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Biomedical subjects

P Valenzuela

Publications and source records attributed to P Valenzuela.

At least 55 records · Page 3Linked to original sources
PubMed1989

[Medical care to cerebrovascular syndrome].

We analyzed clinical data from all patients with a stroke admitted to the Emergency Service of a General Hospital in Santiago, from 1984 to 1986. 371 patients (196 women and 175 men) were diagnosed as having thrombosis (43%), embolic occlusion (18%), intracerebral hemorrhage (36%) and subarachnoid hemorrhage (3%). CAT scans were performed in 25% and angiography in 16%. The diagnosis was considered proven in 40% of cases. Overall hospital mortality was 46%, raising to 66% for hemorrhages. Prevention of cerebral edema was the main medical treatment. The present data suggest that primary prevention of and technological facilities to treat cerebrovascular episodes are inadequate at a general hospital level in Santiago.

Adult↗
PubMed1989

[Computerized registry of medical procedures and diagnostic codification].

Retrospective analysis of clinical information requires easy access to reliably stored data. We developed a program running on a microcomputer and using codes from the International classification of diseases, to be used on line. The program stores diagnostic codes, medical actions and a summary for each case. It uses inexpensive hardware and is friendly to inexperienced users.

Emergency Service, Hospital↗
PubMed1988

Synthesis and assembly of a functionally active recombinant platelet-derived growth factor AB heterodimer.

A Chinese hamster ovary cell line that stably expresses transfected human platelet-derived growth factor (PDGF) A and B chain precursors was established. All three dimeric combinations of PDGF chains were produced by this cell line; their biosynthesis, assembly, and processing were followed by pulse-chase analyses. PDGF-AA, PDGF-AB, and PDGF-BB were processed to Mr values of about 30,000 and were accumulated in these forms in the medium. In addition, PDGF-BB was further processed to a 24-kDa component, which remained cell-associated. The major secreted component was PDGF-AB, which was purified and shown to have structural and functional characteristics indistinguishable from PDGF-AB purified from human platelets.

Animals↗
PubMed1988

Characterization of recombinant human epidermal growth factor produced in yeast.

Four different forms of human epidermal growth factor (h-EGF) are found in the culture medium of a recombinant strain of Saccharomyces cerevisiae. These forms were characterized after purification using reverse-phase high-performance liquid chromatography. The most abundant form of secreted recombinant h-EGF has leucine at the carboxyl terminus and is identical with gamma-urogastrone. A second species is identical with the most abundant form except that it lacks the carboxyl-terminal leucine. This form appears to be the product of a carboxypeptidase found in the growth medium. The other two forms of recombinant h-EGF are the respective oxidation products of the above where the single methionine residue has been converted to methionine sulfoxide. These four forms of recombinant h-EGF are fully active; they bind to the EGF receptor of A431 cells as well as stimulate mitotic activity of human foreskin fibroblasts with equal specific activity. The location of the disulfide bonds in the predominant form of recombinant h-EGF was determined following digestion with thermolysin. The amino acid compositions of the resulting peptides showed that the placement of disulfide bonds in recombinant h-EGF is identical with that in murine EGF.

Amino Acid Sequence↗
PubMed1987

Measurement of the endometrial cavity length using Wing Sound I.

Parity is a factor that influences the axial length of the uterus. The knowledge of different measurements will help in the fitting of the IUD. In this paper, 657 cavimetries have been studied in relation to parity. A progressive increase of both the total uterine length and the endometrial cavity length have been observed in relation to parity, but none regarding the cervical length.

Cervix Uteri↗
PubMed1987

The yeast tRNA(Phe) gene family: structures and transcriptional activities reveal member differences not explained by intragenic promoters.

Several cloned members of the yeast tRNA(Phe) gene family were transcribed in vitro using a HeLa extract and a yeast extract. The optimum DNA concentration was determined and kinetic experiments were performed for each clone to compare transcription levels. Both extract systems were able to splice the intervening sequence, but only the yeast extract produced the mature product. Some genes were not transcribed with the homologous system while they were transcribed with the HeLa extract, suggesting a control mechanism that is not operating in the heterologous system. Competition experiments demonstrated that the intragenic promoters of the inactive genes were able to bind transcription factor(s), but not as efficiently as active genes. This binding was not so strong when using linear DNA and was dependent on the presence of the 3' intragenic control region. DNA sequencing and computer analysis indicated the presence of short conserved sequences upstream from the genes. These sequences, which are not related to the intragenic promoters, are direct repeats of part of the 3' coding region in those genes that are transcribed in the homologous system. The relevance of these sequences on homologous transcription in vitro remains to be established.

Base Sequence↗
PubMed1986

Enhancement of epidermal regeneration by biosynthetic epidermal growth factor.

Epidermal regeneration depends on mitosis and migration of keratinocytes. Epidermal growth factor is known to stimulate growth of keratinocytes in vitro, thus it might be expected to promote wound healing. The results of this study show that topical application of biosynthetic human epidermal growth factor accelerates epidermal regeneration in split-thickness wounds and partial-thickness burns. The significant enhancement of epidermal regeneration suggests the potential for clinical use of epidermal growth factor for accelerating healing of burns, wounds from trauma, diabetic ulcers, skin graft donor sites, and others.

Animals↗
PubMed1985

Biosynthetic human EGF accelerates healing of Neodecadron-treated primate corneas.

Topical administration of biosynthetic human epidermal growth factor (h-EGF), given in combination with an antibiotic and synthetic steroid (Neodecadron) accelerated the rate of corneal epithelial regeneration and significantly increased the strength of full-thickness stromal incisions in primates. The regenerated epithelial cells of EGF-Neodecadron-treated corneas appeared normal on histologic examination and showed no evidence of hypertrophy or hyperplasia. The EGF-Neodecadron-treated stromal incisions were characterized by new collagen formation and a smaller epithelial cell plug than Neodecadron-treated control corneas. These results suggest that biosynthetic h-EGF, which lacks the immunologic potential of nonhuman proteins, may be effective in accelerating healing of corneal epithelial defects and stromal incisions in patients whose healing is suppressed by treatment with steroids.

Animals↗
PubMed1984

Isolation and sequence of a rat chymotrypsin B gene.

A cDNA clone encoding part of chymotrypsin B was isolated from a cDNA library prepared from rat pancreatic mRNA and used as a probe to isolate the chymotrypsin B gene. The nucleotide sequence of this gene is presented. The 4709-base pair transcribed portion of the isolated gene was inferred from the cDNA and gene sequence, and the 5' border was determined by primer extension on pancreatic polyadenylated RNA. The coding portion of the gene is interrupted by six introns. The active site residues His 57, Asp 102, and Ser 195 are encoded by separate exons. Moreover, two regions of the enzyme which form the substrate-binding pocket are also encoded by separate exons. Thus, the substrate specificity and catalytic activity of the enzyme are produced by joining several exons encoding protein segments that are intrinsically catalytically inactive. The number and location of the intron/exon junctions of the chymotrypsin gene as compared to those of other serine protease genes, as well as the location of the genes on separate chromosomes, suggest that the duplication that resulted in the formation of the chymotrypsin gene was an ancient evolutionary event.

Amino Acid Sequence↗