518 results on '"Serrano, V."'
Search Results
502. The activation of human [Glu1]plasminogen by human single-chain urokinase.
- Author
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Urano T, de Serrano VS, Gaffney PJ, and Castellino FJ
- Subjects
- Aminocaproic Acid, Antibodies, Monoclonal, Antibody Specificity, Aprotinin, Enzyme Activation, Fibrinolysin antagonists & inhibitors, Fibrinolysin physiology, Fluorescence Polarization, Humans, Kinetics, Protein Conformation, Structure-Activity Relationship, Urokinase-Type Plasminogen Activator immunology, Plasminogen metabolism, Urokinase-Type Plasminogen Activator physiology
- Abstract
The activation of human [Glu1]plasminogen ([Glu1]Pg) by single-chain human urokinase (SCUKase) displays a substantial lag phase at physiological levels of [Glu1]Pg. Employing a monoclonal antibody that exhibits a high level of specificity for SCUKase, as compared to two-chain urokinase (TCUKase), we have demonstrated conclusively that during this lag phase a progressive loss of SCUKase occurs, most likely resulting from its conversion to TCUKase, in a reaction catalyzed by plasmin (HPm). The overall activation of [Glu1]Pg by SCUKase is inhibited by physiological levels of Cl- and stimulated by epsilon-amino caproic acid. Kinetic studies demonstrate that both these effects are based on first, the reaction of [Glu1]Pg with the TCUKase that is formed during the activation, and, second, the concomitant rate at which HPm is provided for the conversion of SCUKase to TCUKase. The results indicate that at physiological levels of [Glu1]Pg, its activation in the presence of SCUKase is regulated in one manner by the rate at which SCUKase is converted to TCUKase, in a process that is strongly influenced by physiological levels of Cl-. Finally, and importantly, we show that SCUKase possesses very little, if any, inherent ability to activate [Glu1]Pg at a rate that influences the kinetics of HPm generation under physiological conditions of [Glu1]Pg and Cl- concentrations.
- Published
- 1988
- Full Text
- View/download PDF
503. [Unilateral exophthalmos as primary manifestation of an adenocarcinoma of the colon].
- Author
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Curull Serrano V, Vilaseca Momplet J, Arnau de Bolós JM, and Rilo Beltrán A
- Subjects
- Humans, Male, Middle Aged, Orbital Neoplasms complications, Adenocarcinoma complications, Colonic Neoplasms complications, Exophthalmos etiology, Orbital Neoplasms secondary
- Published
- 1983
504. Influence of various structural domains of fibrinogen and fibrin on the potentiation of plasminogen activation by recombinant tissue plasminogen activator.
- Author
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de Serrano VS, Urano T, Gaffney PJ, and Castellino FJ
- Subjects
- Binding Sites, Catalysis, Drug Synergism, Fibrinolysin analysis, Humans, Hydrolysis, Kinetics, Peptide Fragments pharmacology, Recombinant Proteins pharmacology, Spectrophotometry, Tissue Plasminogen Activator genetics, Fibrin analysis, Fibrinogen analysis, Plasminogen metabolism, Tissue Plasminogen Activator pharmacology
- Abstract
Fibrinogen, fibrin, and related fragments have varying stimulatory effects on the initial rate of the activation of human plasminogen ([ Glu1]Pg) by recombinant tissue plasminogen activator (rt-PA). A detailed analysis of this enhancement was undertaken using various purified and complexed forms of the known domains of fibrin(ogen) with a view to gaining additional knowledge regarding the substructures of fibrinogen and fibrin that are important for their stimulatory capacities. Both arvin-mediated fibrin, as well as fibrinogen fragments generated as a result of its cleavage with CNBr, stimulate the activation in a biphasic manner, most likely as a result of changes in the promoter molecule accompanying the denaturation processes that are normally employed to either solubilize or generate these particular promoters. Using purified fibrinogen and fibrin fragments, it was found that fragment E, which binds to [Glu1]Pg, does not enhance the activation reaction, while fragment D1 has a potentiating effect. This suggests that the binding of [Glu1]Pg to fibrin(ogen) alone is not, in itself, sufficient for stimulation of activation to occur, but that the rt-PA-fibrin(ogen) interaction is fundamental to this same process. All purified and mixtures of fragments containing the fragment D domain (e.g., D2E, X-oligomer, fragment X) stimulate the reaction to a greater degree than fibrinogen and fragment D1. It is concluded that the fibrinogen D domain is a sine qua non for the enhancement reaction, while structures containing the E domain had a symbiotic effect on enhancement.
- Published
- 1989
- Full Text
- View/download PDF
505. [Paget's disease involving the face. Apropos of 4 cases].
- Author
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Lucas M, Serrano V, Naval L, and Balda I
- Subjects
- Aged, Diagnosis, Differential, Female, Humans, Mandibular Diseases diagnostic imaging, Maxillary Diseases diagnostic imaging, Middle Aged, Osteitis Deformans diagnostic imaging, Radiography, Mandibular Diseases pathology, Maxillary Diseases pathology, Osteitis Deformans pathology
- Abstract
This study describes four cases of Paget's deforming dystrophy involving the jaw. In three of them the course of the disease affected only the bone involved whilst in the fourth the bones of the vault of the skull and some cranial nerves were affected in time. The prevalence of the female sex and of involvement of the maxilla was evident. The mandible was involved in only one case. Biochemical abnormalities were the same in all cases as well as being identical to those in cases of Paget's disease with multiple bone involvement. The authors suggest medical treatment (calcitonin, Na etidronate, mitramycin ) and surgery only when required for bone remodelling when there is interference with function.
- Published
- 1984
506. Estimation of nitrogen balance based on a six-hour urine collection in infants.
- Author
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Lopez AM, Wolfsdorf J, Raszynski A, and Contijoch-Serrano V
- Subjects
- Child, Preschool, Critical Care, Humans, Infant, Infant, Newborn, Time Factors, Urinary Catheterization, Nitrogen urine
- Abstract
The accuracy of a 6-hr vs a 24-hr urine collection for the determination of urinary urea nitrogen was studied in 15 infants. Patient's age ranged from 2 weeks to 3 yr, encompassing a wide variety of diagnoses. All patients had normal renal function at the time of the study. Participants had indwelling foley catheters throughout the study. Urine specimens were collected over a continuous 24-hr period. Aliquots obtained from urine collected over 0 to 6 hr and the total urine collection were analyzed utilizing the urease enzymatic method in the Astra. Statistical analysis was performed comparing the actual 24-hr determination to the estimation based on the 6-hr collection, utilizing linear regression. The analysis of data produced a highly significant correlation (r = 0.904, p less than 0.0001). When a 24-hr urine collection is not possible, a 6-hr collection is a useful alternative for the calculation of nitrogen balance in infants.
- Published
- 1986
- Full Text
- View/download PDF
507. [Salivary lithiasis as a complication of surgically treated Robin syndrome].
- Author
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Naval L, Herreros P, Serrano V, and Lucas M
- Subjects
- Adolescent, Cicatrix complications, Female, Humans, Postoperative Complications etiology, Pierre Robin Syndrome surgery, Salivary Duct Calculi etiology, Submandibular Gland pathology
- Abstract
A 15-year-old girl, operated upon (surgical ankyloglossia) at birth for glossoptosis due to Pierre Robin's syndrome provoking respiratory distress, presented with lithiasis of Wharton's duct. The pathogenesis of the lithiasis is considered to be related to the wounds and scars following the sublingual surgery, findings in this case also strongly suggesting the role of mechanical and inflammatory factors in the etiology of salivary gland lithiasis in general.
- Published
- 1983
508. [Renal transplants and pregnancy].
- Author
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Beltrán Suárez R, Castellanos Coutiño J, González Gómez M, and Concha Serrano VR
- Subjects
- Adult, Female, Humans, Immunosuppressive Agents administration & dosage, Obstetric Labor, Premature, Postoperative Period, Pregnancy Complications, Pregnancy, Multiple, Prenatal Care, Kidney Transplantation, Pregnancy
- Published
- 1985
509. Control of human plasminogen activation.
- Author
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Castellino FJ, Urano T, de Serrano V, Morris JP, and Chibber BA
- Subjects
- Aminocaproic Acid pharmacology, Chlorides pharmacology, Enzyme Activation drug effects, Humans, Kinetics, Plasminogen analogs & derivatives, Plasminogen antagonists & inhibitors, Streptokinase pharmacology, Tissue Plasminogen Activator pharmacology, Urokinase-Type Plasminogen Activator pharmacology, Plasminogen metabolism, Plasminogen Activators pharmacology
- Abstract
The activation of Glu1-plasminogen (Glu-Pg) by streptokinase (SK), urokinase (UK) and tissue plasminogen activator (tPA) is under rigorous control by molecules such as epsilon-aminocaproic acid (EACA), fibrinogen (Fg), fibrin (Fn) and, as we have recently discovered, anions. This presentation will focus on the biochemical mechanisms that are involved in these processes. In the case of activation by SK, a species of activator complex, composed of Glu-Pg and SK, can be identified that is inhibited by anions, such as Cl-, and stimulated by Fg and Fn. This species rapidly decays to another activator complex, also consisting of Glu-Pg and SK, that is much less sensitive to control by these effector molecules. The most stable activator complex, containing equimolar SK and plasmin, is not affected to a great extent by anions, Fg or Fn. In the overall activation of Glu-Pg by SK, Cl- behaves as a mixed inhibitor, with a Ki of 6.4-9.2 mM, and Fg functions as a mixed activator, displaying a Ka of 110-240 nM. These results show that activation of Glu-Pg by SK in physiological samples would be considerably inhibited by Cl- in the absence of Fg. The activation of Glu-Pg by both high- and low-molecular weight UK is also inhibited by Cl-, but is stimulated by EACA. The inhibition by Cl- does not occur in the presence of concentrations of EACA that saturate its weak binding sites on Glu-Pg, and the stimulation by EACA is maximally exhibited in the presence of Cl-.(ABSTRACT TRUNCATED AT 250 WORDS)
- Published
- 1988
- Full Text
- View/download PDF
510. [Gastric leiomyoma].
- Author
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Marin A, Bellido F, Domínguez F, Marin V, Sánchez de Vega, and Serrano V
- Subjects
- Aged, Diagnosis, Differential, Female, Humans, Leiomyoma pathology, Leiomyoma surgery, Stomach Neoplasms pathology, Stomach Neoplasms surgery
- Published
- 1978
511. Roles for chloride ion and fibrinogen in the activation of [Glu1]plasminogen in human plasma.
- Author
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Gaffney PJ, Urano T, de Serrano VS, Mahmoud-Alexandroni M, Metzger AR, and Castellino FJ
- Subjects
- Humans, Kinetics, Recombinant Proteins pharmacology, Thrombin physiology, Tissue Plasminogen Activator physiology, Chlorides pharmacology, Fibrinogen physiology, Plasminogen metabolism, Plasminogen Activators
- Abstract
Using two-dimensional immunoelectrophoresis and an antibody to alpha 2-antiplasmin, we assessed the plasmin generated in serum under different conditions as the plasmin-alpha 2-antiplasmin complex. Activation in serum of human [Glu1]plasminogen ([Glu1]Pg) by recombinant tissue plasminogen activator was inhibited by the normal serum levels of Cl- and was enhanced by physiological levels of fibrinogen in the presence or absence of Cl-. These results agree with the recognized ability of Cl- to induce a conformation in [Glu1]Pg less favorable for its activation than the conformation that results without Cl-. The enhancing effect of fibrinogen surpassed the inhibitory effect of Cl- over a wide range of recombinant tissue plasminogen activator concentrations in physiological serum. Lesser inhibition by Cl- was seen in a purified clot-lysis system, suggesting that [Glu1]Pg conformation when attached to soluble fibrin matrix was less affected by the anion. The data regarding the roles of circulating fibrinogen and Cl- in controlling the plasma level of activated [Glu1]Pg have important implications in thrombolytic therapy with recombinant tissue plasminogen activator.
- Published
- 1988
- Full Text
- View/download PDF
512. Examination of the secondary structure of the kringle 4 domain of human plasminogen.
- Author
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Castellino FJ, de Serrano VS, Powell JR, Johnson WR, and Beals JM
- Subjects
- Chymotrypsin, Circular Dichroism, Humans, Muramidase, Protein Conformation, Solubility, Spectrophotometry, Ultraviolet, Peptide Fragments blood, Plasminogen
- Abstract
The structure of a small region of human plasminogen (F4), consisting of amino acid residues Val354-Ala439 and containing its kringle 4 (K4) domain (residues Cys357-Cys434), has been predicted from Chou-Fasman calculations and hydropathy profiles, and compared to circular dichroism (CD) measurements on the isolated fragment. Calculations, by the Chou-Fasman method, of the probabilities of various types of secondary structures that exist in this region reveal that no helical structures are present. Of the total of 86 amino acid residues present in this K4-containing peptide region, 37% can adopt conformations of beta-pleated sheets, 48% of the amino acids can exist in beta-turns, and 15% of the residues can be present as coils. The structure of F4 in dilute aqueous solution has been experimentally evaluated by CD measurements. At pH = 7.4, in dilute salt solutions, a total of 64% beta-structures, 30% beta-turns, and 6% coiled structures is estimated to be present in this peptide region. Consideration of the marginal stability of many of the conformational regions of F4, as predicted by Chou-Fasman calculations, suggests that secondary structural flexibility is present in this fragment, which could result in ready adoption of new conformations. The hydropathy profile of F4 has been determined and suggests that this polypeptide is highly hydrophilic, especially in the regions of residues His387-Tyr396 and Cys406-Lys413. Thus, it appears as though a large portion of the surface of F4 can be exposed to solvent in its native conformation.
- Published
- 1986
- Full Text
- View/download PDF
513. [Routine aspiration and dental anesthesia. Study of 1,018 cases].
- Author
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Calatayud J, Manso FJ, Serrano V, and Zapata T
- Subjects
- Adolescent, Adult, Aged, Child, Humans, Middle Aged, Nerve Block, Anesthesia, Dental, Anesthesia, Local
- Published
- 1988
514. Effectors of the activation of human [Glu1]plasminogen by human tissue plasminogen activator.
- Author
-
Urano T, Sator de Serrano V, Gaffney PJ, and Castellino FJ
- Subjects
- Aminocaproic Acid pharmacology, Chlorides pharmacology, Enzyme Activation, Fibrinogen metabolism, Humans, Kinetics, Plasminogen metabolism, Recombinant Proteins metabolism, Tissue Plasminogen Activator metabolism
- Abstract
The activation of human [Glu1]plasminogen [( Glu1]Pg) by human recombinant (rec) two-chain tissue plasminogen activator (t-PA) is inhibited by Cl-, at physiological concentrations, and stimulated by epsilon-aminocaproic acid (EACA), as well as fibrin(ogen). Chloride functions as a result of its binding to [Glu1]Pg, with a Ki of approximately 9.0 mM, thereby rendering [Glu1]Pg a less effective substrate for two-chain rec-t-PA. EACA stimulates the activation in Cl-(-)containing solutions, with a Ka of approximately 4.0 mM, primarily by reversal of the Cl-(-)inhibitory effect. Fibrinogen appears to exert its stimulatory properties mainly through effects on the enzyme, two-chain rec-t-PA, with a Ka of approximately 3.7 microM in activation systems containing physiological levels of Cl-. Analysis of the results of this paper reveals that normal plasma components, Cl- and fibrinogen, exert major regulatory roles on the ability of [Glu1]Pg to be activated by two-chain rec-t-PA, in in vitro systems. The presence of Cl- inhibits the stimulation of [Glu1]Pg activation that would normally occur in the presence of fibrinogen, a result of possible importance to the observation that some degree of systemic fibrinogenolysis accompanies therapeutic use of tissue plasminogen activator.
- Published
- 1988
- Full Text
- View/download PDF
515. The control of the urokinase-catalyzed activation of human glutamic acid 1-plasminogen by positive and negative effectors.
- Author
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Urano T, Sator de Serrano V, Chibber BA, and Castellino FJ
- Subjects
- Anions, Humans, Kinetics, Osmolar Concentration, Salts, Plasminogen metabolism, Plasminogen Activators, Urokinase-Type Plasminogen Activator metabolism
- Abstract
The urokinase-catalyzed activation of human Glu1-plasminogen (Glu1Pg) has been found to be inhibited by monovalent anions in the following order of effectiveness: I- greater than SCN- greater than Cl- greater than IO3- greater than HCOO- greater than F- greater than OAc-. The inhibition is reversed by epsilon-aminocaproic acid, with its effectiveness in this capacity generally inversely proportional to the strength of the binding of the anion. The physical basis for the anion inhibition and epsilon-aminocaproic acid stimulation lies in the ability of these effectors to cause measurable opposite alterations in the conformation of Glu1Pg, which are revealed through study of the sedimentation velocity of the protein under various conditions. The kinetic mechanism of the chloride inhibition of Glu1Pg activation has been examined in detail. It has been found that the Glu1Pg.Cl complex serves as an alternate substrate to Glu1Pg for urokinase, with a greatly increased Km (25 +/- 3 and 2.2 +/- 0.3 microM, respectively) for activation. The kcat for the urokinase.Glu1Pg.Cl complex is approximately the same as that for urokinase.Glu1Pg (1.6 +/- 0.2 - 2.0 +/- 0.2/s). Similarly, the stimulation by epsilon-aminocaproic acid also results from effects on the Km of the activation, which is reduced to 1.8 +/- 0.2 microM for the Glu1Pg.Cl.epsilon-aminocaproic acid complex. The kcat for the urokinase.Glu1Pg.Cl.epsilon-aminocaproic acid of 2.4 +/- 0.3/s complex is not greatly different from that for urokinase.Glu1Pg.Cl. Nuclear magnetic resonance studies of the Glu1Pg-induced line broadening of the 35Cl- spectra in the presence and absence of epsilon-aminocaproic acid suggest that Cl- and epsilon-aminocaproic acid simultaneously bind to the protein and that each of these effectors displays its effects through separate binding sites.
- Published
- 1987
516. [Pulmonary atresia with intact intraventricular septum].
- Author
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Palacios-Macedo X, Rodríguez-Galaz F, Siordia-Zamorano R, Concha-Serrano V, Palacios-Cacacho E, and Pérez-Treviño C
- Subjects
- Female, Heart Defects, Congenital surgery, Humans, Infant, Pulmonary Valve surgery, Pulmonary Valve abnormalities
- Published
- 1979
517. Appearance of plasminogen activator activity during a synchronous cycle of a rat adenocarcinoma cell line, PA-III.
- Author
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Scott FM, Sator de Serrano V, and Castellino FJ
- Subjects
- Adenocarcinoma enzymology, Animals, Cell Cycle drug effects, Cell Line, Clone Cells, DNA Replication drug effects, Hydroxyurea pharmacology, Kinetics, Male, Prostatic Neoplasms enzymology, Rats, Thymidine metabolism, Adenocarcinoma pathology, Prostatic Neoplasms pathology, Tissue Plasminogen Activator biosynthesis, Urokinase-Type Plasminogen Activator biosynthesis
- Abstract
A study of the appearance of plasminogen activators during the cell cycle of a rat prostate adenocarcinoma cell line, PA-III, was undertaken. After release from a hydroxyurea (HU) block, the length of the cell cycle was determined and found to be 20-25 h, with the S-G2-M portions comprising approx. 10-15 h and the G1 phase occurring over a similar 10-15-h period. Assays for tissue-like plasminogen activator (t-PA) and urokinase-like plasminogen activator (u-PA) in cell-conditioned medium revealed an increased appearance of both enzymes shortly after the S phase of the cycle. The pattern of production of these activators remained the same under differing conditions of cell synchronization.
- Published
- 1987
- Full Text
- View/download PDF
518. [Methods for making local anesthesia more comfortable].
- Author
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Calatayud J, Manso FJ, Serrano V, and Kaiser C
- Subjects
- Humans, Injections, Anesthesia, Dental methods, Anesthesia, Local methods
- Published
- 1987
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