THE RAT INTERLEUKIN 10 RECEPTOR: CLONING AND SEQUENCING OF cDNA CODING FOR THE ALPHA-CHAIN PROTEIN SEQUENCE, AND DEMONSTRATION BY WESTERN BLOTTING OF EXPRESSION IN THE RAT BRAIN

Abstract Objective: To explore the effects of hypoxic at different altitude and duration on the expression of HIF-1α in the rat tissues. Methods: A total of 72 Wistar rats were randomly divided into 6 groups (n=12 in each group): normoxic group and 5 experimental groups. Normoxia group was placed in the normal circumstances of Lanzhou (1500 m altitude), rats in the experimental groups were exposed to hypoxia in the hypobaric hypoxic animal experiment chamber simulating the altitudes of 3000, 4500, 6000, 7500, and 8000 m for 12 h, respectively. HE staining was conducted to observe the pathological changes of hippocampus tissues and the expression of HIF-1α in the rat brain, lung and heart tissues under the condition of hypoxia was detected by RT-PCR and Western Blotting. A total of 72 Wistar rats were randomly divided into 6 groups (n =12 in each group): normoxic group and 5 experimental groups. Rats in the experimental groups were exposed to hypoxia in the hypobaric hypoxic animal experiment chamber simulating the altitudes of 7500 m for 6, 12, 24, 36 and 72 h, respectively. Detect the same indicator after dissection. Results: We demonstrated that with the increased of hypoxia altitude and prolonged hypoxia, the expression of HIF-1α in the rat showed rising tendency (P<0.05) and the severe damage was revealed by pathological biopsy. Conclusion: We conclude that the expression of HIF1α in the rat was enslaved to the different altitude and duration of altitude hypoxia exposure.

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Hypophysectomy Enhances Interleukin-1beta, Tumor Necrosis Factor-alpha, and Interleukin-10 mRNA Expression in the Rat Brain

Journal of Interferon & Cytokine Research ◽

10.1089/107999099313712 ◽

1999 ◽

Vol 19 (6) ◽

pp. 583-587 ◽

Cited By ~ 8

Author(s):

Maha Mustafa ◽

Amged Mustafa ◽

Fred Nyberg ◽

Halinder Mangat ◽

Adlan Elhassan ◽

...

Keyword(s):

Tumor Necrosis Factor ◽

Mrna Expression ◽

Rat Brain ◽

Tumor Necrosis Factor Alpha ◽

Tumor Necrosis ◽

Interleukin 10 ◽

Necrosis Factor Alpha ◽

Factor Alpha ◽

Interleukin 1Beta ◽

Necrosis Factor

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A Novel CTX-M β-Lactamase (CTX-M-8) in Cefotaxime-ResistantEnterobacteriaceae Isolated in Brazil

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.44.7.1936-1942.2000 ◽

2000 ◽

Vol 44 (7) ◽

pp. 1936-1942 ◽

Cited By ~ 126

Author(s):

R. Bonnet ◽

J. L. M. Sampaio ◽

R. Labia ◽

C. De Champs ◽

D. Sirot ◽

...

Keyword(s):

Protein Sequence ◽

Clinical Laboratory ◽

Enterobacter Aerogenes ◽

Enterobacter Cloacae ◽

Cloning And Sequencing ◽

E Coli ◽

Class A ◽

The Family ◽

Synergy Test ◽

Citrobacter Amalonaticus

ABSTRACT To estimate the diversity of extended-spectrum β-lactamases in Brazil, 18 strains from different species of the familyEnterobacteriaceae exhibiting a positive double-disk synergy test were collected by a clinical laboratory from several hospitals in Rio de Janeiro, Brazil, in 1996 and 1997. Four strains (Proteus mirabilis, Enterobacter cloacae,Enterobacter aerogenes, and Citrobacter amalonaticus) hybridized with a 550-bp CTX-M probe. The P. mirabilis strain produced a CTX-M-2 enzyme. The E. cloacae, E. aerogenes, and C. amalonaticus isolates harbored a bla gene which was identified by cloning and sequencing as abla CTX-M gene. E. coli HB101 transconjugants and the E. coli DH5α transformant harboring a recombinant plasmid produced a CTX-M β-lactamase with an isoelectric point of 7.6 conferring a resistance phenotype characterized by a higher level of resistance to cefotaxime than to ceftazidime, as observed with the other CTX-M enzymes. The deduced protein sequence showed a novel Ambler class A CTX-M enzyme, named CTX-M-8, which had 83 to 88% identity with the previously described CTX-M enzymes. The phylogenic study of the CTX-M family including CTX-M-8 revealed four CTX-M types, CTX-M-8 being the first member of a new phylum of CTX-M enzymes. The evolutionary distances between the four types of CTX-M were large, suggesting that the four clusters branched off early from a distant unknown enzyme and that intermediate enzymes probably existed.

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Cloning and expression of cDNAs for the alpha subunit of the murine lymphocyte-Peyer's patch adhesion molecule.

The Journal of Cell Biology ◽

10.1083/jcb.115.4.1149 ◽

1991 ◽

Vol 115 (4) ◽

pp. 1149-1158 ◽

Cited By ~ 40

Author(s):

H Neuhaus ◽

M C Hu ◽

M E Hemler ◽

Y Takada ◽

B Holzmann ◽

...

Keyword(s):

Amino Acids ◽

Adhesion Molecule ◽

Protein Sequence ◽

Cleavage Site ◽

Cloning And Expression ◽

Cdna Clones ◽

Peyer’S Patch ◽

Peyer's Patch ◽

Alpha Chain ◽

Murine Lymphocyte

cDNA clones encoding the alpha chain of the murine lymphocyte-Peyer's patch adhesion molecule (LPAM), which is associated with lymphocyte homing, have been isolated by screening with the human VLA-4 (alpha 4h) probe. Several alpha 4 antigenic determinants were identified on COS-7 cells after transfection. From overlapping clones, approximately 5 kb of contiguous nucleotide sequence have been determined, encoding a protein sequence of 1039 amino acids for the LPAM alpha chain (alpha 4m). LPAM is a member of the integrin family of cell-surface heterodimers, and alpha 4m is the murine homologue of the human alpha 4 h chain. The two proteins have a total sequence similarity of 84%, with an almost perfect conservation (31/32 amino acids) in the cytoplasmic domain. Like alpha 4h, alpha 4m is distinct from other integrin alpha chains because it has neither an I-domain nor a COOH-terminal cleavage site. The positions of the characteristic Cysteine residues are conserved, and a putative protease cleavage site is located near the middle of the protein sequence. The NH2-terminal part of the protein contains seven homologous repeats, and three of them include putative divalent cation-binding sites. These sites are among the most conserved between the alpha 4m sequence and other alpha chains, and may therefore be involved in the binding of integrin alpha and beta chains. An additional cDNA clone was isolated which shares a sequence of perfect homology with the alpha 4m encoding cDNAs, but has a unique 3' poly-A end. This observation correlates with the fact that three discrete murine RNA bands are observed in Northern blot experiments using alpha 4m as a probe, whereas only two human RNA species are described for alpha 4h, indicating a higher complexity for murine than for human sequences.

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Interleukin-10 and Interleukin refeceptor-I Are Upregulated in Glial Cells After an Excitotoxic Injury to the Postnatal Rat Brain

Journal of Neuropathology & Experimental Neurology ◽

10.1097/nen.0b013e31819dca30 ◽

2009 ◽

Vol 68 (4) ◽

pp. 391-403 ◽

Cited By ~ 32

Author(s):

Pau Gonzalez ◽

Ferran Burgaya ◽

Laia Acarin ◽

Hugo Peluffo ◽

Bernardo Castellano ◽

...

Keyword(s):

Rat Brain ◽

Glial Cells ◽

Interleukin 10 ◽

Excitotoxic Injury

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The cloning and sequencing of cervine interleukin 10

DNA Sequence ◽

10.3109/10425179509030978 ◽

1995 ◽

Vol 5 (5) ◽

pp. 265-268 ◽

Cited By ~ 3

Author(s):

Euan Lockhart ◽

Lynn Slobbe ◽

Louis Droogmans ◽

Frank Griffin ◽

Glenn Buchan

Keyword(s):

Interleukin 10 ◽

Cloning And Sequencing

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Immunochemical and Biochemical Evidence for Expression of Phenobarbital-and 3-Methylcholanthrene-Inducible Isoenzymes of Cytochrome P450 in Rat Brain

International Journal of Toxicology ◽

10.1080/109158198225883 ◽

1998 ◽

Vol 17 (6) ◽

pp. 619-630 ◽

Cited By ~ 17

Author(s):

Devendra Parmar ◽

Alok Dhawan ◽

Monika Dayal ◽

Prahlad K. Seth

Keyword(s):

Cytochrome P450 ◽

Rat Brain ◽

Western Blotting ◽

Polyclonal Antibodies ◽

Biochemical Evidence ◽

Catalytic Activities ◽

Brain Microsomes ◽

The Brain

Expression of P450 1A1l 1A2 and 2 B1l 2B2 isoenzymes in rat brain was studied by Western blotting, using polyclonal antibodies raised against hepatic P450 1A1l 1A2 and 2B1l 2B2 isoenzymes. In addition, biochemical characterizations of the catalytic activities, pen toxyresorufin O-dealkylation (PROD) and ethoxyre-sorufin O-deethylation (EROD), selective for P450 2B1l 2B2 (PROD) and P450 1A1l 1A2 (EROD), were performed with rat brain microsomes. Control rat brain microsomes did not crossreact with either of the antibodies, whereas microsomes obtained from 3-methylcholanthrene (MC)-pretreated rats revealed significant immunoreactivity with anti-P450 1A1l 1A2. Similar results were observed with phenobarbital (PB)-pretreated rats, with the brain microsomes exhibiting significant immunoreactivity with anti-P450 2B1l 2B2. The induction in the P450 isoenzymes after PB or MC pretreatment was much less in the brain in comparison to the liver. Enzymatic studies indicated that the activities of PROD and EROD were induced in brain 3—4 fold by PB and MC pretreatment, respectively, and were almost completely inhibited on in vitro addition of anti-P450 2B1l 2B2 and 1A1l 1A2. These data demonstrate the expression of P4501A1l 1A2 and 2B1l 2B2 isoenzymes in the brain and indicate that, as in liver, these isoenzymes catalyze EROD and PROD, respectively, in the rat brain.

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Neuroprotective effects of pomegranate (Punica granatum L.) juice and seed extract in paraquat-induced mouse model of Parkinson’s disease

BMC Complementary Medicine and Therapies ◽

10.1186/s12906-021-03298-y ◽

2021 ◽

Vol 21 (1) ◽

Author(s):

Samah M. Fathy ◽

Heba A. El-Dash ◽

Noha I. Said

Keyword(s):

Gene Expression ◽

Dna Fragmentation ◽

Western Blotting ◽

Transforming Growth Factor ◽

Interleukin 10 ◽

Seed Extract ◽

Enzyme Linked Immunosorbent Assay ◽

Antioxidant Enzyme Activities ◽

Protective Effects ◽

Neuroprotective Effects

Abstract Background Paraquat, (PQ), an herbicide that can induce Parkinsonian-like symptoms in rodents and humans. The consumption of phytochemical-rich plants can reduce the risk of chronic illnesses such as inflammation and neurodegenerative diseases. The present study aimed to investigate the protective effects of pomegranate seed extract (PSE) and juice (PJ) against PQ-induced neurotoxicity in mice. Methods Mice were assigned into 4 groups; three groups received PQ (10 mg/kg, i.p.) twice a week for 3 weeks. Two of the PQ-induced groups pretreated with either PSE or PJ. Detection of phytochemicals, total phenolics, and total flavonoids in PSE and PJ was performed. Tyrosine hydroxylase (TH) level was measured in the substantia nigra (SN) by Western blotting technique. Striatal dopamine (DA) and 3,4-dihydroxyphenylacetic acid (DOPAC) were detected using high-performance liquid chromatography (HPLC). The levels of adenosine triphosphate (ATP), malondialdehyde (MDA), and the activity of the antioxidant enzymes were estimated in the striatum by colorimetric analysis. Striatal pro-inflammatory and anti-inflammatory markers using enzyme-linked immunosorbent assay (ELISA) as well as DNA fragmentation degree by qualitative DNA fragmentation assay, were evaluated. Real-time polymerase chain reaction (qPCR) assay was performed for the detection of nuclear factor kappa B (NF-кB) gene expression. Moreover, Western blotting analysis was used for the estimation of the cluster of differentiation 11b (CD11b), transforming growth factor β (TGF-β), and glial cell-derived neurotrophic factor (GDNF) levels in the striatum. Results Pretreatment with PSE or PJ increased the levels of TH in the SN as well as DA and its metabolite in the striatum that were reduced by PQ injection. PSE and PJ preadministration improved the PQ-induced oxidative stress via a significant reduction of the MDA level and the augmentation of antioxidant enzyme activities. PSE and PJ also significantly downregulated the striatal NF-кB gene expression, reduced the PQ-enhanced apoptosis, decreased the levels of; pro-inflammatory cytokines, CD11b, and TGF-β coupled with a significant increase of; interleukin-10 (IL-10), GDNF, and ATP levels as compared with PQ-treated mice. Conclusions The current study indicated that PSE and PJ consumption may exhibit protective effects against PQ-induced neurotoxicity in mice.

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