Peripherin

Last updated
PRPH
Identifiers
Aliases PRPH , NEF4, PRPH1, peripherin
External IDs OMIM: 170710 MGI: 97774 HomoloGene: 4559 GeneCards: PRPH
Orthologs
SpeciesHumanMouse
Entrez

5630

19132

Ensembl

ENSG00000135406

ENSMUSG00000023484

UniProt

P41219

P15331

RefSeq (mRNA)

NM_006262

NM_001163588
NM_001163589
NM_013639

RefSeq (protein)

NP_006253

n/a

Location (UCSC) Chr 12: 49.29 – 49.3 Mb Chr 15: 98.95 – 98.96 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Peripherin is a type III intermediate filament protein expressed mainly in neurons of the peripheral nervous system. It is also found in neurons of the central nervous system that have projections toward peripheral structures, such as spinal motor neurons. Its size, structure, and sequence/location of protein motifs is similar to other type III intermediate filament proteins such as desmin, vimentin and glial fibrillary acidic protein. Like these proteins, peripherin can self-assemble to form homopolymeric filamentous networks (networks formed from peripherin protein dimers), but it can also heteropolymerize with neurofilaments in several neuronal types. This protein in humans is encoded by the PRPH gene. [5] [6] Peripherin is thought to play a role in neurite elongation during development and axonal regeneration after injury, but its exact function is unknown. It is also associated with some of the major neuropathologies that characterize amyotropic lateral sclerosis (ALS), but despite extensive research into how neurofilaments and peripherin contribute to ALS, their role in this disease is still unidentified. [7]

Contents

History

Peripherin, first named such in 1984, was also known as 57 kDa neuronal intermediate filament prior to 1990. In 1987, a second distinct peripherally located retinal rod protein was also given the name peripherin. To distinguish between the two, this second protein is referred to peripherin 2 or peripherin/RDS (retinal degeneration slow) for its location and role in retinal disease. [8]

Structure and properties

Peripherin was discovered as being the major intermediate filament in neuroblastoma cell lines and in rat pheochromocytoma cells. It is classified by gene structure and coding sequence as a type III intermediate filament protein because of its homology with vimentin, glial fibrillary acidic protein, and desmin. [9] All intermediate filament proteins share a common secondary structure consisting of three main domains, the most conserved of which is the central α-helical rod domain. This central coil is capped by non-helical head (N-terminal) and tail (C-terminal) domains. The α-helical rod domain contains repeating segments of hydrophobic amino acids, such that the first and fourth residues of every set of seven amino acids are usually nonpolar. This specific structure enables two intermediate filament polypeptides to coil together and create a "hydrophobic seal". [10] The rod also contains specific placement of alternating acidic and basic residues, many of which are spaced 4 amino acids apart. This spacing is optimal for the formation of ionic salt bridges, which serve to stabilize the α-helical rod through intrachain interactions. [10] A switch from intrachain salt bridges to interchain ionic associations may assist in intermediate filament assembly by utilizing electrostatic interactions to stabilize coiled-coil dimers. [10] The head and tail regions of intermediate filament proteins vary in length and amino acid composition, with greater variations in length occurring in the tail regions. [10]

Peripherin, unlike keratin IFs, can self-assemble and exist as homopolymers (see polymer). They can also heteropolymerize, or co-assemble, with other type III proteins or the light neurofilament subunit (NF-L) to form intermediate filament networks. [10] Type III proteins like peripherin can exist in different states within a cell. These states include nonfilamentous particles which combine to firm short IFs, or squiggles. These squiggles come together to form long IFs that make up cytoskeletal networks. [11] Studies of network assembly in spreading fibroblasts and differentiating nerve cells show that particles move along microtubules in a kinesin and dynein-dependent manner, and as spreading continues, the particles polymerize into intermediate filaments. [11]

In addition to the main species of peripherin, 57 kDa, two other forms have been identified in mice: Per 61 and Per 56. These two alternatives are both made by alternative splicing. Per 61 is created by introducing a 32 amino acid insertion within coil 2b of the α-helical rod domain of peripherin. Per 56 is made by a receptor on exon 9 of the peripherin gene transcript which induces a frameshift and replacement of a 21 amino acid sequence in the C-terminal found on the dominant 57 form with a new 8 amino acid sequence. The functions of these two alternative forms of peripherin are unknown. Per 57 and 56 are normally co-expressed, whereas Per 61 is not found in normal peripherin expression in adult motor neurons. [12]

Tissue distribution

Peripherin is widely expressed in the cell body and axons of neurons in the peripheral nervous system. These include small-sized root ganglion neurons, lower motor neurons, sensory and motor neurons of the cranial nerves, and autonomic neurons in ganglia and the enteric nervous system. It is also expressed in the central nervous system in a small set of brainstem and spinal cord neurons that have projections toward peripheral structures. Some of these structures include the hypothalamic magnocellular nuclei, pontine cholinergic nuclei, some cerebellar nuclei, and scattered neurons in the cerebral cortex. [8] They can also be found in the ventral horn neurons and in the cholinergic laterodorsal tegmentum (LDT) and pedunculopontine tegmentum (PPT) nuclei. [13]

A comparison of peripherin expression in the posterior and lateral hypothalamus in mice showed a sixty-fold higher expression in the posterior hypothalamus. This higher expression is due to the presence of peripherin in the tuberomammillary neurons of the mouse posterior hypothalamus. [13]

Function

The diverse properties of intermediate filaments, compared with the conserved microtubule and actin filament proteins, could be responsible for the distinguishing molecular shapes of different cell types. In nerve cells, for example, the expressions of different types of IFs relates to the change in shape during development. Early stages of development in neurons is marked by the outgrowth of neurites and axons contributing to the cells asymmetric shape. During these transitions in cell shape, only homopolymer type III intermediate filaments, such as those with peripherin, are made. As the nerve cell matures, these type III IFs are replaced by more complex type IV neurofilaments expanding the diameter of axons in order to attain normal velocities of action potentials. [14]

The exact function of peripherin is unknown. Expression of peripherin in development is greatest during the axonal growth phase and decreases postnatally, which suggests a role in neurite elongation and axonal guidance during development. Expression is also increased after axonal injury, such as peripheral axotomy in motor neurons and dorsal root ganglia. This upregulation implies that peripherin may also play a role in axon regeneration. [13] However, experiments using peripherin depleted PC12 cells and peripherin knockout mice provide proof that the majority of neurons have no requirement of peripherin for axonal guidance and regrowth. PC12 cells lacking peripherin showed no defects in neurite outgrowth and peripherin knockout mice develop normally with no anatomical abnormalities or different phenotypes. [9] In these experiments, peripherin deficiency did produce an upregulation of α-internexin, indicating the possibility that this type IV intermediate filament makes up for the loss of peripherin. Future studies of double knockout mice for both the peripherin and α-internexin genes might address this theory. [9] However, while most peripherin knockout mice displayed normal neuron growth, its absence did affect development of a subset of unmyelinated sensory axons. In such mice, there was a "34% reduction in the number of L5 unmyelinated sensory fibers that correlated with a decreased binding of the lectin IB4." [9]

PRPH Localization PRPH is located on the q12-q13 region of the human chromosome 12. Chromosome 12.jpeg
PRPH Localization PRPH is located on the q12-q13 region of the human chromosome 12.

Gene (PRPH)

The complete sequence of the human (GenBank L14565), rat (GenBank M26232) and mouse (EMBL X59840) peripherin genes (PRPH) have been reported and complementary DNAs (cDNA) thus far described are those for rat, mouse and Xenopus peripherin. [8] The use of a mouse cDNA probe during the in situ hybridization procedure allowed for the localization of the PRPH gene to the E-F region of mouse chromosome 15 and the q12-q13 region of human chromosome 12. [6]

The overall structure of the peripherin gene is nine exons separated by eight introns. This configuration is conserved among the three known mammalian species with known coding for peripherin, namely human, rat and mouse. The nucleotide sequences of human and rat exons were 90% identical and produced a predicted protein that differed at only 18 of 475 amino acid residues. Comparison of introns 1 and 2 also yielded high homology of conserved segments. The 5' flanking regions and regulatory sequences were also very similar and a nerve growth factor negative regulatory element, a Hox protein (See Hox gene) binding site, and a heat shock element were found in all known peripherin genes. [15]

Regulatory mechanisms

Nerve growth factor (NGF) plays the major role in the regulation of peripherin. It is both a transcriptional inducer and post-translational regulator of peripherin expression in PC12 and neuroblastoma cells. The mechanism of NGF-induced activation occurs through 5' flanking elements and intragenic sequences involving the TATA box and other upstream elements as well as depression at a negative element. The specific signals regulating peripherin expression in vivo are unknown. The peripherin gene is transcriptionally activated in both small and large sized sensory neurons of the dorsal root ganglion at about day E10, and mRNA is present in these cells after postnatal day 2 and throughout adulthood. Post transcriptional mechanisms reduce detectable peripherin to only the small sized cells; however, crushing of the peripheral processes in dorsal root ganglion neurons lead to mRNA and detectable peripherin in the large sized cells. [8]

The proinflammatory cytokines, interleukin-6 and leukemia inhibitory factor, can also induce peripherin expression through the JAK-STAT signaling pathway. This specific upregulation is linked to neuronal regeneration. [12]

Potential role in the pathogenesis of amyotrophic lateral sclerosis

Protein and neurofilamentous aggregates are characteristic of patients with amyotrophic lateral sclerosis, a progressive, fatal neurodegenerative disease. Spheroids, specifically, which are protein aggregates of neuronal intermediate filaments, have been found in patients with amyotrophic lateral sclerosis. Peripherin has been found in such spheroids in conjunction with other neurofilaments in other neuronal diseases, thus suggesting that peripherin may play a role in the pathogenesis of amyotrophic lateral sclerosis. [7]

Alternative splicing

An alternatively spliced mouse peripherin variant was identified that includes intron 4, a region that is spliced out of the abundant peripherin forms. Because of the change in reading frame, this variant produces a larger form of peripherin (Per61). In human peripherin, the inclusion of introns 3 and 4, regions that are similarly spliced out of the abundant peripherin protein forms, results in the generation of a truncated peripherin protein (Per28). In both cases, an antibody specific to a peptide coded by the intron regions stained the filamentous inclusions of in tissues affected by amyotrophic lateral sclerosis. These studies suggest that such alternative splicing could play a role in the disease and lend themselves to further investigation. [7]

Mutations

Experiments examining peripherin overexpression in mice have suggested that PRPH mutations play a role in the pathogenesis of amyotrophic lateral sclerosis, with more recent studies investigating the prevalence of such mutations in humans. Though many polymorphic variants of PRPH exist, two variants of PRPH were seen uniquely in patients with ALS, both of which consisted of a frameshift mutation. In the first variant, a single base pair deletion in exon 1 of PRPH was predictive of a peripherin species truncated to 85 amino acids. This truncation negatively impacted the ability of the neurofilament network to assemble, thus suggesting that mutations in PRPH may play a role in at least a small percentage of human cases of amyotrophic lateral sclerosis. [16]

The second variant consisted of an amino acid substitution from aspartate to tyrosine as a result of a single point mutation in exon 1. This was also shown to adversely affect the assembly of the neurofilament network. The PRPH mutations observed in amyotrophic lateral sclerosis cause a change in the 3D structure of the protein. Consequently, the mutant peripherin forms aggregates instead of the filamentous network that it usually forms. [17]

Other clinical significance

Peripherin may be involved in the pathology of insulin-dependent diabetes mellitus (or diabetes mellitus type 1) in animals; however, no direct linkage has been found in human patients. In a nonobese diabetic mouse model, peripherin has been found as a known autoantigen (See antigen). B cell clones reactive to peripherin have also been found in early stages of the disease. Since peripherin is expressed in both the peripheral nervous system and, in young animals, by islet beta cells, it is possible that the destruction of both peripheral nervous system elements and islet β-cells in insulin-dependent diabetes mellitus is due to the immune response to autoreactive peripherin. [13]

Peripherin can also play a role in the definitive diagnosis of Hirschsprung disease. Patients suspected of having the disease undergo rectal biopsy to look for the presence or absence of ganglion cells. However, the identification of these cells can be very difficult, especially in newborns where immature ganglion cells are easily confused with endothelial, mesenchyme and inflammatory cells. To aid in identification, a protocol utilizing peripherin and S-100 immunohistochemistry staining was developed to assist in the recognition of ganglion cells in rectal biopsies. [18]

Potential applications

Possible involvement of intermediate filaments such as peripherin in neurodegenerative diseases is currently being investigated. Interactions between intermediate filaments and other proteins are also being pursued. Peripherin has been shown to associate with protein kinase Cε, inducing its aggregation and leading to increased apoptosis. It may be possible to regulate this aggregation and apoptosis using siRNAs and protein kinase Cε. [19] Pinpointing the source and possible resolution of protein aggregates is a promising direction for potential therapeutics. [7]

Related Research Articles

<span class="mw-page-title-main">Schwann cell</span> Glial cell type

Schwann cells or neurolemmocytes are the principal glia of the peripheral nervous system (PNS). Glial cells function to support neurons and in the PNS, also include satellite cells, olfactory ensheathing cells, enteric glia and glia that reside at sensory nerve endings, such as the Pacinian corpuscle. The two types of Schwann cells are myelinating and nonmyelinating. Myelinating Schwann cells wrap around axons of motor and sensory neurons to form the myelin sheath. The Schwann cell promoter is present in the downstream region of the human dystrophin gene that gives shortened transcript that are again synthesized in a tissue-specific manner.

<span class="mw-page-title-main">Intermediate filament</span> Cytoskeletal structure

Intermediate filaments (IFs) are cytoskeletal structural components found in the cells of vertebrates, and many invertebrates. Homologues of the IF protein have been noted in an invertebrate, the cephalochordate Branchiostoma.

<span class="mw-page-title-main">Astrogliosis</span> Increase in astrocytes in response to brain injury

Astrogliosis is an abnormal increase in the number of astrocytes due to the destruction of nearby neurons from central nervous system (CNS) trauma, infection, ischemia, stroke, autoimmune responses or neurodegenerative disease. In healthy neural tissue, astrocytes play critical roles in energy provision, regulation of blood flow, homeostasis of extracellular fluid, homeostasis of ions and transmitters, regulation of synapse function and synaptic remodeling. Astrogliosis changes the molecular expression and morphology of astrocytes, in response to infection for example, in severe cases causing glial scar formation that may inhibit axon regeneration.

Internexin, alpha-internexin, is a Class IV intermediate filament approximately 66 KDa. The protein was originally purified from rat optic nerve and spinal cord. The protein copurifies with other neurofilament subunits, as it was originally discovered, however in some mature neurons it can be the only neurofilament expressed. The protein is present in developing neuroblasts and in the central nervous system of adults. The protein is a major component of the intermediate filament network in small interneurons and cerebellar granule cells, where it is present in the parallel fibers.

Neurofilaments (NF) are classed as type IV intermediate filaments found in the cytoplasm of neurons. They are protein polymers measuring 10 nm in diameter and many micrometers in length. Together with microtubules (~25 nm) and microfilaments (7 nm), they form the neuronal cytoskeleton. They are believed to function primarily to provide structural support for axons and to regulate axon diameter, which influences nerve conduction velocity. The proteins that form neurofilaments are members of the intermediate filament protein family, which is divided into six types based on their gene organization and protein structure. Types I and II are the keratins which are expressed in epithelia. Type III contains the proteins vimentin, desmin, peripherin and glial fibrillary acidic protein (GFAP). Type IV consists of the neurofilament proteins NF-L, NF-M, NF-H and α-internexin. Type V consists of the nuclear lamins, and type VI consists of the protein nestin. The type IV intermediate filament genes all share two unique introns not found in other intermediate filament gene sequences, suggesting a common evolutionary origin from one primitive type IV gene.

<span class="mw-page-title-main">L1 (protein)</span> Mammalian protein found in Homo sapiens

L1, also known as L1CAM, is a transmembrane protein member of the L1 protein family, encoded by the L1CAM gene. This protein, of 200-220 kDa, is a neuronal cell adhesion molecule with a strong implication in cell migration, adhesion, neurite outgrowth, myelination and neuronal differentiation. It also plays a key role in treatment-resistant cancers due to its function. It was first identified in 1984 by M. Schachner who found the protein in post-mitotic mice neurons.

In cellular neuroscience, an axotomy is the cutting or otherwise severing of an axon. This type of denervation is often used in experimental studies on neuronal physiology and neuronal death or survival as a method to better understand nervous system diseases.

<span class="mw-page-title-main">Neurodegenerative disease</span> Central nervous system disease

A neurodegenerative disease is caused by the progressive loss of structure or function of neurons, in the process known as neurodegeneration. Such neuronal damage may ultimately involve cell death. Neurodegenerative diseases include amyotrophic lateral sclerosis, multiple sclerosis, Parkinson's disease, Alzheimer's disease, Huntington's disease, multiple system atrophy, tauopathies, and prion diseases. Neurodegeneration can be found in the brain at many different levels of neuronal circuitry, ranging from molecular to systemic. Because there is no known way to reverse the progressive degeneration of neurons, these diseases are considered to be incurable; however research has shown that the two major contributing factors to neurodegeneration are oxidative stress and inflammation. Biomedical research has revealed many similarities between these diseases at the subcellular level, including atypical protein assemblies and induced cell death. These similarities suggest that therapeutic advances against one neurodegenerative disease might ameliorate other diseases as well.

<span class="mw-page-title-main">CD90</span> Mammalian protein found in Homo sapiens

Thy-1 or CD90 is a 25–37 kDa heavily N-glycosylated, glycophosphatidylinositol (GPI) anchored conserved cell surface protein with a single V-like immunoglobulin domain, originally discovered as a thymocyte antigen. Thy-1 can be used as a marker for a variety of stem cells and for the axonal processes of mature neurons. Structural study of Thy-1 led to the foundation of the Immunoglobulin superfamily, of which it is the smallest member, and led to some of the initial biochemical description and characterization of a vertebrate GPI anchor and also the first demonstration of tissue specific differential glycosylation.

<span class="mw-page-title-main">Nestin (protein)</span> Protein-coding gene in the species Homo sapiens

Nestin is a protein that in humans is encoded by the NES gene.

Nerve tissue is a biological molecule related to the function and maintenance of normal nervous tissue. An example would include, for example, the generation of myelin which insulates and protects nerves. These are typically calcium-binding proteins.

<span class="mw-page-title-main">Peripheral myelin protein 22</span> Protein-coding gene in the species Homo sapiens

Growth arrest-specific protein 3 (GAS-3), also called peripheral myelin protein 22 (PMP22), is a protein which in humans is encoded by the PMP22 gene.

<span class="mw-page-title-main">Semaphorin-3A</span> Protein-coding gene in the species Homo sapiens

Semaphorin-3A is a protein that in humans is encoded by the SEMA3A gene.

<span class="mw-page-title-main">NEFM</span> Protein-coding gene in the species Homo sapiens

Neurofilament medium polypeptide (NF-M) is a protein that in humans is encoded by the NEFM gene.

<span class="mw-page-title-main">SCN8A</span> Protein-coding gene in the species Homo sapiens

Sodium channel protein type 8 subunit alpha also known as Nav1.6 is a membrane protein encoded by the SCN8A gene. Nav1.6 is one sodium channel isoform and is the primary voltage-gated sodium channel at each node of Ranvier. The channels are highly concentrated in sensory and motor axons in the peripheral nervous system and cluster at the nodes in the central nervous system.

<span class="mw-page-title-main">Neurofilament light polypeptide</span> Protein-coding gene in the species Homo sapiens

Neurofilament light polypeptide, also known as neurofilament light chain, abbreviated to NF-L or Nfl and with the HGNC name NEFL is a member of the intermediate filament protein family. This protein family consists of over 50 human proteins divided into 5 major classes, the Class I and II keratins, Class III vimentin, GFAP, desmin and the others, the Class IV neurofilaments and the Class V nuclear lamins. There are four major neurofilament subunits, NF-L, NF-M, NF-H and α-internexin. These form heteropolymers which assemble to produce 10nm neurofilaments which are only expressed in neurons where they are major structural proteins, particularly concentrated in large projection axons. Axons are particularly sensitive to mechanical and metabolic compromise and as a result axonal degeneration is a significant problem in many neurological disorders. The detection of neurofilament subunits in CSF and blood has therefore become widely used as a biomarker of ongoing axonal compromise. The NF-L protein is encoded by the NEFL gene. Neurofilament light chain is a biomarker that can be measured with immunoassays in cerebrospinal fluid and plasma and reflects axonal damage in a wide variety of neurological disorders. It is a useful marker for disease monitoring in amyotrophic lateral sclerosis, multiple sclerosis, Alzheimer's disease, and more recently Huntington's disease. It is also promising marker for follow-up of patients with brain tumors. Higher levels of blood or CSF NF-L have been associated with increased mortality, as would be expected as release of this protein reflects ongoing axonal loss. Recent work performed as a collaboration between EnCor Biotechnology Inc. and the University of Florida showed that the NF-L antibodies employed in the most widely used NF-L assays are specific for cleaved forms of NF-L generated by proteolysis induced by cell death. Methods used in different studies for NfL measurement are sandwich enzyme-linked immunosorbent assay (ELISA), electrochemiluminescence, and high-sensitive single molecule array (SIMOA).

<span class="mw-page-title-main">Chromatolysis</span> Dissolution of a neurons Nissl bodies

In cellular neuroscience, chromatolysis is the dissolution of the Nissl bodies in the cell body of a neuron. It is an induced response of the cell usually triggered by axotomy, ischemia, toxicity to the cell, cell exhaustion, virus infections, and hibernation in lower vertebrates. Neuronal recovery through regeneration can occur after chromatolysis, but most often it is a precursor of apoptosis. The event of chromatolysis is also characterized by a prominent migration of the nucleus towards the periphery of the cell and an increase in the size of the nucleolus, nucleus, and cell body. The term "chromatolysis" was initially used in the 1940s to describe the observed form of cell death characterized by the gradual disintegration of nuclear components; a process which is now called apoptosis. Chromatolysis is still used as a term to distinguish the particular apoptotic process in the neuronal cells, where Nissl substance disintegrates.

Collapsin response mediator protein family or CRMP family consists of five intracellular phosphoproteins of similar molecular size and high (50–70%) amino acid sequence identity. CRMPs are predominantly expressed in the nervous system during development and play important roles in axon formation from neurites and in growth cone guidance and collapse through their interactions with microtubules. Cleaved forms of CRMPs have also been linked to neuron degeneration after trauma induced injury.

<span class="mw-page-title-main">Epigenetics of neurodegenerative diseases</span> Field of study

Neurodegenerative diseases are a heterogeneous group of complex disorders linked by the degeneration of neurons in either the peripheral nervous system or the central nervous system. Their underlying causes are extremely variable and complicated by various genetic and/or environmental factors. These diseases cause progressive deterioration of the neuron resulting in decreased signal transduction and in some cases even neuronal death. Peripheral nervous system diseases may be further categorized by the type of nerve cell affected by the disorder. Effective treatment of these diseases is often prevented by lack of understanding of the underlying molecular and genetic pathology. Epigenetic therapy is being investigated as a method of correcting the expression levels of misregulated genes in neurodegenerative diseases.

Research on amyotrophic lateral sclerosis (ALS) has focused on animal models of the disease, its mechanisms, ways to diagnose and track it, and treatments.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000135406 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000023484 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ "Entrez Gene: Peripherin".
  6. 1 2 Moncla A, Landon F, Mattei MG, Portier MM (April 1992). "Chromosomal localisation of the mouse and human peripherin genes". Genetical Research. 59 (2): 125–9. doi: 10.1017/s0016672300030330 . PMID   1378416.
  7. 1 2 3 4 Liem RK, Messing A (July 2009). "Dysfunctions of neuronal and glial intermediate filaments in disease". The Journal of Clinical Investigation. 119 (7): 1814–24. doi:10.1172/JCI38003. PMC   2701870 . PMID   19587456.
  8. 1 2 3 4 Vale, Ronald; Kreis, Thomas (1999). Guidebook to the Cytoskeletal and Motor Proteins (2nd ed.). Sambrook & Tooze Partnership.
  9. 1 2 3 4 Larivière RC, Nguyen MD, Ribeiro-da-Silva A, Julien JP (May 2002). "Reduced number of unmyelinated sensory axons in peripherin null mice". Journal of Neurochemistry. 81 (3): 525–32. doi:10.1046/j.1471-4159.2002.00853.x. PMID   12065660. S2CID   15737750.
  10. 1 2 3 4 5 Fuchs E, Weber K (1994). "Intermediate filaments: structure, dynamics, function, and disease". Annual Review of Biochemistry. 63: 345–82. doi:10.1146/annurev.bi.63.070194.002021. PMID   7979242.
  11. 1 2 Chang L, Shav-Tal Y, Trcek T, Singer RH, Goldman RD (February 2006). "Assembling an intermediate filament network by dynamic cotranslation". The Journal of Cell Biology. 172 (5): 747–58. doi:10.1083/jcb.200511033. PMC   2063706 . PMID   16505169.
  12. 1 2 Xiao S, McLean J, Robertson J (2006). "Neuronal intermediate filaments and ALS: a new look at an old question". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1762 (11–12): 1001–12. doi: 10.1016/j.bbadis.2006.09.003 . PMID   17045786.
  13. 1 2 3 4 Eriksson KS, Zhang S, Lin L, Larivière RC, Julien JP, Mignot E (2008). "The type III neurofilament peripherin is expressed in the tuberomammillary neurons of the mouse". BMC Neuroscience. 9: 26. doi: 10.1186/1471-2202-9-26 . PMC   2266937 . PMID   18294400.
  14. ↑ Chang L, Goldman RD (August 2004). "Intermediate filaments mediate cytoskeletal crosstalk". Nature Reviews. Molecular Cell Biology. 5 (8): 601–13. doi:10.1038/nrm1438. PMID   15366704. S2CID   31835055.
  15. ↑ Foley J, Ley CA, Parysek LM (July 1994). "The structure of the human peripherin gene (PRPH) and identification of potential regulatory elements". Genomics. 22 (2): 456–61. doi:10.1006/geno.1994.1410. PMID   7806235.
  16. ↑ Gros-Louis F, Larivière R, Gowing G, Laurent S, Camu W, Bouchard JP, Meininger V, Rouleau GA, Julien JP (October 2004). "A frameshift deletion in peripherin gene associated with amyotrophic lateral sclerosis". The Journal of Biological Chemistry. 279 (44): 45951–6. doi: 10.1074/jbc.M408139200 . PMID   15322088.
  17. ↑ Leung CL, He CZ, Kaufmann P, Chin SS, Naini A, Liem RK, Mitsumoto H, Hays AP (July 2004). "A pathogenic peripherin gene mutation in a patient with amyotrophic lateral sclerosis". Brain Pathology. 14 (3): 290–6. doi:10.1111/j.1750-3639.2004.tb00066.x. PMC   8095763 . PMID   15446584. S2CID   43439366.
  18. ↑ Holland SK, Hessler RB, Reid-Nicholson MD, Ramalingam P, Lee JR (September 2010). "Utilization of peripherin and S-100 immunohistochemistry in the diagnosis of Hirschsprung disease". Modern Pathology. 23 (9): 1173–9. doi: 10.1038/modpathol.2010.104 . PMID   20495540.
  19. ↑ Sunesson L, Hellman U, Larsson C (June 2008). "Protein kinase Cepsilon binds peripherin and induces its aggregation, which is accompanied by apoptosis of neuroblastoma cells". The Journal of Biological Chemistry. 283 (24): 16653–64. doi: 10.1074/jbc.M710436200 . PMID   18408015.
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