Polymerized and polyethylene glycol-conjugated hemoglobins: A globin-based calibration curve for dynamic light scattering analysis

Faggiano, Serena; Ronda, Luca; Bruno, Stefano; Jankevics, Hanna; Mozzarelli, Andrea

doi:10.1016/j.ab.2010.02.025

Cited by 5 publications

(3 citation statements)

References 36 publications

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“…5D ). Using the Mark-Houwink-Sakurada equation, molecular weight = a(D H ) b , where parameters a and b were found to be 0.41 ± 0.05 and 2.48 ± 0.04, respectively, for proteins in the range of 17–440 kD 32 , the corresponding molecular weights deduced from these D H values are 93 ± 6 kD, 32 ± 2 kD and 28 ± 1 kD, for CT, CT-ΔC1 and CT-Δdouble, respectively, indicating a predominant trimeric structure for CT and monomeric structures for the two deletion mutants under this experimental condition. These data indicated that C1 deletion significantly breaks down trimerization of CT, in support of the importance of C1 for oligomerization.…”

Section: Resultsmentioning

confidence: 99%

A novel PKD2L1 C-terminal domain critical for trimerization and channel function

Zheng

Hussein

Yang

et al. 2015

Sci Rep

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As a transient receptor potential (TRP) superfamily member, polycystic kidney disease 2-like-1 (PKD2L1) is also called TRPP3 and has similar membrane topology as voltage-gated cation channels. PKD2L1 is involved in hedgehog signaling, intestinal development, and sour tasting. PKD2L1 and PKD1L3 form heterotetramers with 3:1 stoichiometry. C-terminal coiled-coil-2 (CC2) domain (G699-W743) of PKD2L1 was reported to be important for its trimerization but independent studies showed that CC2 does not affect PKD2L1 channel function. It thus remains unclear how PKD2L1 proteins oligomerize into a functional channel. By SDS-PAGE, blue native PAGE and mutagenesis we here identified a novel C-terminal domain called C1 (K575-T622) involved in stronger homotrimerization than the non-overlapping CC2, and found that the PKD2L1 N-terminus is critical for dimerization. By electrophysiology and Xenopus oocyte expression, we found that C1, but not CC2, is critical for PKD2L1 channel function. Our co-immunoprecipitation and dynamic light scattering experiments further supported involvement of C1 in trimerization. Further, C1 acted as a blocking peptide that inhibits PKD2L1 trimerization as well as PKD2L1 and PKD2L1/PKD1L3 channel function. Thus, our study identified C1 as the first PKD2L1 domain essential for both PKD2L1 trimerization and channel function, and suggest that PKD2L1 and PKD2L1/PKD1L3 channels share the PKD2L1 trimerization process.

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Section: Resultsmentioning

confidence: 99%

A novel PKD2L1 C-terminal domain critical for trimerization and channel function

Zheng

Hussein

Yang

et al. 2015

Sci Rep

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“…Heart and kidney tissue samples were obtained from 14 Hartley Guinea pigs that underwent either autotransfusion or transfusion with PEG-Hb oxy or PEG-Hb deoxy , two PEGylated hemoglobin-based oxygen carriers [1] , [2] , [3] , [4] , [5] , [6] endowed with different oxygen affinity [2] , as described in FRBM [11] . The aim of the work was to assess the degree of oxidative stress in the treatment groups in comparison with the control (autotransfused) group by determining the level of carbonylated proteins.…”

Section: Experimental Design Materials and Methodsmentioning

confidence: 99%

Protein carbonylation detection methods: A comparison

et al. 2018

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The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11]). We measured the carbonyl content of organ extracts by using i) the Levine spectrophotometric method, which takes advantage of the chromogenic reaction of carbonyl groups with 2,4-dinitrophenylhydrazine (DNPH), ii) a commercially available ELISA assay based on an anti-DNPH antibodies, iii) a commercially available Western blot method based on anti-DNPH antibodies and iv) an in-gel detection approach with the fluorophoric reagent fluorescein-5-thiosemicarbazide. The former two methods measure total protein carbonylation of a sample, whereas the latter two require an electrophoretic separation and therefore potentially allow for the identification of specific carbonylated proteins.

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“…Designing low oxygen affinity blood substitutes with enhanced molecular size (dimensions) has been initially attempted by one-step oligomerization platform that introduces intra and intermolecular crosslinking using glutaraldehyde. Chang introduced the oligomerization concept (Chang 1964(Chang , 1971, and since then many new bifunctional crosslinkers have been advanced for the oligomerization of Hb (Bunn et al 1969;Payne 1973;Marini et al 1989;D'Agnillo and Chang 1998;Hai et al 1999;MacDonald and Pepper 1994;Hai et al 1994;Bakker et al 1992;Dellacherie and Vigneron 1991;Zhang and Palmer 2010;Faggiano et al 2010;Tarasov et al 2007;Buehler et al 2006;Scurtu et al 2013;Berbers et al 1991;Adachi et al 1991).…”

Section: Enhancing the Molecular Dimensions Of Hb By Oligomerizationmentioning

confidence: 99%

Design of Nonhypertensive Conjugated Hemoglobins as Novel Resuscitation Fluids

Acharya

Intaglietta

Tsai

et al. 2013

Hemoglobin-Based Oxygen Carriers as Red Cell Substitutes and Oxygen Therapeutics

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Polymerized and polyethylene glycol-conjugated hemoglobins: A globin-based calibration curve for dynamic light scattering analysis

Cited by 5 publications

References 36 publications

A novel PKD2L1 C-terminal domain critical for trimerization and channel function

A novel PKD2L1 C-terminal domain critical for trimerization and channel function

Protein carbonylation detection methods: A comparison

Design of Nonhypertensive Conjugated Hemoglobins as Novel Resuscitation Fluids

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