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J M Pascual

Publications and source records attributed to J M Pascual.

At least 73 records · Page 4Linked to original sources
PubMed1989

[Postoperative serum amylases of patients undergoing cardiac surgery].

Serum amylase was studied in twenty seven patients submitted to cardiac operation. The ages ranged between 16 and 74 (mean 55) years; twenty one (78) were male and six (22%) female. Myocardial revascularization was carried on in 17 patients, mitral valve replacement in four patients, aortic valve replacement in two patients, plastic surgery of the aortic valve in two patients, plastic surgery of the mitral valve in one patient. Blalock Taussig anastomosis was carried on in one patient. The serum amylase was determined in samples obtained before operations, 24 hours and 48 hours postoperatively. Seven (26%) patients showed postoperative elevation of seric amylase in the absence of clinical signs of pancreatitis. Thus, postoperative elevation of seric amylase after cardiac surgery may occur in the absence of pancreatitis and may be due to other factors associated with the patient, with the operative procedure, with drugs used and with surgical complications.

Adolescent↗
PubMed1989

PAF-acether, superoxide anion and beta-glucuronidase as parameters of polymorphonuclear cell activation associated with cardiac surgery and cardiopulmonary bypass.

1. Seven patients submitted to myocardial revascularization surgery with cardiopulmonary bypass were studied. Blood samples were obtained immediately before and 24 h after surgery. The parameters studied were the production of platelet activating factor (PAF-acether) and superoxide anion, cellular beta-glucuronidase activity as well as polymorphonuclear cell (PMN) and platelet counts. 2. Twenty-four h after surgery, there was a 54% decrease in platelet number (P less than 0.005), a 121% increase in PMN number (P less than 0.005), a 353% increase in PAF-acether (P less than 0.01), a 211% increase in superoxide anion (O2-) and a 104% increase in beta-glucuronidase (P less than 0.05) levels when compared with the pre-surgery levels. 3. The present results indicate that PMN are more reactive after surgery with cardiopulmonary bypass.

Blood Cell Count↗
PubMed1987

Drug fever.

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Azathioprine↗
PubMed1985

Plasma glucagon and glucagon-like immunoreactive components in Type 1 (insulin-dependent) diabetic patients and normal subjects before and after an oral glucose load.

Biogel P-30 filtration of plasma from Type 1 (insulin-dependent) diabetic patients and normal subjects in basal state and after an oral glucose load was assayed with a C-terminal (30 K) and a glucagon-like immunoreactivity-cross-reacting antiserum (R8). Up to four immunoreactive peaks of approximate molecular sizes of greater than 20,000 (fraction I), 9000 (fraction II), 3500 (fraction III) and 2000 (fraction IV) were detected with the two antisera in both groups. In the basal state, the only significant difference observed between both groups was a higher R8-reactivity in fraction II in the group of diabetic patients, although the R8 minus 30 K values for this fraction did not show a significant difference between both groups. After glucose the only significant differences were an increase of R8-reactivity in fraction II in both groups (p less than 0.01) and a decrease of 30 K-reactivity in fraction III (IRG3500) in normal subjects (p less than 0.05). In seven out of 12 diabetic patients, 30 K-reactivity in fraction II (IRG9000) and III (IRG3500) increased above their basal values. The gut-glucagon-like immunoreactivity response to oral glucose (delta R8-delta 30 K values in fraction II) was similar in both the diabetic and normal subjects. These results indicate that the paradoxical rise in plasma immunoreactive glucagon after oral glucose in diabetic patients may be due to an increase of both IRG3500 and/or IRG9000, the gut-glucagon-like immunoreactivity released during glucose absorption has a molecular weight of approximately 9000, and no differences in plasma gut-glucagon-like immunoreactivity were observed in Type 1 diabetic patients when compared with normal subjects, either in the basal state or after glucose ingestion.

Adult↗
PubMed1985

Plasma glucagon-immunoreactive components in early life in dogs.

High plasma concentrations of C-terminal immunoreactive glucagon (IRG) have been found during early life in several mammalian species. We have analyzed the plasma IRG of 12 h to 60 day-old dogs in terms of the 4 peaks (IRG greater than 20,000, IRG9000, IRG3500 and IRG2000) obtained by gel filtration on Bio-Gel P-30. Significant changes with age and in response to administered agents were confined to IRG9000 and IRG3500. IRG9000 was 9-fold higher in 12-36 h old dogs than in adults (108 +/- 24 pg/ml pancreatic glucagon equivalents v. 12 +/- 3 pg/ml, mean +/- SEM) and showed a decline to 2-fold higher (27 +/- 5 pg/ml) at 31-60 days. IRG3500 was higher than in the adult only during the first 36 h of life (36 +/- 5 pg/ml v. 15 +/- 3 pg/ml). Arginine infusion (0.5 g/kg over 15 min) caused an increase in plasma levels of both IRG9000 and IRG3500 in the newborn, whereas in adult dogs only IRG3500 was increased. Insulin injection (0.2 U/kg intravenously) causing a marked hypoglycemia had no significant effect on the plasma level of any IRG component in newborn dogs. Dihydrosomatostatin infusion (10 micrograms/kg bolus +/- 90 micrograms/kg over 30 min) caused a decrease in both IRG9000 and IRG3500. The increased basal level and secretory response to arginine of IRG9000 in newborn dogs may reflect an immaturity of the A cells, whereby more of this component, which may represent a precursor of pancreatic glucagon, is secreted than in the adult. The immature A cells also appear to have an impaired secretory response to hypoglycemia.

Aging↗
PubMed1982

Renal metabolism of gut glucagon-like immunoreactivity.

To examine the role of the kidney in the catabolism of gut glucagon-like immunoreactivity (GLI), we compared the plasma GLI responses of normal and nephrectomized dogs given intraduodenal glucose loads and studied the clearance of gut GLI by the isolated perfused rat kidney. Both basal and postload plasma samples were analyzed with a glucagon C-terminal specific antibody and a GLI-reacting N-terminal antibody. The GLI response was taken to be the difference between the increments seen with these two antibodies after glucose loading. Although glucose-induced GLI increments could not be detected in untreated plasma from nephrectomized dogs, chromatographed plasma revealed a significant rise in GLI-fraction II (7000--12000 daltons) in both nephrectomized and normal dogs (732 +/- 200 and 586 +/- 111 pg/ml, respectively). We also found that crystalline glucagon was cleared by the isolated closed-circuit perfused rat kidney, but gut-GLI either as crude extract or as peak I (7000--12000 daltons) was not. Our data suggest that the kidney may not play an important role in gut-GLI catabolism.

Animals↗