Various forms of electrical stimulation are being used more frequently for bladder and muscle rehabilitation following spinal injury. Fifteen patients with spinal cord injury underwent a four to eight week period of thigh muscle reconditioning by surface electrical stimulation. The accumulated effects of this program on bladder function were assessed by urodynamic evaluation before and after the test period. Seven patients had beneficial changes of either an increase in bladder capacity and/or a decrease in bladder pressure. Six patients had a decrease in bladder capacity and/or an increase in bladder pressure, although two of these six patients had resolution of spinal shock. Two patients with detrusor areflexia had no changes in pressure or capacity. There was no change in the basic urodynamic patterns, only the parameters of bladder capacity and pressure. Increasing the use of electrical stimulation for rehabilitation of the spinal cord population might alter bladder function, although not consistently. One should, therefore, be aware of these changes when setting up such rehabilitation programs.

Adult↗

PubMedDate not supplied

Hormone metabolism and response of adenylate cyclase to parathyroid hormone in kidney.

1. Incubation of parathyroid hormone with plasma membranes from rat kidney cortex resulted in rapid loss of all hormal activity. 2. Chick kidney membranes showed no ability to inactivate parathyroid hormone even with prolonged incubation. 3. Biologically active, labelled parathyroid hormone was degraded to fragments by rat kidney membranes, but not by chick kidney. 4. Hormone-responsive adenylate cyclase activity in a mixture of rat and chick kidney membranes was additive. 5. Parathyroid hormone bound specifically to chick kidney palsma membranes. 6. It is concluded that hormone in activation during incubation has little relevance to the effectiveness of parathyroid hormone in stimulating adenylate cyclase activity in kidney, and furthermore that failure of chick kidney to metabolize the hormone is not the explanation for the greater sensitivity of this species to the hormone.

Adenylyl Cyclases↗

PubMedDate not supplied

Inhibition of human peptidyl dipeptidase (angiotensin I converting enzyme: kininase II) by human serum albumin and its fragments.

Purified peptidyl dipeptidase (angiotensin I converting enzyme or kininase II) from human lung or hog kidney is inhibited by commercially prepared plasma protein preparations, by human serum albumin and by the additive albumin stabilizer, acetyltryptophan. After the initial steps of purification, albumin was detected by immunodiffusion as a component in human lung peptidyl dipeptidase preparation. Fragment C of albumin (sequence 124-298) is a more potent inhibitor than the parent molecule (Ki = 1.7 X 10(-5)M). Reduction and carboxymethylation of five of the six S-S bridges in Fragment C yield the most potent noncompetitive inhibitor (Ki = 3 X 10(-6)M). Reduction of the sixth bridge raises the K1. This indicates that maintenance of the tertiary structure in Fragment C is of importance for the inhibition. Neither albumin nor Fragment C are substrates of the enzyme. Fragment C and its derivative also inhibit the inactivation of bradykinin by the purified human enzyme and by the peptidyl dipeptidase on the surface of intact cultured human endothelial cells.

Angiotensin-Converting Enzyme Inhibitors↗