AMPH
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Official Full Name
amphiphysin
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Overview
This gene encodes a protein associated with the cytoplasmic surface of synaptic vesicles. A subset of patients with stiff-man syndrome who were also affected by breast cancer are positive for autoantibodies against this protein. Alternate splicing of this gene results in two transcript variants encoding different isoforms. Additional splice variants have been described, but their full length sequences have not been determined. A pseudogene of this gene is found on chromosome 11. -
Synonyms
AMPH; amphiphysin; amphiphysin (Stiff Man syndrome with breast cancer 128kDa autoantigen) , amphiphysin (Stiff Mann syndrome with breast cancer 128kD autoantigen); amphiphysin I; amphiphysin (Stiff-Mann syndrome with breast cancer 128kD autoantigen); AMP;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Chicken
- Human
- Mouse
- Rat
- Zebrafish
- E.coli
- E.Coli or Yeast
- HEK293
- HEK293T
- In Vitro Cell Free System
- Mammalian Cell
- Wheat Germ
- C
- Myc
- DDK
- GST
- His
- His (Fc)
- Avi
- N/A
- Involved Pathway
- Protein Function
- Interacting Protein
- AMPH Related Research Area
AMPH involved in several pathways and played different roles in them. We selected most pathways AMPH participated on our site, such as Endocytosis, Fc gamma R-mediated phagocytosis, which may be useful for your reference. Also, other proteins which involved in the same pathway with AMPH were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Endocytosis | HRASB;WASLB;VPS25;CAV1;WIPF2B;GRK7A;ADRB3;RAB8A;USP8 |
Fc gamma R-mediated phagocytosis | ARPC1A;PPAP2B;BIN1;FCGR2A;WASF3;RAC1;SPHK1;ASAP3;RPS6KB2 |
AMPH has several biochemical functions, for example, phospholipid binding, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by AMPH itself. We selected most functions AMPH had, and list some proteins which have the same functions with AMPH. You can find most of the proteins on our site.
Function | Related Protein |
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phospholipid binding | SMURF1;WDFY4;ABCA1;PACSIN1A;BAD;ARHGAP26;APOEA;SYT14;GRK5 |
protein binding | NAA50;BNIP3;GUCY1B3;FBLN1;EIF4A3;NAALADL2;CHDH;SCAMP2;SEMA4D |
AMPH 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 AMPH here. Most of them are supplied by our site. Hope this information will be useful for your research of AMPH.
DNM1; DNM2; Ap2a2; Necap1; SYNJ1
- Q&As
- Reviews
Q&As (22)
Ask a questionYes, in addition to its role in synaptic vesicle endocytosis, AMPH protein can impact other aspects of neuronal function. For example, it has been suggested to play a role in regulating synaptic plasticity, which is essential for learning and memory. AMPH protein may also contribute to axonal growth and guidance during development, as well as neuronal migration in the developing brain.
Dysregulation of AMPH protein expression or function can have various consequences for neuronal function and synaptic vesicle recycling. Reduced or impaired AMPH protein function has been associated with decreased synaptic vesicle endocytosis, which can lead to reduced neurotransmitter release and impaired synaptic transmission. It may also impact synaptic plasticity, vesicle pool replenishment, and overall synaptic activity. Dysregulation of AMPH protein has been implicated in neurological and psychiatric disorders, highlighting its importance in neuronal physiology.
As our understanding of the role of AMPH protein in psychiatric disorders grows, it may become a potential target for therapeutic interventions. However, developing specific drugs that modulate AMPH activity or its associated pathways is challenging and would require further research and development.
Currently, there are no specific drugs or therapies targeting AMPH protein. However, research into understanding its role in neurological disorders may lead to potential therapeutic approaches in the future.
While AMPH protein is predominantly found in the brain and the nervous system, it has also been identified in other tissues to a lesser extent. These include tissues like the adrenal gland, kidney, and pancreas.
The expression of AMPH protein in neurons is regulated by various mechanisms. Transcription factors, such as myocyte enhancer factor 2 (MEF2) and neurogenic differentiation factor 1 (NeuroD1), can bind to the regulatory regions of the AMPH gene and control its expression. Additionally, epigenetic modifications, such as DNA methylation and histone acetylation, can influence AMPH gene expression. Furthermore, signaling pathways, like the cAMP-PKA pathway, can modulate AMPH protein expression through phosphorylation events.
AMPH protein has not been directly linked to neurodegenerative diseases. However, some studies have suggested its involvement in Parkinson's disease, a neurodegenerative disorder. Further research is needed to fully understand the relationship between AMPH protein and neurodegenerative diseases.
While research on the involvement of AMPH protein in neurodegenerative diseases is limited, there is emerging evidence to suggest its potential involvement. Studies have shown altered expression of AMPH protein in neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease.
Mutations or dysregulation of AMPH protein can disrupt synaptic vesicle endocytosis and neurotransmitter release, leading to impaired synaptic transmission. This can contribute to neurological disorders such as epilepsy, schizophrenia, and Parkinson's disease.
Yes, AMPH protein interacts with several other proteins and signaling pathways. One important interaction is with dynamin, a protein involved in vesicle scission during endocytosis. AMPH also interacts with clathrin, which is involved in the formation of clathrin-coated vesicles. Additionally, AMPH can interact with other synaptic proteins, such as synapsin and synaptophysin, which regulate synaptic vesicle trafficking.
AMPH protein plays a crucial role in synaptic vesicle endocytosis, a process essential for rapid recycling of vesicles after neurotransmitter release. Upon stimulation, AMPH protein is recruited to clathrin-coated pits, where it promotes vesicle membrane invagination and subsequent fission from the plasma membrane. This activity depends on the N-terminal BAR domain of AMPH, which binds to and induces membrane curvature.
AMPH protein is found mainly in the brain and the nervous system, particularly in synapses.
There is evidence to suggest that AMPH protein may be implicated in the pathophysiology of psychiatric disorders. Genetic studies have identified variations in the AMPH gene associated with psychiatric conditions such as schizophrenia and bipolar disorder.
The expression of AMPH protein can be regulated at the transcriptional level through interactions with transcription factors or signaling pathways. Additionally, post-translational modifications, such as phosphorylation, can affect its activity and stability.
The activity of AMPH protein is tightly regulated during synaptic vesicle endocytosis. It can be controlled through phosphorylation by various kinases, such as cyclin-dependent kinase 5 (CDK5) or cAMP-dependent protein kinase (PKA). These phosphorylation events can modulate AMPH protein function and localization, impacting its role in vesicle endocytosis.
Yes, several cellular and animal models have been used to study AMPH protein function. These include cell culture models, such as neuronal cell lines or primary neuronal cultures, where the effects of manipulating AMPH expression or function can be assessed. Animal models, such as mice or flies, with genetic modifications in the AMPH gene or alterations in AMPH protein expression, have also been used to investigate its role in neuronal function and disease. These models provide valuable insights into the cellular and physiological consequences of AMPH protein dysfunction.
Currently, there are no drugs specifically designed to target AMPH protein function or expression. However, certain medications used in the treatment of neurological and psychiatric disorders indirectly affect AMPH-related pathways. For example, drugs that increase dopamine or norepinephrine levels, such as amphetamines or certain antidepressants, can affect AMPH protein function.
Current areas of research on AMPH protein include investigating its precise mechanisms in synaptic vesicle endocytosis, understanding its role in neurological disorders, and exploring potential therapeutic strategies targeting AMPH-related pathways.
AMPH protein interacts with other proteins, such as dynamin and clathrin, to facilitate the formation of clathrin-coated vesicles. These vesicles engulf the neurotransmitter-filled synaptic vesicle membrane after neurotransmitter release, allowing for its retrieval and recycling.
Although there are currently no specific drugs targeting AMPH protein, understanding its role in neurological disorders may lead to potential therapeutic interventions in the future. Strategies could involve modulating the activity of proteins interacting with AMPH, or exploring AMPH-related pathways for drug development.
Yes, various animal models have been developed to study the function and role of AMPH protein. This includes genetically modified mice with altered AMPH expression or mutations in the AMPH gene. These models allow researchers to investigate the impact of AMPH dysfunction on synaptic vesicle endocytosis and neurotransmission.
The potential of targeting AMPH protein for therapeutic purposes in neurodegenerative diseases is not well-established. While its involvement in these conditions suggests a possible avenue for drug development, more research is needed to determine the extent of its contribution and to identify specific mechanisms that could be targeted. This would involve understanding the precise role of AMPH protein in neurodegeneration and developing strategies to modulate its activity or expression.
Customer Reviews (5)
Write a reviewTheir team of experts has been instrumental in resolving any queries or challenges I encountered regarding the application and utilization of the AMPH protein.
Its impeccable purity and integrity make it a valuable asset in my research endeavors.
Its reliability, versatility, and ability to deliver clear and reliable results make it a top choice for researchers in need of a high-quality protein for their experiments.
The AMPH protein surpasses expectations in terms of quality and is an ideal match for my experimental requirements.
This enhanced visibility and distinctness of the protein bands greatly aided in the accurate analysis and interpretation of my Western Blotting results.
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