Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Kinases and Phosphatases

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...

Transducer Mechanism: Enzyme-Linked Receptors

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Early-onset neuroinflammation drives neurodegeneration caused by lysosomal PI(3,5)P<sub>2</sub> insufficiency.

Neurobiology of disease·2026

Same author

Running an electron microscopy core facility.

Journal of microscopy·2026

Same author

Rab24 protein levels show dynamic changes in mouse tissues and human cancers.

Cell and tissue research·2026

Same author

Ribosome-binding protein 1 maintains peroxisome biogenesis.

Journal of cell science·2025

Same author

Multimodal approach to characterize surgically removed epileptogenic zone from patients with focal drug-resistant epilepsy: From operating room to wet lab.

Epilepsia open·2025

Same author

The RAB27A effector SYTL5 regulates mitophagy and mitochondrial metabolism.

eLife·2025

Search research articles

Related Experiment Video

Updated: Jul 13, 2026

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Published on: August 2, 2018

Prostatic acid phosphatase is not a prostate specific target.

Ileana B Quintero¹, César L Araujo, Anitta E Pulkka

¹Research Center for Molecular Endocrinology and WHO Collaborating Centre, Biocenter Oulu, University of Oulu, Finland.

Cancer Research

|July 20, 2007

Summary

A novel transmembrane prostatic acid phosphatase (TM-PAP) is expressed widely in non-prostate tissues, unlike secretory PAP. This finding is crucial for designing effective PAP-based prostate cancer immunotherapies.

More Related Videos

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Direct Detection of Isolevuglandins in Tissues Using a D11 scFv-Alkaline Phosphatase Fusion Protein and Immunofluorescence

Direct Detection of Isolevuglandins in Tissues Using a D11 scFv-Alkaline Phosphatase Fusion Protein and Immunofluorescence

Published on: July 5, 2021

Related Experiment Videos

Last Updated: Jul 13, 2026

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Published on: August 2, 2018

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Direct Detection of Isolevuglandins in Tissues Using a D11 scFv-Alkaline Phosphatase Fusion Protein and Immunofluorescence

Direct Detection of Isolevuglandins in Tissues Using a D11 scFv-Alkaline Phosphatase Fusion Protein and Immunofluorescence

Published on: July 5, 2021

Area of Science:

Immunology
Molecular Biology
Oncology

Background:

Prostatic acid phosphatase (PAP) is a target for prostate cancer immunotherapy.
Secretory PAP is known for high prostatic expression.

Purpose of the Study:

To describe a novel PAP spliced variant mRNA encoding a type I transmembrane (TM) protein.
To investigate the expression and localization of TM-PAP in various tissues and cell types.
To assess the implications of TM-PAP expression for PAP-based immunotherapy.

Main Methods:

mRNA sequencing to identify PAP spliced variants.
Western blotting and immunohistochemistry to detect TM-PAP expression.
Cellular localization studies using immunofluorescence and co-localization with markers.

Main Results:

A novel TM-PAP variant was identified, featuring extracellular phosphatase activity and a lysosomal targeting signal.
TM-PAP is broadly expressed in non-prostate tissues (brain, kidney, liver, etc.) and certain cell lines (fibroblast, Schwann, LNCaP), but not PC-3 cells.
Secretory PAP expression decreased in prostate cancer, while TM-PAP expression was not detected in these samples.
TM-PAP localizes to the plasma membrane-endosomal-lysosomal pathway, co-localizing with flotillin-1.

Conclusions:

The wide expression of TM-PAP in non-prostate tissues, including neuronal and muscle tissues, must be considered in the design of PAP-based immunotherapies.
The distinct expression patterns of secretory PAP and TM-PAP highlight the complexity of PAP's role in prostate cancer and immunotherapy.