Mary E. Maier

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We report the primary sequence of TASK-4, a novel member of the acid-sensitive subfamily of tandem pore K(+) channels. TASK-4 transcripts are widely expressed in humans, with highest levels in liver, lung, pancreas, placenta, aorta and heart. In Xenopus oocytes TASK-4 generated K(+) currents displaying a marked outward rectification which was lost by(More)
We studied the inhibition of tissue kallikrein by protein C inhibitor (PCI), a relatively unspecific heparin-dependent serine protease inhibitor present in plasma and urine. PCI inhibited the amidolytic activity (cleavage of H-D-valyl-L-leucyl-arginine-p-nitroaniline) of urinary kallikrein with an apparent second order rate constant of 2.3 x 10(4) M-1 s-1(More)
To assess the value of microscopic analysis of urinary erythrocyte morphology as the initial step in the investigation of patients with isolated symptomless microhaematuria, 316 consecutive patients were grouped according to whether they excreted eumorphic or mixed forms of erythrocytes or only dysmorphic forms. The former group was investigated fully, and(More)
A synthetic peptide (RS-83277) derived from the structure of human C-reactive protein (CRP) was previously shown to have antitumor activity in three different murine tumor models when administered in multilamellar vesicles (MLV). The therapeutic effects were comparable to those seen with MLV-encapsulated native CRP. The present study evaluated the(More)
Fab fragments from two new monospecific anti-human tissue kallikrein sera were examined for their capacity to inhibit the functional activities of purified human urinary kallikrein and purified human pancreatic kallikrein. Fragments from a new anti-urinary kallikrein serum and from an anti-pancreatic kallikrein serum yielded mixed inhibition of(More)
In hematuria, dysmorphic red blood cells found in the urine sediment are known to indicate glomerular origin of bleeding. To better understand the mechanisms which might cause the typical membrane changes in dysmorphic erythrocytes in vivo, we have exposed normal human erythrocytes in vitro to an osmotic and enzymatic environment similar to that of the(More)
Tryptase, the major neutral protease of human pulmonary mast cell secretory granules, rapidly inactivates human high m.w. kininogen (HMWK) in vitro. HMWK (5600 nM) lost 50% of its capacity to release kinin in response to kallikrein after a 5-min incubation with tryptase (31 nM), even though kinin activity was neither generated nor, when bradykinin was(More)
The types of kinins released from purified native, single chain human high and low molecular mass kininogens (HMMKs and LMMKs, respectively) by purified human urinary kallikrein were separated by reverse-phase HPLC and quantitated by the rat uterus bioassay. [Hyp3]-lysyl-bradykinin, a recently discovered kinin, represented up to 58% of the biological(More)
The capacity of purified tryptase, the major neutral tryptic protease of human lung mast cells, to serve as a kininogenase was examined with purified human low molecular weight kininogen (LMWK) as the substrate. Incubating of 25 mug of tryptase with LMWK for 2 to 30 minutes, with or without heparin, yielded no net time-dependent kinin release as determined(More)
In an effort to investigate the efficiency of various pharmacological agents in protecting the kidney against normothermic ischemia, an animal model was developed and the post-ischemic hemodynamics in the renal cortex of rabbit kidneys were studied. Renal cortical blood flow was evaluated 5-30 min after 60 min of normothermic ischemia of the left kidney(More)