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Biomedical subjects

J Baranowski

Publications and source records attributed to J Baranowski.

48 records · Page 3Linked to original sources
PubMed1988

Plasma fibronectin concentrations in breast fed and formula fed neonates.

Plasma fibronectin concentration was measured in neonates of 2 to 5 days of age. Although breast fed and formula fed infants were similar in demographic characteristics, the mean (SD) plasma concentration of fibronectin in 26 breast fed infants, 237 (117) mg/l, was significantly higher than in 27 formula fed infants (171 (91) mg/l). Fibronectin was detected in five colostrum specimens (mean concentration 13.4 mg/l). Similar bands were detected after gel electrophoresis of purified adult plasma fibronectin and whole plasma from breast fed and formula fed neonates after staining or immunoblotting. Fibronectin isolated from breast milk also appeared similar to purified plasma fibronectin. It is possible, although unlikely, that fibronectin is absorbed intact from ingested colostrum. Alternatively, a factor(s) might be present in colostrum that contributes to the regulation of plasma fibronectin concentration.

Bottle Feeding↗
PubMed1985

Qualitative analysis of Coomassie-blue-stained proteins from normal prostate, benign prostatic hypertrophy, or adenocarcinoma of the prostate, separated by two-dimensional protein electrophoresis.

Samples from nine normal prostates (N), ten benign hypertrophic prostates (BPH), and eight adenocarcinomas of the prostate (ACP), obtained from the National Prostatic Cancer Project were analyzed by two-dimensional (2D)-protein electrophoresis. Qualitative analysis of Coomassie-blue-stained acidic proteins between pI 3.5 and 6.8 yielded these results: The total number of enumerated proteins was 136 (N), 107 (BPH), and 147 (ACP). Ninety-two denoted proteins were deemed common to the three kinds of samples, three were considered present in N and BPH, 7 in BPH and ACP, and 28 in N and ACP. Thirteen, five, and 20 proteins were detected only in N, BPH, or ACP. These proteins cannot be considered "unique" to their respective samples, since amounts of protein that do not exceed the minimum sensitivity of the dye may be present in the other samples. The similarity in the patterns of proteins from these three types of prostate samples is consistent with the following hypothesis: The distribution of proteins from histologically ambiguous prostate samples will correlate more closely with these protein profiles than with those associated with cancers originating from other organs.

Adenocarcinoma↗
PubMed1985

Comparison of the Du Pont Isolator 1.5 Microbial Tube and Trypticase soy broth for the recovery of Haemophilus influenzae type b in experimental bacteremia.

The isolator 1.5 Microbial Tube (E. I. du Pont de Nemours & Co., Inc., Wilmington, Del.) is a new blood culture system for detection of bacteremia in children which involves lysis of blood cells and direct plating of blood lysate on agar media. Haemophilus influenzae type b is a major pediatric pathogen and may be associated with low-density bacteremia (less than or equal to 50 CFU per ml), yet the clinical data on the efficacy of this system for recovery of H. influenzae b are limited. We used a rat model of H. influenzae b bacteremia and fresh, whole human blood inoculated in vitro with H. influenzae b to compare the 1.5 Microbial Tube and conventional Trypticase soy broth (BBL Microbiology Systems, Cockeysville, Md.) for the detection of low-density H. influenzae b bacteremia. There was a significantly lower recovery of H. influenzae b from blood of bacteremic rats and from in vitro-inoculated human blood by using the 1.5 Microbial Tube than by using Trypticase soy broth. Studies on the mechanism of this lower recovery suggested that the contents of the 1.5 Microbial Tube are toxic to H. influenzae b in the presence of human blood. Additional clinical data are necessary before the 1.5 Microbial Tube can be recommended for detection of low-density H. influenzae b bacteremia.

Animals↗
PubMed1984

Nuclear protein synthesis in a temperature-sensitive Chinese hamster ovary cell line at 40 degrees C.

We examined the incorporation of radioactive amino acids into nuclear proteins occurring at nonpermissive conditions in tsH1 Chinese hamster ovary cells with a temperature-sensitive defect in cytosol nonmitochondrial protein synthesis. In leucine-free medium at 40 degrees C, total cellular protein synthesis declined by 1-1.5%/min. As reported by others, preincubating these cells at 42 degrees C for 5-10 min sharply increased the rate of decline. The synthesis of acidic nuclear proteins at nonpermissive conditions (40 degrees C + 300 micrograms/ml cycloheximide) was demonstrated by the nuclear incorporation of 3H-tryptophan. Radioactivity, seen by autoradiography to be associated with these isolated Triton-X-100-washed nuclei, was released after incubating labelled nuclei with proteolytic enzymes. During incubation of tsH1 cells at nonpermissive conditions, pulse/chase experiments were consistent with the loss of some nuclear radioactivity into the cytoplasm. The distribution of cytosol and nuclear proteins, labelled at permissive or nonpermissive conditions and separated by isoelectric focusing, differed quantitatively and probably qualitatively, confirming the residual synthesis of acidic nuclear proteins at 40 degrees C in the presence of cycloheximide. Most newly synthesized acidic proteins retained by nuclei from cells labeled at nonpermissive conditions were present in a transciptionally active chromatin fraction. Although under these conditions the apparent rate of cellular RNA synthesis was unchanged, inhibiting residual cycloheximide-resistant nuclear protein synthesis with puromycin proportionately reduced RNA synthesis. Preincubating cells with 20 micrograms/ml of actinomycin D did not inhibit residual labelling of nuclear proteins; effects on residual nuclear labelling of impaired mitochondrial respiration were ambiguous. Nuclear proteins labelled under nonpermissive conditions probably included some of the 'prompt' heat shock proteins recently described. Provided certain assumptions are correct, our results are consistent with very limited protein synthesis associated with and even intrinsic to cell nuclei. They also suggest that this residual cycloheximide-resistant protein synthesis could be concerned with optimum synthesis or processing of certain nuclear RNA species.

Animals↗
PubMed1983

The distribution of acidic coomassie blue-stained proteins from uninvolved human liver, hepatoma, normal colon, primary colon cancer, and colon metastases to the liver, determined by two-dimensional protein electrophoresis.

The distribution of Coomassie blue-stained proteins from uninvolved regions of 4 human livers, from 1 hepatocellular carcinoma, and from 4 samples each of uninvolved colon, primary adenocarcinoma of the colon, and colon cancer metastatic to the liver was analyzed by two-dimensional protein electrophoresis. From a comparison of acidic proteins between pI 3.5 and 6.5, we conclude (1) that the majority (66 of 82) of denoted acidic proteins from 4 normal liver samples were represented in the hepatocellular carcinoma. Fifty-one of 58 proteins denoted in the 4 colon samples were detected in each of the 4 primary colon cancers; (2) that the "normograms" of proteins from normal colon and normal liver differed in many details, and their dissimilar patterns identified the source of the sample; (3) that hepatoma and primary adenocarcinoma of the colon were easily distinguished by their distribution of proteins; (4) that colon cancer metastatic to the liver contained a majority (50/58) of acidic proteins enumerated in primary colon cancer. These results indicate that uninvolved liver and colon and their primary or secondary cancers can be identified by their distribution of electrophoresed acidic proteins.

Adenocarcinoma↗
PubMed1983

Provisional "normograms" for identifying adenocarcinomas of the prostate or colon and hepatocellular carcinoma derived from their distribution of proteins separated by two-dimensional electrophoresis.

The distribution of proteins in samples from 8 prostate and 4 colon adenocarcinomas and 1 hepatoma was analyzed by 2-dimensional protein electrophoresis. Composite "normograms" based upon their distribution of proteins were developed from these patterns. Particular attention was paid to acidic proteins between pI 3.5 and 5.9. Of 161 proteins enumerated, 23 of the first 135 were present in prostate cancers, compared with 68 in colon cancer and 85 in the hepatoma. The 26 proteins denoted from nos. 135 to 161 were prostate associated, and none was evident in the colon or hepatoma samples. Twenty-seven prostate, 20 colon, and 48 liver cancer proteins were "unique" to each of the 3 cancers, respectively. The patterns of protein associated with each type of cancer were so dissimilar that with this technique no difficulty should be experienced in distinguishing these carcinomas originating from 3 different types of "stem" cells without obligatory recourse to microscopy.

Adenocarcinoma↗
PubMed1981

Two-dimensional protein electrophoresis and the identification of histologically indeterminate human cancers.

It is proposed to identify histologically indeterminate human cancers by comparing their qualitative content of stained proteins, separated by two-dimensional electrophoresis, with patterns of proteins from a series of identified human cancers of comparable or different stem cell origin. The hypothesis to be tested is that in cancer, biochemical ontogeny, reflected in the distribution of cellular and tissue proteins, will recapitulate phylogeny, albeit in a manner less organized than normal. Patterns of protein from cancer cells, whether histologically identified or not but originating from embryologically similar stem cells, are expected to exhibit greater homology, compared with protein profiles of cancer cells derived from stem cells of different embryologic origin. Normal or cancer cell proteins common or unique to one or more cell sources can be identified, and subsets of proteins that characterize cancer cells of specific stem cell origin identified. There are reasons to believe that cancer cells rarely, if ever express properties inconsistent with the basic cellular commitment of their stem cell of origin. Photo-optical scanning and computer-assisted analysis will greatly facilitate collating the many hundreds of discrete proteins, among which those used to characterize different cancer cells are to be found.

Electrophoresis, Polyacrylamide Gel↗
PubMed1976

Gastric acid and serum gastrin secretion before and after bypass of the small intestine for morbid obesity.

Six obese patients undergoing end-to-side jejunoileal bypass had gastric acid output and serum gastrin measurements performed preoperatively and within three months postoperatively. Meat extract stimulated acid output was higher in obese than in normal patients. Following the bypass procedure, basal and meat extract stimulated acid output significantly decreased. Basal and meat extract stimulated serum gastrin levels did not change following bypass. These studies demonstrate that after a small intestinal bypass, acid output decreases. Gastrin plays no role in this change.

Clinical Trials as Topic↗
PubMedDate not supplied

Identification of normal rat organs by two-dimensional protein electrophoresis.

Proteins from nine normal rat organs, including heart, lung thymus, liver, spleen, kidney, prostate, abdominal muscle, and brain, were solubilized, separated by electrophoresis according to their different isoelectric points and molecular weights, and stained with Coomassie blue. Patterns of major proteins unique to each organ were identified. Nine "unknown" samples, chosen from the same sources and submitted for analysis in a single blind study, were easily identified by comparing their protein profiles against the nine "reference" patterns. The ability to identify the origin of a tissue sample without recourse to microscopy, by comparing the pattern of its electrophoresed proteins with a "catalogue" of identified protein profiles, provides a prototype for the identification of histologically indeterminate normal and abnormal cells, tissues, and organs. Application of this technique to problems in human pathology and forensic medicine could prove to be very useful.

Abdominal Muscles↗