Distribution of serine proteinase inhibitor, clade B, member 6 (Serpinb6) in the adult mouse brain

Kishi, Tadaaki; Matsuhashi, Hitomi; Bird, Phillip I.; Kato, Keiko

doi:10.1016/s1567-133x(02)00014-5

Cited by 6 publications

(5 citation statements)

References 14 publications

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“…PI-6 and SPI3 are efficient inhibitors of neuropsin/kallikrein 8. SPI3 is coexpressed with neuropsin in various regions of the brain, particularly in neurons of the hippocampus (25), and its expression is up-regulated during ischemia (31). Other serpins also expressed in the rodent brain have been shown to protect neurons from damage induced by stroke (8,42).…”

Section: Spi3-deficient Micementioning

confidence: 99%

“…Although SPI3 is expressed in mouse brain (25), is up-regulated during transient focal ischemia (31), and is known to regulate the neuronal protease neuropsin (24), SPI3-deficient mice do not exhibit increased infarct size in response to stroke. This suggests that SPI3 is not involved in regulating proteases activated during ischemic injury and that other serpins, such as neuroserpin, may be more important for this function.…”

Section: Spi3-deficient Micementioning

confidence: 99%

“…Neuropsin processes extracellular matrix, is important for neuronal plasticity, and is significantly up-regulated in cases of Alzheimer's disease (17,38). Coexpression of PI-6 and neuropsin occurs in developing and adult brains (24,25), and PI-6 is up-regulated following ischemia (31), suggesting that it protects against ectopic neuropsin. As exemplified by PSA (9), kallikreins are stored in cytoplasmic storage vesicles analogous to leukocyte granules, so PI-6 may protect against kallikrein leakage from storage vesicles or from protease that is reinternalized after release.…”

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confidence: 99%

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Targeted Disruption of SPI3/Serpinb6 Does Not Result in Developmental or Growth Defects, Leukocyte Dysfunction, or Susceptibility to Stroke

Scarff¹,

Ung²,

Nandurkar

et al. 2004

Molecular and Cellular Biology

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Protease inhibitor 6 (PI-6/SERPINB6) is a widely expressed nucleocytoplasmic serpin. It inhibits granulocyte cathepsin G and neuronal neuropsin, and it is thought to protect cells from death caused by ectopic release or internalization of protease during stress such as infection or cerebral ischemia. To probe the biological functions of PI-6, we generated mice lacking its ortholog (SPI3/Serpinb6). SPI3-deficient mice developed normally and were fertile, and no abnormal pathology or increased sensitivity to cerebral ischemia was observed. There were no perturbations in leukocyte development or numbers, and recruitment of leukocytes to the peritoneal cavity was normal. SPI3-deficient mice were equally susceptible as wild-type mice to systemic Candida albicans infection, although there was a slight decrease in the ability of neutrophils from SPI3-deficient mice to kill C. albicans in vitro. Increased levels of a related inhibitor Serpinb1 (monocyte/neutrophil elastase inhibitor) in the tissues of targeted mice suggests that compensation by other serpins reduces the impact of SPI3 deficiency in these animals and may explain the lack of a more obvious phenotype.

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Section: Spi3-deficient Micementioning

confidence: 99%

Section: Spi3-deficient Micementioning

confidence: 99%

mentioning

confidence: 99%

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Targeted Disruption of SPI3/Serpinb6 Does Not Result in Developmental or Growth Defects, Leukocyte Dysfunction, or Susceptibility to Stroke

Scarff¹,

Ung²,

Nandurkar

et al. 2004

Molecular and Cellular Biology

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“…In the present study, the expression of neuropsin in both the amygdala and stomach was increased in the FD group, while that of the serine peptidase inhibitor serpinb6 was decreased. Serpinb6 has been found to be strongly expressed in most somatic and visceral motoneurons 25 and in the mast cells in all organs 26 . It inhibits granulocyte cathepsin G and neuronal neuropsin, and is thought to protect cells from death caused by ectopic release or internalization of protease during stress 7 .…”

Section: Discussionmentioning

confidence: 99%

The role of amygdala neuropsin/serpinb6 pathway in the regulation of gastric hypersensitivity and anxiety by electroacupuncture

Chen

Yang

Zhang

et al. 2022

J of Digest Diseases

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Objective To investigate whether the neuropsin pathway in the amygdala and stomach may participate in the development of anxiety‐related gastric hypersensitivity, and whether electroacupuncture (EA) at the Zusanli acupoint could improve this condition by regulating such pathway in the rat model of functional dyspepsia (FD). Methods A total of 48 SD rats were randomly divided into the control group, FD model group and FD + EA group (stimulation at Zusanli acupoint for 30 min daily for 7 consecutive days). Abdominal withdrawal reflex (AWR) score and open field test were used to evaluate visceral hypersensitivity and anxiety‐like disorder, respectively. Electrical activity in the amygdala nucleus in each group was recorded by extracellular electrophysiology. Neuropsin and serpinb6 protein expressions in the amygdala and stomach were detected by Western blot. Results AWR score in the FD group increased but did not differ after EA therapy than that in the contro group. Both the center square entries and center entries ratio in the FD group were lower than those in the control and FD + EA groups. The total number and frequency of amygdala nucleus discharges induced by gastric distension in the FD group were significantly higher than those in the control and FD + EA groups. Expression of neuropsin increased and that of serpinb6 decreased in the gastric mucosa and amygdale in the FD group, while no change was observed in gastric mucosa after EA therapy. Conclusion EA stimulation at the Zusanli acupoint may improve visceral hypersensitivity and anxiety in FD rats through the neuropsin/serpinb6 pathway.

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“…Tandem mass spectrometry analysis of the precipitates identified an unbiased, comprehensive collection of neuropsin substrates; neuregulin-1 (NRG-1), fibronectin and vitronectin, as well as known specific inhibitors; α 2-macroglobulin and neuroserpin. Interestingly, all S1 family trypsin-type proteases (clan SA) have an SS6 disulfide bond (Barret and Rawlings, 1995), therefore this may be the critical part in the formation of an enzyme-substrate intermediate complex (Kishi et al, 2002;Oka et al, 2002).…”

Section: Unbiased Search For Potential Substrates Of Neuropsinmentioning

confidence: 99%

Does extracellular proteolysis control mammalian cognition?

Tamura

Ishikawa

Shiosaka

2013

Reviews in the Neurosciences

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Distribution of serine proteinase inhibitor, clade B, member 6 (Serpinb6) in the adult mouse brain

Cited by 6 publications

References 14 publications

Targeted Disruption of SPI3/Serpinb6 Does Not Result in Developmental or Growth Defects, Leukocyte Dysfunction, or Susceptibility to Stroke

Targeted Disruption of SPI3/Serpinb6 Does Not Result in Developmental or Growth Defects, Leukocyte Dysfunction, or Susceptibility to Stroke

The role of amygdala neuropsin/serpinb6 pathway in the regulation of gastric hypersensitivity and anxiety by electroacupuncture

Does extracellular proteolysis control mammalian cognition?

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