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A Pancreatic Source of Protease Activity in the Spontaneously Hypertensive Rat and its Reduction During Short‐term Food Reduction
Author(s) -
Chan Amy,
SchmidSchönbein Geert
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.640.22
Chronic hypertension is accompanied by multi‐faceted cellular and organ failures. We recently demonstrated in the spontaneously hypertensive rats (SHR) an uncontrolled activity of plasma proteases, including serine proteases, which causes degradation of key membrane receptors, leading to vasoconstriction, elevated blood pressure, insulin resistance, and immune suppression. But the source(s) of the plasma enzymatic activity is unknown. We determined with zymography the serine protease activity of SHR and its normotensive (WKY rat) controls in several organs of the digestive track. The results showed that the SHR pancreas has higher enzymatic activity, contributed by trypsin and chymotrypsin, than WKY in the pancreas, in pancreatic venules, and in venous blood (p<0.05). No elevation of protease activity was found in the SHR's intestinal wall or the liver. Furthermore, after 18 hr fasting SHRs show a trend for reduction of these enzyme activities associated with a significant decrease in systolic pressure. These results provide the first time a lead for the origin of uncontrolled enzymes in the SHR and suggest leakage of highly degrading enzymes from the pancreas into the circulation through its venules leading to receptor cleavage. Supported by HL10881.