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Related Experiment Videos

Study on dipeptidylpeptidase II (DPP II)

R Gossrau, Z Lojda

    Histochemistry
    |January 1, 1980
    PubMed
    Summary

    Dipeptidylpeptidase II (DPP II) activity was studied in multiple species using biochemical and histochemical methods. DPP II is widely distributed, with highest activity in specific organs and cell types, particularly lysosomes.

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    Area of Science:

    • Biochemistry
    • Histochemistry
    • Enzymology

    Background:

    • Dipeptidylpeptidase II (DPP II) is an enzyme involved in protein metabolism.
    • Understanding its activity and localization is crucial for various biological processes.

    Purpose of the Study:

    • To investigate the activity and localization of dipeptidylpeptidase II (DPP II) in different organs and species.
    • To identify optimal substrates and methods for DPP II detection and quantification.

    Main Methods:

    • Biochemical assays using various substrates (e.g., Lys-Pro-MNA, Ala-Pro-MNA, Lys-Ala-MNA) to determine kinetic properties (Km, Vmax).
    • Histochemical staining with specific substrates and coupling agents (e.g., Fast Blue B) on different tissue preparations (freeze-dried, fixed sections).
    • Quantitative microdensitometry for enzyme activity measurement in enterobiopsies.

    Main Results:

    • Lys-Pro-MNA and Ala-Pro-MNA were identified as sensitive substrates for DPP II, with Lys-Ala-MNA showing higher specificity.
    • DPP II exhibits optimal activity at pH 5.5 and is inhibited by DFP, Tris, and puromycin.
    • Significant organ and species-specific differences in DPP II activity were observed, with high activity in rat kidneys, epididymis, and spleen, and in guinea-pig epididymis and testis.
    • Histochemical analysis revealed DPP II localization primarily in lysosomes across various cell types, including renal tubules, macrophages, and enterocytes.

    Conclusions:

    • DPP II is ubiquitously present across investigated organs and species, with notable variations in activity.
    • Lys-Ala-MNA is a suitable substrate for both biochemical and histochemical studies of DPP II.
    • Lysosomal localization of DPP II is common, with specific cell types exhibiting particularly high activity.

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