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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
pH Regulation in Cells01:28

pH Regulation in Cells

pH plays a critical role in maintaining normal cellular activities. It helps maintain the structure and function of various proteins, dictates the charge on cellular membranes, and is crucial for metabolic reactions inside the cell. Moreover, cells use the energy from the proton motive force to generate ATP.
Cytosolic pH
Under physiological conditions, the cytosolic pH is slightly more acidic than the extracellular pH. However, cells must prevent further acidification of their cytosol to...
pH Homeostasis01:31

pH Homeostasis

Acid-base homeostasis is essential for maintaining normal physiological activities in humans. The pH of various body fluids is strictly regulated because it is critical for the optimal activity of enzymes involved in metabolic reactions. Enzymes are basically proteins, so, any significant change in pH can affect their structure and activity. In humans, pH is regulated using three primary mechanisms— chemical buffer systems, respiratory regulation, and renal regulation.
Respiratory Regulation of...
Renal Regulation of Acid-Base Balance01:29

Renal Regulation of Acid-Base Balance

Metabolic reactions in the body produce nonvolatile acids, such as sulfuric acid, which generate an acid load of approximately 1 mEq of H+ per kilogram of body weight daily. Excreting H+ in the urine is essential to balance this acid load.
In the kidneys, cells within the proximal convoluted tubules (PCT) and the collecting ducts secrete hydrogen ions (H+) into the tubular fluid. Specifically, in the PCT, Na+/H+ antiporters secrete H+ while reabsorbing Na+.
However, the intercalated cells in...
Stomach pH Regulation01:21

Stomach pH Regulation

The human body carefully regulates the internal pH of different organs to maintain homeostasis. For example, while the blood plasma maintains a neutral pH of 7, the stomach lumen has an acidic pH of 1.5 - 3.5. The low pH of stomach lumen helps kill pathogens in the food and break down complex food molecules.
The acid-secreting gastric mucosal epithelial cells (parietal cells) lining the stomach lumen maintain the low pH in the lumen. Numerous ion transporters and channels on these parietal...

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Related Experiment Video

Updated: May 11, 2026

Phosphopeptide Analysis of Rodent Epididymal Spermatozoa
09:30

Phosphopeptide Analysis of Rodent Epididymal Spermatozoa

Published on: December 30, 2014

Human prostatic acid phosphatase: structure, function and regulation.

Sakthivel Muniyan1, Nagendra K Chaturvedi, Jennifer G Dwyer

  • 1Department of Biochemistry and Molecular Biology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198, USA. mlin@unmc.edu.

International Journal of Molecular Sciences
|May 24, 2013
PubMed
Summary

Human prostatic acid phosphatase (PAcP) dephosphorylates ErbB-2 in prostate cancer cells, reducing tumor growth. Its expression, regulated by NF-κB, impacts androgen sensitivity and castration resistance, crucial for understanding prostate cancer progression.

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Area of Science:

  • Biochemistry
  • Oncology
  • Molecular Biology

Background:

  • Human prostatic acid phosphatase (PAcP) is a glycoprotein implicated in prostate cancer (PCa).
  • Cellular PAcP (cPAcP) exhibits protein tyrosine phosphatase activity.
  • ErbB-2/Neu/HER-2 is a key receptor in cancer cell signaling.

Purpose of the Study:

  • To investigate the role of cPAcP in prostate cancer cell tumorigenicity and androgen sensitivity.
  • To elucidate the regulatory mechanisms of PAcP expression.
  • To explore the therapeutic implications of cPAcP in PCa.

Main Methods:

  • Functional assays to assess cPAcP phosphatase activity.
  • Western blotting and gene knockdown to study protein interactions and expression.
  • Promoter analysis to identify regulatory elements.

Main Results:

  • cPAcP dephosphorylates ErbB-2/Neu/HER-2, reducing PCa cell tumorigenicity.
  • cPAcP regulates androgen sensitivity; its knockdown promotes castration-resistant phenotype.
  • PAcP expression is potentially regulated by NF-κB via a novel binding sequence, independent of androgen levels.

Conclusions:

  • cPAcP plays a critical role in modulating prostate cancer cell growth and androgen sensitivity.
  • Understanding PAcP's function and NF-κB-mediated regulation is vital for PCa progression and therapeutic strategies.