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Left heart bypass (LHBP) with heparin coated perfusion equipment including an arterial filter (pore size: 40 microns) was performed in five canine experiments after full systemic heparinization (heparin 300 IU/kg; activated coagulation time [ACT] > 480 sec). The heparin coated filter was replaced after 45 min with a second heparin coated filter. Protamine (1:1) was added after 45 min and perfusion was continued for another 45 min before the second filter was replaced with an uncoated control filter. In addition to continuous hemodynamic monitoring, all filters were disassembled and analyzed morphometrically with a scanning electron microscope (deposits on screens were expressed as percent of surface covered with fibrin or number of cells/100 micron 2, respectively). For the first heparin coated filter (ACT > 480), 0.3 +/- 0.5% of the surface was covered with fibrin, 0.7 +/- 0.7% with platelets, and 0.02 +/- 0.0% with red cells. For the second heparin coated filter exposed to neutralization of heparin with protamine, surface coverage was fibrin in 22 +/- 15%, platelets in 3.2 +/- 0.8%, and red cells in 0.2 +/- 0.1% (p < 0.05 for all comparisons with filter 1). For uncoated control filters (ACT = 120), surface coverage was fibrin in 31 +/- 33%, platelets in 3.7 +/- 2.9%, and red cells in 0.2 +/- 0.1% (not significant [NS] for all comparisons with filter 2). Although all arterial filters used in this study remained patent throughout the scheduled period, it became clear that protamine given during perfusion reduces the antithrombotic activity of bonded heparin. Hence, protaminization during perfusion with heparin coated equipment cannot be recommended.

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Thirty-eight occluded hemodialysis accesses were infused with urokinase on 43 occasions. In 49% of the cases, the access patency was reestablished for a week or longer, although 38% of this subset subsequently rethrombosed. Postthrombolysis angiography detected a stenotic segment in 14 of 22 angiograms (64%). Local bleeding was common, but the thrombolytic therapy was generally well tolerated. Percutaneous thrombolysis in conjunction with angiography and access revision provides a clinically useful means of access preservation.

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Pancreatic secretory protein profiles differed significantly between patients with chronic pancreatitis (CP) and pancreatic carcinoma (CA). Specific regions of the patterns were altered when CP versus CA and when CP versus normals were compared. Bands isoelectric in the region of pH 9-11 were elevated in CP. The possible identification of this band as lactoferrin is discussed.

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Pancreatic cancer secretory protein profiles were shown to be different from normals by a microcomputer-assisted analysis of isoelectric focusing patterns. Two acidic protein band regions (pI 3.0 and 4.5) of the pancreatic carcinoma profiles were significantly increased, and eight protein bands (pI 3.7, 5.0, 5.5, 6.5, 6.9, 7.3, 8.0, greater than 10.0) were significantly decreased. Highly significant decreases occurred at pH 7.3 (chymotrypsinogen) and at pH 5.0 (procarboxypeptidase Al, DNase I) in nonactivated specimens. The ratio between the absorbance points at 2.08 and 2.63 cm from the anode in each protein pattern differentiated the pancreas cancer specimens from the control group. Profiles found for the control group gave pI values similar to those found in the literature. The potential value of these findings in the search for tumor markers warrants further investigation as to whether these specimens can be differentiated from those from chronic pancreatitis patients.

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A program is described for a computer-aided analysis system for isoelectric focusing (IEF) patterns. This system is primarily aimed at comparing and statistically analyzing large numbers of one-dimensional electrofocusing patterns in the search for specific tumor markers in pancreatic ductal secretions. It is designed to collect raw densitometric data, allow interactive processing, matching and statistical tests, and prepare high-quality plots of data at various stages.

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Pancreatic secretions from the hamster model for pancreatic ductal adenocarcinoma were analyzed to determine whether alterations had occurred in the protein composition. CCK-and secretin-stimulated secretions were collected from 13 animals with cancer and 16 normal controls. Subsequent separation of the proteins by isoelectric focusing showed the following: (1) Significant changes occurred in the protein composition from animals with carcinoma. An unusually dark band was present at pH 7.5 just below amylase (pH 7.65); two unidentified bands, present in the normals at pH 6.9 and 7.0, were missing; and marked decreases occurred in the cathodic proteins with isoelectric points above pH 9, (2) CCK provided the optimal stimulus for differentiating specimens from animals with carcinoma from the normal controls. (3) The protein concentrations of CCK-stimulated secretions of animals with carcinoma were significantly lower than the controls. We have concluded that the protein alterations which have occurred in the hamster model for pancreatic ductal adenocarcinoma warrant further investigation.

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