Fib420 , the Novel Fibrinogen Subclass: Newborn Levels Are Higher Than Adult

Abstract Fib420 is a recently identified subclass of normal human fibrinogen in which two extended α chain isoforms (αE ) replace the common α chains, yielding a molecule (ca. 420 kD) which is larger than the more abundant 340-kD form. Evidence for preservation of this subclass throughout vertebrate evolution suggests it performs some as yet unidentified vital function. A survey was undertaken to establish the range of plasma Fib420 levels in normal, healthy adults and in placental cord (fetal) blood. For measuring Fib420 , a quantitative Western blot assay was developed using monoclonal antibody against the exon-VI encoded C-terminus of the molecule's unique αE chain. This αE chain signal was normalized to that of the β chain, common to both fibrinogen forms. Analysis of plasma samples from the adult and newborn cohorts (n = 25 each; total fibrinogen ca. 2.6 mg/mL in both) revealed a statistically significant difference, with a mean level of 100 ± 28 μg/mL in the neonate compared to 34 ± 7 μg/mL in the adult. On average, 1 out of every 100 fibrinogen molecules in adult plasma belongs to the Fib420 subclass. Unlike in the newborn, adult Fib420 levels remained the same over a wide range of total plasma fibrinogen. The striking difference observed between these two cohorts suggests a changing developmental expression of the Fib420 subclass and a homeostatic control operating in later stages of life.

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Fib420 , the Novel Fibrinogen Subclass: Newborn Levels Are Higher Than Adult

Blood ◽

10.1182/blood.v90.7.2609.2609_2609_2614 ◽

1997 ◽

Vol 90 (7) ◽

pp. 2609-2614 ◽

Cited By ~ 2

Author(s):

Gerd Grieninger ◽

Xianghan Lu ◽

Yan Cao ◽

Yiping Fu ◽

Bohdan J. Kudryk ◽

...

Keyword(s):

Developmental Expression ◽

Striking Difference ◽

The Novel ◽

Western Blot Assay ◽

Human Fibrinogen ◽

C Terminus ◽

Wide Range ◽

Significant Difference ◽

Adult Plasma ◽

Normal Human

Fib420 is a recently identified subclass of normal human fibrinogen in which two extended α chain isoforms (αE ) replace the common α chains, yielding a molecule (ca. 420 kD) which is larger than the more abundant 340-kD form. Evidence for preservation of this subclass throughout vertebrate evolution suggests it performs some as yet unidentified vital function. A survey was undertaken to establish the range of plasma Fib420 levels in normal, healthy adults and in placental cord (fetal) blood. For measuring Fib420 , a quantitative Western blot assay was developed using monoclonal antibody against the exon-VI encoded C-terminus of the molecule's unique αE chain. This αE chain signal was normalized to that of the β chain, common to both fibrinogen forms. Analysis of plasma samples from the adult and newborn cohorts (n = 25 each; total fibrinogen ca. 2.6 mg/mL in both) revealed a statistically significant difference, with a mean level of 100 ± 28 μg/mL in the neonate compared to 34 ± 7 μg/mL in the adult. On average, 1 out of every 100 fibrinogen molecules in adult plasma belongs to the Fib420 subclass. Unlike in the newborn, adult Fib420 levels remained the same over a wide range of total plasma fibrinogen. The striking difference observed between these two cohorts suggests a changing developmental expression of the Fib420 subclass and a homeostatic control operating in later stages of life.

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RNAi-mediated silencing of vitellogenin gene curtails oogenesis in the almond moth Cadra cautella

PLoS ONE ◽

10.1371/journal.pone.0245928 ◽

2021 ◽

Vol 16 (2) ◽

pp. e0245928

Author(s):

Mureed Husain ◽

Khawaja Ghulam Rasool ◽

Muhammad Tufail ◽

Waleed Saleh Alwaneen ◽

Abdulrahman Saad Aldawood

Keyword(s):

Amino Acids ◽

Expression Profiles ◽

Yolk Protein ◽

Developmental Expression ◽

Egg Hatchability ◽

Amino Terminal ◽

Cadra Cautella ◽

Type D ◽

C Terminus ◽

Significant Difference

Vitellogenins, major yolk protein precursors, play an essential role in the reproduction and spread of all oviparous species, including insects. To investigate reproductive strategies of the warehouse moth Cadra cautella at the molecular level, a partial transcript of the C. cautella vitellogenin (CcVg) gene was extended through the rapid amplification of cDNA ends PCR and sequenced. The complete CcVg mRNA transcript was 5,334 bp long, which encoded a protein of 1,778 amino acids, including the first 14 amino acids of the signal peptide. The deduced CcVg protein contained a putative cleavage site (RTRR) at the amino-terminal side, similar to several other insect species. DGQR and GI/LCG motifs were present at the CcVg gene C-terminus, followed by nine cysteine residues. CcVg harbored 131 putative phosphorylation sites, numbering 84, 19, and 28 sites for serine, threonine, and tyrosine, respectively. The transcript showed a great resemblance with other lepidopteran Vgs. CcVg protein analysis revealed three conserved regions: 1) vitellogenin-N domain, 2) DUF 1943 (domain of unknown function), and 3) a von Willebrand factor type D domain. Additionally, sex, stage-specific, and developmental expression profiles of the CcVg gene were determined through RT-PCR. The Vg was first expressed in 22-day-old female larvae, and its expression increased with growth. The phylogenetic analysis based on different insect Vgs revealed that the CcVg exhibited close ancestry with lepidopterans. The CcVg-based RNAi experiments were performed, and the effects were critically evaluated. The qRT-PCR results showed that CcVg-based dsRNA suppressed the Vg gene expression up to 90% at 48 h post-injection. Moreover, CcVg-based RNAi effects resulted in low fecundity and egg hatchability in the CcVg-based dsRNA-treated females. The females laid eggs, but because of insufficient yolk protein availability the eggs could not succeed to hatch. The significant difference in the fecundity and hatchability unveils the importance of CcVg gene silencing and confirmed that the Vg gene plays a key role in C. cautella reproduction and it has the potential to be used as a target for RNAi-mediated control of this warehouse pest.

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Clinical Study of the Novel Antiseptic Olanexidine Gluconate in Gastrointestinal Cancer Surgery

10.21203/rs.3.rs-396765/v1 ◽

2021 ◽

Author(s):

Naoki Kubo ◽

Norihiko Furusawa ◽

Daisuke Takeuchi ◽

Shinichiro Imai ◽

Hitoshi Masuo ◽

...

Keyword(s):

Retrospective Study ◽

Gastrointestinal Cancer ◽

Deep Infection ◽

Cancer Surgery ◽

Control Group ◽

The Novel ◽

Superficial Infection ◽

Digestive Surgery ◽

Wide Range ◽

Significant Difference

Abstract Background Surgical site infection (SSI) is a common complication of digestive surgery .Olanexidine gluconate (OLG) is a novel developed skin antiseptic and effective against a wide range of bacteria. The purpose of this study is to evaluate the bactericidal efficacy of OLG in gastrointestinal cancer surgery. Methods This retrospective study included a total of 281patients who underwent gastrointestinal cancer surgery (stomach or colon). There were two group: 223 patients were treated with OLG (OLG group), and 58 patients were treated with povidone-iodine (PVP-I) (control group). The efficacy and the safety outcomes were measured as the rate of surgical SSI within 30 days after surgery. In addition, we also conducted subgroups defined according to the surgical approach (open or laparoscopic) or primary lesion (stomach or colon). Results There was a significant difference in the rate of SSI between the control group and OLG group (10.3% vs. 2.7% ; p = 0.02). There was a significant difference in the SSI rate in superficial infection (8.6% vs. 2.2% ; p = 0.0345) but not in deep infection (1.7% vs. 0.5% ; p = 0.371). There was no significant difference between the control group and OLG group in the overall rate of adverse skin reaction (5.2% vs. 1.8% ; p = 0.157). Conclusion This retrospective study demonstrates that OLG is more effective than PVP-I for preventing SSI during gastrointestinal cancer surgery.

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Clinical Study of The Novel Antiseptic Olanexidine Gluconate in Gastrointestinal Cancer Surgery

10.21203/rs.3.rs-396765/v2 ◽

2021 ◽

Author(s):

Naoki Kubo ◽

Norihiko Furusawa ◽

Daisuke Takeuchi ◽

Shinichiro Imai ◽

Hitoshi Masuo ◽

...

Keyword(s):

Retrospective Study ◽

Gastrointestinal Cancer ◽

Deep Infection ◽

Cancer Surgery ◽

Control Group ◽

The Novel ◽

Superficial Infection ◽

Digestive Surgery ◽

Wide Range ◽

Significant Difference

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Formation of the Human Fibrinogen Subclass Fib420: Disulfide Bonds and Glycosylation in Its Unique (EChain) Domains

Blood ◽

10.1182/blood.v92.9.3302.421k48_3302_3308 ◽

1998 ◽

Vol 92 (9) ◽

pp. 3302-3308 ◽

Cited By ~ 2

Author(s):

Yiping Fu ◽

Jian-Zhong Zhang ◽

Colvin M. Redman ◽

Gerd Grieninger

Keyword(s):

Disulfide Bonds ◽

Cell Transfection ◽

The Novel ◽

Disulfide Bridges ◽

Human Fibrinogen ◽

Cos Cells ◽

C Terminus ◽

Symmetrical Molecule ◽

American Society

COS cell transfection has been used to monitor the assembly and secretion of fibrinogen molecules, both those of the subclass containing the novel E chain and those of the more abundant subclass whose  chains lack E’s globular C-terminus. That region, referred to as the EC domain, is closely related to the ends of β and γ chains of fibrinogen (βC and γC). Transfection of COS cells with E, β, and γ cDNAs alone results in secretion of the symmetrical molecule (Eβγ)2, also known as Fib420. Cotransfection with cDNA for the shorter  chain yielded secretion of both (βγ)2 and (Eβγ)2 but no mixed molecules of the structure E(βγ)2. Exploiting the COS cells’ fidelity with regard to Fib420 production, identification was made of the highly conserved Asn667 as the sole site of N-linked glycosylation in the E chain. No evidence from Cys → Ser replacements was found for interchain disulfide bridges involving the four cysteines of the EC domain. However, for fibrinogen secretion, the E, β, and γ subunits do exhibit different requirements for integrity of the two intradomain disulfide bridges located at homologous positions in their respective C-termini, indicating dissimilar structural roles in the process of fibrinogen assembly. © 1998 by The American Society of Hematology.

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Formation of the Human Fibrinogen Subclass Fib420: Disulfide Bonds and Glycosylation in Its Unique (EChain) Domains

Blood ◽

10.1182/blood.v92.9.3302 ◽

1998 ◽

Vol 92 (9) ◽

pp. 3302-3308 ◽

Cited By ~ 13

Author(s):

Yiping Fu ◽

Jian-Zhong Zhang ◽

Colvin M. Redman ◽

Gerd Grieninger

Keyword(s):

Disulfide Bonds ◽

Cell Transfection ◽

The Novel ◽

Disulfide Bridges ◽

Human Fibrinogen ◽

Cos Cells ◽

C Terminus ◽

Symmetrical Molecule ◽

American Society

Abstract COS cell transfection has been used to monitor the assembly and secretion of fibrinogen molecules, both those of the subclass containing the novel E chain and those of the more abundant subclass whose  chains lack E’s globular C-terminus. That region, referred to as the EC domain, is closely related to the ends of β and γ chains of fibrinogen (βC and γC). Transfection of COS cells with E, β, and γ cDNAs alone results in secretion of the symmetrical molecule (Eβγ)2, also known as Fib420. Cotransfection with cDNA for the shorter  chain yielded secretion of both (βγ)2 and (Eβγ)2 but no mixed molecules of the structure E(βγ)2. Exploiting the COS cells’ fidelity with regard to Fib420 production, identification was made of the highly conserved Asn667 as the sole site of N-linked glycosylation in the E chain. No evidence from Cys → Ser replacements was found for interchain disulfide bridges involving the four cysteines of the EC domain. However, for fibrinogen secretion, the E, β, and γ subunits do exhibit different requirements for integrity of the two intradomain disulfide bridges located at homologous positions in their respective C-termini, indicating dissimilar structural roles in the process of fibrinogen assembly. © 1998 by The American Society of Hematology.

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IMMUNOLOGICAL REACTIVITY OF INSULIN IN HUMAN SERUM

Acta Endocrinologica ◽

10.1530/acta.0.0530673 ◽

1966 ◽

Vol 53 (4) ◽

pp. 673-680 ◽

Cited By ~ 5

Author(s):

Torsten Deckert ◽

Kai R. Jorgensen

Keyword(s):

Normal Subjects ◽

The Other ◽

Human Pancreas ◽

Porcine Pancreas ◽

Crystalline Insulin ◽

Endogenous Insulin ◽

Significant Difference ◽

Human Sera ◽

Normal Human ◽

The One

ABSTRACT The purpose of this study was to investigate whether a difference could be demonstrated between crystalline insulin extracted from normal human pancreas, and crystalline insulin extracted from bovine and porcine pancreas. Using Hales & Randle's (1963) immunoassay no immunological differences could be demonstrated between human and pig insulin. On the other hand, a significant difference was found, between pig and ox insulin. An attempt was also made to determine whether an immunological difference could be demonstrated between crystalline pig insulin and crystalline human insulin from non diabetic subjects on the one hand and endogenous, circulating insulin from normal subjects, obese subjects and diabetic subjects on the other. No such difference was found. From these experiments it is concluded that endogenous insulin in normal, obese and diabetic human sera is immunologically identical with human, crystalline insulin from non diabetic subjects and crystalline pig insulin.

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Reading Beyond the Code

10.1093/oso/9780198794776.001.0001 ◽

2018 ◽

Cited By ~ 6

Keyword(s):

Relevance Theory ◽

Literary Studies ◽

The Novel ◽

Human Communication ◽

Communicative Acts ◽

Face To Face ◽

Code Model ◽

Wide Range ◽

Central Claim

This book explores the value for literary studies of relevance theory, an inferential approach to communication in which the expression and recognition of intentions plays a major role. Drawing on a wide range of examples from lyric poetry and the novel, nine of the ten chapters are written by literary specialists and use relevance theory both as an overall framework and as a resource for detailed analysis. The final chapter, written by the co-founder of relevance theory, reviews the issues addressed by the volume and explores their implications for cognitive theories of how communicative acts are interpreted in context. Originally designed to explain how people understand each other in everyday face-to-face exchanges, relevance theory—described in an early review by a literary scholar as ‘the makings of a radically new theory of communication, the first since Aristotle’s’—sheds light on the whole spectrum of human modes of communication, including literature in the broadest sense. Reading Beyond the Code is unique in using relevance theory as a prime resource for literary study, and is also the first to apply the model to a range of phenomena widely seen as supporting an ‘embodied’ conception of cognition and language where sensorimotor processes play a key role. This broadened perspective serves to enhance the value for literary studies of the central claim of relevance theory: that the ‘code model’ is fundamentally inadequate to account for human communication, and in particular for the modes of communication that are proper to literature.

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Biochemical and molecular characterization of Alternaria alternata isolates highly resistant to procymidone from broccoli and cabbage

Phytopathology Research ◽

10.1186/s42483-021-00092-z ◽

2021 ◽

Vol 3 (1) ◽

Author(s):

Bingran Wang ◽

Tiancheng Lou ◽

Lingling Wei ◽

Wenchan Chen ◽

Longbing Huang ◽

...

Keyword(s):

Alternaria Alternata ◽

Single Point ◽

Sodium Dodecyl ◽

Cross Resistance ◽

Molecular Characteristics ◽

Single Point Mutation ◽

Wide Range ◽

Significant Difference ◽

Leaf Blights ◽

High Level

AbstractAlternaria alternata, a causal agent of leaf blights and spots on a wide range of hosts, has a high risk of developing resistance to fungicides. Procymidone, a dicarboximide fungicide (DCF), has been widely used in controlling Alternaria leaf blights in China for decades. However, the resistance of A. alternata against DCFs has rarely been reported from crucifer plants. A total of 198 A. alternata isolates were collected from commercial fields of broccoli and cabbage during 2018–2019, and their sensitivities to procymidone were determined. Biochemical and molecular characteristics were subsequently compared between the high-level procymidone-resistant (ProHR) and procymidone-sensitive (ProS) isolates, and also between ProHR isolates from broccoli and cabbage. Compared with ProS isolates, the mycelial growth rate, sporulation capacity and virulence of most ProHR isolates were reduced; ProHR isolates displayed an increased sensitivity to osmotic stresses and a reduced sensitivity to sodium dodecyl sulfate (SDS); all ProHR isolates showed a reduced sensitivity to hydrogen peroxide (H2O2) except for the isolate B102. Correlation analysis revealed a positive cross-resistance between procymidone and iprodione, or fludioxonil. When treated with 10 μg/mL of procymidone, both mycelial intracellular glycerol accumulations (MIGAs) and relative expression of AaHK1 in ProS isolates were higher than those in ProHR isolates. Sequence alignment of AaHK1 from ten ProHR isolates demonstrated that five of them possessed a single-point mutation (P94A, V612L, E708K or Q924STOP), and four isolates had an insertion or a deletion in their coding regions. No significant difference in biochemical characteristics was observed among ProHR isolates from two different hosts, though mutations in AaHK1 of the cabbage-originated ProHR isolates were distinct from those of the broccoli-originated ProHR isolates.

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Comparative Study for the Assay of Plant Derived Chemicals in Pharmaceutical Formulation Using Methods Dependent on Factorized Spectra

Journal of AOAC International ◽

10.1093/jaoacint/qsab027 ◽

2021 ◽

Author(s):

Nesma M Fahmy ◽

Adel M Michael

Keyword(s):

Pharmaceutical Formulations ◽

Pharmaceutical Formulation ◽

Ternary Mixtures ◽

Ratio Method ◽

The Novel ◽

Naturally Occurring ◽

Accuracy And Precision ◽

Validation Parameters ◽

Significant Difference

Abstract Background Modern built-in spectrophotometer software supporting mathematical processes provided a solution for increasing selectivity for multicomponent mixtures. Objective Simultaneous spectrophotometric determination of the three naturally occurring antioxidants—rutin(RUT), hesperidin(HES), and ascorbic acid(ASC)—in bulk forms and combined pharmaceutical formulation. Method This was achieved by factorized zero order method (FZM), factorized derivative method (FD1M), and factorized derivative ratio method (FDRM), coupled with spectrum subtraction(SS). Results Mathematical filtration techniques allowed each component to be obtained separately in either its zero, first, or derivative ratio form, allowing the resolution of spectra typical to the pure components present in Vitamin C Forte® tablets. The proposed methods were applied over a concentration range of 2–50, 2–30, and 10–100 µg/mL for RUT, HES, and ASC, respectively. Conclusions Recent methods for the analysis of binary mixtures, FZM and FD1M, were successfully applied for the analysis of ternary mixtures and compared to the novel FDRM. All were revealed to be specific and sensitive with successful application on pharmaceutical formulations. Validation parameters were evaluated in accordance with the International Conference on Harmonization guidelines. Statistical results were satisfactory, revealing no significant difference regarding accuracy and precision. Highlights Factorized methods enabled the resolution of spectra identical to those of pure drugs present in mixtures. Overlapped spectra of ternary mixtures could be resolved by spectrum subtraction coupled FDRM (SS-FDRM) or by successive application of FZM and FD1M.

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