Proteins of rat serum IV. Time-course of acute-phase protein expression and its modulation by indomethacine

Eberini, Ivano; Miller, Ingrid; Zancan, Valeria; Bolego, Chiara; Puglisi, L.; Gemeiner, Manfred; Gianazza, Elisabetta

doi:10.1002/(sici)1522-2683(19990101)20:4/5<846::aid-elps846>3.0.co;2-2

Cited by 25 publications

(15 citation statements)

References 49 publications

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“…Subsequently applying our results to pharmacological testing, we were able to define the presence, intensity and detailed pattern of an inflammatory condition in several animal models [4][5][6]. Some of the latter investigations require analysis of samples from rat strains other than Sprague-Dawley, and from additional biological fluids.…”

Section: Introductionsupporting

confidence: 80%

“…Most analytical procedures were as previously described [1,2,4,5,8]. 2-DE maps were obtained by IPG-DALT [9].…”

Section: Electrophoretic Techniquesmentioning

confidence: 99%

“…[26], provides no information of the possible influence of ethnic origin, although data are subdivided by gender and age. An extensive survey on minor protein components in human serum has been undertaken by Leigh Anderson et al (oral communication at 4th Siena Meeting "From Genome to Proteome: Knowledge Acquisition and Representation", Sept. [4][5][6][7]2000). When testing over a larger genetic distance (Mus musculus and Mus spretus vs. two strains), Klose and co-workers detected more than 1000 variant protein spots (in brain, heart, and skeletal muscle) between the two subspecies [27,28].…”

Section: Interstrain Variationmentioning

confidence: 99%

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Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison

et al. 2001

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We have investigated the biological fluids--serum, cerebrospinal fluid, and urine--of three strains of rats; the present data extend our database (also available on-line) and may be of interest for pharmacological and toxicological investigation. Specifically, we have defined reference maps of the major protein components in cerebrospinal fluid and urine. Compartment-specific isoforms were recognized for transferrin and transthyretin. Mass spectrometric data established the cleavage site of the signal peptide and identified the N-terminal blocking group of prostaglandin D synthase from rat cerebrospinal fluid. A previously undescribed member of the family of low molecular mass rat urinary proteins was characterized as containing a sequence similar, but not identical, to the N-terminal region of rat urinary protein-2 (RUP-2), and divergent from RUP-1.

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Section: Introductionsupporting

confidence: 80%

“…Most analytical procedures were as previously described [1,2,4,5,8]. 2-DE maps were obtained by IPG-DALT [9].…”

Section: Electrophoretic Techniquesmentioning

confidence: 99%

Section: Interstrain Variationmentioning

confidence: 99%

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Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison

et al. 2001

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“…At least two different groups examined the effects of nonsteroidal anti-inflammatory drugs (NSAID) on the serum proteome of a rodent inflammation model [29,30]. Eberini et al [29] compared the abundance of serum proteins in an inflamed rodent to one treated with indomethacin and a typical serum protein expression profile for NSAID was developed that includes a 2 -macroglobulin, a 2 -HS-glycoprotein, C-reactive protein, and kallikrein-binding protein.…”

Section: Signature Patterns Related To Drug Toxicity and Efficacymentioning

confidence: 99%

“…Eberini et al [29] compared the abundance of serum proteins in an inflamed rodent to one treated with indomethacin and a typical serum protein expression profile for NSAID was developed that includes a 2 -macroglobulin, a 2 -HS-glycoprotein, C-reactive protein, and kallikrein-binding protein.…”

Section: Signature Patterns Related To Drug Toxicity and Efficacymentioning

confidence: 99%

Proteomics: Applications and opportunities in preclinical drug development

Steiner

Witzmann

2000

Electrophoresis

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Advances in DNA sequencing and the near-term availability of whole genome sequences for several pharmaceutically relevant organisms promise to dramatically alter the breadth and scale of high-throughput proteomic studies. The substantial amount of literature is available in the public domain, demonstrate the potential of proteomics in the preclinical phases of pharmaceutical development. Over the next few years, it is anticipated that functional genomics and proteomics will have major impacts on the clinical phases of drug development. Expected benefits are earlier proof-of-concept studies in man and increased efficiency of clinical trials through the availability of biologically relevant markers for drug efficacy and safety.

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Proteins of rat serum: III. Gender-related differences in protein concentration under baseline conditions and upon experimental inflammation as evaluated by two-dimensional electrophoresis

et al. 1999

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Proteins of rat serum IV. Time-course of acute-phase protein expression and its modulation by indomethacine

Cited by 25 publications

References 49 publications

Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison

Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison

Proteomics: Applications and opportunities in preclinical drug development

Proteins of rat serum: III. Gender-related differences in protein concentration under baseline conditions and upon experimental inflammation as evaluated by two-dimensional electrophoresis

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