor and the marker EGFP with or without the r-rds cassette were electroporated in vitro into retinal explants from 1-day-old pups. The retinae were dissociated at day 14, and transduced cells were FACS-sorted using the coexpressed EGFP marker and analyzed by RT-PCR. si/shRNAs decreased rds mRNA and protein expression by up to 82%, while r-rds was protected from suppression in COS-7 cells. Similarly, efficient RNAi-mediated suppression of endogenous rds was detected in retinal explants, while concomitant rescue of r-rds was also achieved. These data validate the concept of RNAi-based suppression coupled with replacement technology for the development of therapies targeting RDS-linked autosomal-dominant RP, and suggest that such approaches could potentially be used for other autosomal-dominant diseases with similarly extensive intragenic heterogeneity.

Animals↗