Synthesis of plasma proteins in fetal, adult, and neoplastic human brain tissue

Dzięgielewska, Katarzyna M.; Saunders, NR; Schejter, Eduardo; Zakut, Haim; Zevin-Sonkin, Dina; Zisling, Rivka; Soreq, Hermona

doi:10.1016/0012-1606(86)90231-9

Cited by 77 publications

(35 citation statements)

References 29 publications

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“…Previous reports have, indeed, shown the presence of ␣2M in adult human brain (65,66), confirming our immunofluorescence results. The immunofluorescence signals localized to neuronal cell bodies and neurites in the CA1-CA3 subfields of the hippocampus (Fig.…”

Section: Discussionsupporting

confidence: 93%

Serine Proteinase Inhibitor 3 and Murinoglobulin I Are Potent Inhibitors of Neuropsin in Adult Mouse Brain

Kato

Kishi

Kamachi

et al. 2001

Journal of Biological Chemistry

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Extracellular serine protease neuropsin (NP) is expressed in the forebrain limbic area of adult brain and is implicated in synaptic plasticity. We screened for endogenous NP inhibitors with recombinant NP (r-NP) from extracts of the hippocampus and the cerebral cortex in adult mouse brain. Two SDS-stable complexes were detected, and after their purification, peptide sequences were determined by amino acid sequencing and mass spectrometry, revealing that target molecules were serine proteinase inhibitor-3 (SPI3) and murinoglobulin I (MUG I). The addition of the recombinant SPI3 to r-NP resulted in an SDS-stable complex, and the complex formation followed bimolecular kinetics with an association rate constant of 3.4 ؎ 0.22 ؋ 10 6 M ؊1 s ؊1, showing that SPI3 was a slow, tight binding inhibitor of NP. In situ hybridization histochemistry showed that SPI3 mRNA was expressed in pyramidal neurons in the hippocampal CA1-CA3 subfields, as was NP mRNA. Alternatively, the addition of purified plasma MUG I to r-NP resulted in an SDS-stable complex, and MUG I inhibited degradation of fibronectin by r-NP to 24% at a r-NP/MUG I molar ratio of 1:2. Immunofluorescence histochemistry showed that MUG I localized in the hippocampal neurons. These findings indicate that SPI3 and MUG I serve to inactivate NP and control the level of NP in adult brain, respectively. Extracellular proteolysis exerted by secretory serine proteases has been implicated in neural development, plasticity, and degeneration and regeneration in the nervous system (1) and might be controlled by specific inhibitors (2). Neuropsin (NP), 1 a serine protease with a chimeric structure similar to trypsin and nerve growth factor-␥ (3), was found to be expressed in the nervous system (4) and has been demonstrated to be engaged in activity-dependent plasticity changes in neurons. NP mRNA and protein levels increased in the hippocampus after kindled seizures and injection of antibody against NP led to retardation of epilepticus in mice (5, 6). Furthermore, application of recombinant NP induced an increase in the amplitude of the tetanic stimulation-induced early phase long term potentiation in the Schaffer collateral pathway (7). It has been proposed that the plasticity changes are regulated by the balance between the accumulation and degradation of the extracellular matrix (ECM) proteins. There is, indeed, some evidence that the formation of hippocampal LTP is attributable to cell-ECM interactions, involving cadherin (8), integrin (9, 10), N-syndecan (11), cell adhesion molecules, NCAM, and L1 (12)(13)(14). NP acted to degrade ECM including fibronectin (15), for which integrins were receptors (16, 17), and L1. 2 Therefore, rearrangement of these ECM components by NP and a specific inhibitor might implicated in the formation of LTP.As another characteristic of NP, it has been shown that NP mRNA was restricted to neurons in the limbic areas of adult brain involving the CA1-CA3 subfields of the hippocampus, the amygdaloid nucleus, the cingulate cortex, the anterior olfact...

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Section: Discussionsupporting

confidence: 93%

Serine Proteinase Inhibitor 3 and Murinoglobulin I Are Potent Inhibitors of Neuropsin in Adult Mouse Brain

Kato

Kishi

Kamachi

et al. 2001

Journal of Biological Chemistry

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“…It is also found within specific neurons in the brain and in the adrenal cortex. These findings are also in agreement with earlier immunochemical data concerning humans (50). The function of the AAT in these locations has not been determined.…”

Section: Discussionsupporting

confidence: 88%

Multiple tissues express alpha 1-antitrypsin in transgenic mice and man.

Carlson¹,

Rogers²,

Sifers³

et al. 1988

J. Clin. Invest.

150

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“…The function of a,M-R/LRP in normal brain is stall unknown, however, protemases, proteinase inhibitors and cytokmes are important effecters of ghal-neuronal cell interactions. Based on its ability to bmd diverse hgands (some of which are carriers of other macromole- [23] and m adult bram durmg subacute responses to mlury and chronic degenerative states [24,25], a,M may influence the traffickmg of TGF-P and PDGF between cells m the brain The ultimate delivery of a,M-TGF-j? or a,M-PDGF complex to a particular bram cell depends on expression of a,M-RILRP Disease processes which increase a,M-RILRP expression m ghal cells might facilitate ol,M-targetmg of TGF-/3 and PDGF to these cells Bmdmg of hgands to cx,M-RILRP results m receptor clustering m clathrm-coated pits and rapid clearance of the receptor-hgand complexes from the cell surface by endocytosls [26] The hgands are transferred to lysosomes while the a,M-RILRP typically recycles to the cell surface [27] Although all types of ghomas exhlblted a,M-RILRP immunoreactlvlty, the more mvaslve astrocytomas demonstrated a predommantly cytoplasmlc pattern of a,M-R/LRP stammg while the less mvaslve pllocytlc astrocytomas expressed a,M-RILRP primarily m cell processes Pllocytlc astrocytomas express high levels of protemase mhlbltors compared with other ghal cell neoplasms [28] Whether expression of protemase mhlb-…”

Section: Resultsmentioning

confidence: 99%

Expression of α₂‐macroglobulin receptor/low density lipoprotein receptor‐related protein is increased in reactive and neoplastic glial cells

et al. 1994

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a,-Macroglobuhn receptor/low density hpoprotem receptor-related protein (cc,M-RILRP) IS a multi-functional cell-surface receptor that has been tmphcated m diverse physiologic processes In normal human brain, a,M-R/LRP IS expressed prmclpally by pyramldal neurons with locahzation to cell bodies and proximal processes By contrast, a,M-R/LRP 1s not present m either the cell bodies or processes of most normal macrogha (mcludmg astrocytes) In this mvestlgatlon, we studied the expression of a,M-FULRP m the brain, followmg tissue InJury or neoplastic transformation, by lmmunohistochemlstry Significantly increased a,M-R/LRP lmmunoreactivlty was ldentlfied m reactive astrocytes, mdlcatmg that expression of this receptor is regulated m viva m response to brain injury a2M-R/LRP lmmunoreactivlty was also detected m ghal cell tumors. this finding 1s novel since malignant transformation 1s typically thought to turn off expression of this receptor

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Synthesis of plasma proteins in fetal, adult, and neoplastic human brain tissue

Cited by 77 publications

References 29 publications

Serine Proteinase Inhibitor 3 and Murinoglobulin I Are Potent Inhibitors of Neuropsin in Adult Mouse Brain

Serine Proteinase Inhibitor 3 and Murinoglobulin I Are Potent Inhibitors of Neuropsin in Adult Mouse Brain

Multiple tissues express alpha 1-antitrypsin in transgenic mice and man.

Expression of α₂‐macroglobulin receptor/low density lipoprotein receptor‐related protein is increased in reactive and neoplastic glial cells

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Synthesis of plasma proteins in fetal, adult, and neoplastic human brain tissue

Cited by 77 publications

References 29 publications

Serine Proteinase Inhibitor 3 and Murinoglobulin I Are Potent Inhibitors of Neuropsin in Adult Mouse Brain

Serine Proteinase Inhibitor 3 and Murinoglobulin I Are Potent Inhibitors of Neuropsin in Adult Mouse Brain

Multiple tissues express alpha 1-antitrypsin in transgenic mice and man.

Expression of α2‐macroglobulin receptor/low density lipoprotein receptor‐related protein is increased in reactive and neoplastic glial cells

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Expression of α₂‐macroglobulin receptor/low density lipoprotein receptor‐related protein is increased in reactive and neoplastic glial cells