PRPH

Case Study 1: Todd M Doran, 2016

A major goal in understanding autoimmune diseases is to define the antigens that elicit a self-destructive immune response, but this is a difficult endeavor. In an effort to discover autoantigens associated with type 1 diabetes (T1D), the researchers used epitope surrogate technology that screens combinatorial libraries of synthetic molecules for compounds that could recognize disease-linked autoantibodies and enrich them from serum. Autoantibodies from one patient revealed a highly phosphorylated form of peripherin, a neuroendocrine filament protein, as a candidate T1D antigen. Peripherin antibodies were detected in 72% of donor patient sera. Further analysis revealed that the T1D-associated antibodies only recognized a dimeric conformation of peripherin. These data explain why peripherin was dismissed as an important T1D antigen previously. The discovery of this novel autoantigen would not have been possible using standard methods, such as hybridizing serum antibodies to recombinant protein arrays, highlighting the power of epitope surrogate technology for probing the mechanism of autoimmune diseases.

Fig1. Assessment of serum antibody binding to 4 from healthy and control donors in the absence of competitor (black bars).

Fig2. Competition serum binding analysis using phosphoprotein enriched peripherin as the specific competitor.

Case Study 2: Jesse McLean, 2010

Peripherin is a type III intermediate filament protein that is up-regulated during neuronal injury and is a major component of pathological inclusions found within degenerating motor neurons of patients with amyotrophic lateral sclerosis (ALS). The relationship between these inclusions and their protein constituents remains largely unknown. Here, the researchers profile peripherin isoform expression and ratio changes in traumatic neuronal injury, transgenic mouse models of motor neuron disease, and ALS. Extensive western blot analyses of Triton X-100 soluble and insoluble fractions of neuronal tissue from these conditions revealed significant changes in peripherin isoform content which could be differentiated by electrophoretic banding patterns to produce distinct peripherin biochemical signatures. Significantly, they found that the pattern of peripherin expression in ALS most closely approximates that of peripherin over-expressing mice, but differs with regard to inter-individual variations in isoform-specific expression.

Fig3. The sciatic nerve of sham- and crush-operated WT mice were separated into Triton X-100 insoluble.

Fig4. Prototypical electrophoretic banding patterns of peripherin isoform expression in various conditions reveal distinct biochemical signatures.

PRPH involved in several pathways and played different roles in them. We selected most pathways PRPH participated on our site, such as Amyotrophic lateral sclerosis (ALS), which may be useful for your reference. Also, other proteins which involved in the same pathway with PRPH were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

PRPH has several biochemical functions, for example, protein heterodimerization activity, structural molecule activity. Some of the functions are cooperated with other proteins, some of the functions could acted by PRPH itself. We selected most functions PRPH had, and list some proteins which have the same functions with PRPH. You can find most of the proteins on our site.

PRPH has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with PRPH here. Most of them are supplied by our site. Hope this information will be useful for your research of PRPH.

VIM; KRT15; GABARAPL2; ESR2; GABARAPL1