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Characterization of a novel prepro VIP derived peptide
Biochemical and Biophysical Research Communications
|September 30, 1986
Summary
A novel, large molecular weight form of peptide histidine methionine (PHM) is present in the stomach, nasal mucosa, and urogenital system. Tissue-specific processing of prepro-VIP may explain these findings, with unclear biological significance.
Area of Science:
- Biochemistry
- Molecular Biology
- Endocrinology
Background:
- Peptide histidine methionine (PHM) is a peptide hormone.
- Previous studies identified PHM in the stomach.
Purpose of the Study:
- To investigate the distribution of a newly identified large molecular weight form of PHM.
- To explore the post-translational processing of prepro-VIP in different tissues.
Main Methods:
- Immunohistochemistry using an antibody against the spacer peptide sequence prepro-VIP 111-122.
- Detection of PHM in various tissue homogenates.
Main Results:
- The large molecular weight PHM form was found in high concentrations in the nasal mucosa and urogenital system, in addition to the stomach.
- This form was notably absent in the central nervous system, intestine, and lung.
- The antibody to the spacer peptide also reacted with the large molecular weight PHM, suggesting altered processing.
Conclusions:
- The post-translational processing of prepro-VIP appears to be tissue-specific.
- In certain tissues, cleavage at the C-terminal end of PHM may not occur as expected.
- The biological significance of this large molecular weight PHM form remains to be elucidated.