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High resolution structure confirm for the first time that the Serpin 42 Da isoforms are typical inhibitory serpin family members with the conserved serpin fold and inhibitory mechanism.
involved in the cellular regulation of prohormone convertases
Results report the identification of Spn4A, a previously uncharacterized secretory pathway serine protease inhibitor (serpin) from Drosophila melanogaster that contains a consensus furin cleavage site.
Spn4 gene represents a versatile defence tool kit that may provide multiple antiproteolytic functions.
The results of this identify neuroserpin as a modulator of synaptic plasticity, and point to a role for neuroserpin in learning and memory.
the protective effect of neuroserpin maybe independent from its canonical interaction with a tissue-type plasminogen activator
Brain metastatic cells from lung cancer and breast cancer express high levels of anti-plasminogen activator (PA) serpins, including neuroserpin and serpin B2, to prevent plasmin generation and its metastasis-suppressive effects.
Data indicate that the neuroprotective effect of neuroserpin is due to inhibition of plasmin-mediated excitotoxin-induced cell death and is independent of neuroserpin's ability to inhibit tissue plasminogen activator activity.
Neuroserpin reduces microglial activation and, therefore, plasminogen activator levels; it has a neuroprotective role after focal ischemic stroke.
Neuroserpin mRNA is widely expressed in neuronal cells in the primary visual cortex during normal development as well as in the adult mouse.
Our results implicate neuroserpin in the regulation of emotional behavior through a mechanism that is at least in part independent of tissue type plasminogen activator activity
neuroserpin levels appear to be carefully regulated by LRP and an unidentified cofactor, and this pathway may be critical for maintaining the balance between proteases and inhibitors
Altogether, these data suggest that an overexpression of neuroserpin in the brain parenchyma might limit the deleterious effect of tPA on NMDA receptor-mediated neuronal death, which occurs following experimental ischemia.
Transgenic mice overexpressing neuroserpin have decreased plasminogen activators in sciatic nerve and spinal cord, confirming a role for neuroserpin in the evolution of a neurodegenerative disease.
the existence of an AMH-dependent signalling pathway in the brain leading to an overexpression of the serine-protease inhibitor, neuroserpin, and neuronal survival
Mutation-, aging-, and gene dosage-dependent accumulation of neuroserpin (G392E) in endoplasmic reticula and lysosomes of neurons in transgenic mice
We present two pediatric cases of progressive myoclonic epilepsy with SERPINI1 pathogenic variants that lead to a severe presentation.
Data indicated that rs9853967 and rs11714980 polymorphisms in CCM3 and SERPINI1respectively could be associated with a protective role in cerebral cavernous malformations disease.
SERPINI1 is an important regulator of epithelial-mesenchymal transition in an orthotopic implantation model of colorectal cancer
The thermal and chemical stability along with the polymerisation propensity of both Wild Type and Glu289Ala NS were characterized.
This C-terminal lability is not required for neuroserpin polymerisation in the endoplasmic reticulum, but the additional glycan facilitates degradation of the mutant protein during proteasomal impairment.
Neuroserpin is expressed in naive effector memory and central memory CD4 and CD8 T cell subsets, and monocytes, B cells, and NK cells. T-cell activation caused its translocation to the immunologic synapse, secretion, and delayed downregulation.
Molecular Dynamics simulations suggest that Neuroserpin conformational stability and flexibility arise from a spatial distribution of intramolecular salt-bridges and hydrogen bonds.
Alzheimer's disease brain tissues with elevated neuroserpin protein also showed increased expression of THRbeta1 and HuD
our study did not provide any evidence for an association between genetic variation at the SERPINI1 locus and ischemic stroke
the origins of conformational lability
Neuroprotective properties of neuroserpin may be related to the inhibition of excitotoxicity, inflammation, as well as blood brain barrier disruption that occur after acute ischemic stroke.
Hrd1 and gp78 mediate mutant neuroserpin turnover through the ERAD pathway.
high serum neuroserpin levels before intravenous tPA and neuroserpin levels decrease at 24 h after ischaemic stroke, independently of tPA treatment, may have a role in good functional outcome
The latent and polymer hNS forms obtained at 45 degrees C and 85 degrees C differ in their chemical and thermal stabilities; furthermore, the human neuroserpin polymers also differ in size and morphology
investigated the refolding and polymerization pathways of wild-type neuroserpin and of the pathogenic mutants S49P and H338R
Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro
The interactions between NSP and t-PA were distinct from those between plasmin and NSP, suggesting that the physiologic effect of t-PA-NSP interactions may be more complex than previously thought.
Neuroserpin has a role as a selective inhibitor of tissue-type plasminogen activator in the central nervous system [review]
neuroserpin mutants that cause dementia accumulate as polymers within the endoplasmic reticulum
This gene encodes a member of the serpin superfamily of serine proteinase inhibitors. The protein is primarily secreted by axons in the brain, and preferentially reacts with and inhibits tissue-type plasminogen activator. It is thought to play a role in the regulation of axonal growth and the development of synaptic plasticity. Mutations in this gene result in familial encephalopathy with neuroserpin inclusion bodies (FENIB), which is a dominantly inherited form of familial encephalopathy and epilepsy characterized by the accumulation of mutant neuroserpin polymers. Multiple alternatively spliced variants, encoding the same protein, have been identified.
, serine protease inhibitor 4
, serpin 4
, serpin 42Da
, serpin peptidase inhibitor, clade I (neuroserpin), member 1
, peptidase inhibitor 12
, protease inhibitor 17
, serine protease inhibitor 17
, serpin I1
, serine (or cysteine) proteinase inhibitor, clade I (neuroserpin), member 1
, serine (or cysteine) peptidase inhibitor, clade I, member 1
, serine (or cysteine) proteinase inhibitor clade member 1
, serpin peptidase inhibitor, clade I, member 1