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Rat and human membrane dipeptidase: tissue distribution and developmental changes.

Y Kera1, Z Liu, T Matsumoto

  • 1Department of Environmental Systems Engineering, Nagaoka University of Technology, Niigata, Japan.

Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
|July 30, 1999
PubMed
Summary

Membrane dipeptidase activity, crucial for hydrolyzing glycyl-D-alanine, shows distinct distribution and developmental patterns in rat and human tissues. This enzyme

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Area of Science:

  • Biochemistry
  • Enzymology
  • Physiology

Background:

  • Membrane dipeptidase (also known as leukine-enkephalinase) plays a role in peptide metabolism.
  • Understanding its distribution and activity is key to comprehending physiological processes.

Purpose of the Study:

  • To investigate the tissue distribution and developmental changes of membrane dipeptidase activity in rats and humans.
  • To characterize the enzyme responsible for glycyl-D-alanine hydrolysis.

Main Methods:

  • Enzyme activity assays using glycyl-D-alanine as a substrate.
  • Inhibition studies with cilastatin to confirm enzyme identity.
  • Analysis of tissue samples from rats of different ages and postmortem human tissues.
  • Measurement of enzyme activity in serum and urine from healthy volunteers.

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Main Results:

  • Membrane dipeptidase activity was high in rat lung, kidney, pancreas, testis, and intestinal/adrenal mucosa, with lower levels in spleen, liver, serum, and heart.
  • Activity in rat lung, kidney, adrenal, and intestinal mucosa increased with age up to 8 weeks.
  • Pancreatic, testicular, and splenic activity peaked around 3 weeks and then declined.
  • Human tissue distribution mirrored rat patterns, except for very low lung activity.
  • Enzyme activity was detected in human serum and urine, correlated with creatinine in urine.

Conclusions:

  • Membrane dipeptidase exhibits specific tissue distribution and developmental regulation in rats.
  • Human tissue distribution is largely similar to rats, with notable exceptions.
  • The enzyme is present in human biofluids (serum, urine), suggesting potential roles in physiological or pathological states.