Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

You might also read

Related Articles

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

Sort by
Same author

[Mid-to long-term efficacy of drug-eluting stents for vertebral artery ostial stenosis].

Zhonghua yi xue za zhi·2026
Same author

Nutrient excess remodels islet autonomic innervation via pancreatic schwann cells.

bioRxiv : the preprint server for biology·2025
Same author

Observation of tt[over ¯] Production in Pb+Pb Collisions at sqrt[s_{NN}]=5.02  TeV with the ATLAS Detector.

Physical review letters·2025
Same author

Search for Dark Matter Produced in Association with a Dark Higgs Boson in the bb[over ¯] Final State Using pp Collisions at sqrt[s]=13  TeV with the ATLAS Detector.

Physical review letters·2025
Same author

Safety and efficacy of stent-assisted coiling of unruptured distal anterior cerebral artery aneurysms with low-profile braided stents.

Clinical radiology·2025
Same author

Search for Magnetic Monopole Pair Production in Ultraperipheral Pb+Pb Collisions at sqrt[s_{NN}]=5.36  TeV with the ATLAS Detector at the LHC.

Physical review letters·2025

Related Experiment Video

Updated: Jun 24, 2026

Mouse In Vivo Placental Targeted CRISPR Manipulation
07:39

Mouse In Vivo Placental Targeted CRISPR Manipulation

Published on: April 14, 2023

Protein processing by the placental protease, cathepsin P.

M Hassanein1, A Sri Bojja, L Glazewski

  • 1Department of Biomedical Research, Alfred I duPont Hospital for Children, Wilmington, DE 19803, USA.

Molecular Human Reproduction
|April 7, 2009
PubMed
Summary

Cathepsin P, a placental enzyme, processes endoplasmic reticulum proteins like calreticulin by removing their retention signal. This suggests a role in trophoblast giant cell differentiation.

More Related Videos

siRNA Transfection and EMSA Analyses on Freshly Isolated Human Villous Cytotrophoblasts
09:57

siRNA Transfection and EMSA Analyses on Freshly Isolated Human Villous Cytotrophoblasts

Published on: September 20, 2016

Comprehensive Evaluation of the Effectiveness and Safety of Placenta-Targeted Drug Delivery Using Three Complementary Methods
09:04

Comprehensive Evaluation of the Effectiveness and Safety of Placenta-Targeted Drug Delivery Using Three Complementary Methods

Published on: September 10, 2018

Related Experiment Videos

Last Updated: Jun 24, 2026

Mouse In Vivo Placental Targeted CRISPR Manipulation
07:39

Mouse In Vivo Placental Targeted CRISPR Manipulation

Published on: April 14, 2023

siRNA Transfection and EMSA Analyses on Freshly Isolated Human Villous Cytotrophoblasts
09:57

siRNA Transfection and EMSA Analyses on Freshly Isolated Human Villous Cytotrophoblasts

Published on: September 20, 2016

Comprehensive Evaluation of the Effectiveness and Safety of Placenta-Targeted Drug Delivery Using Three Complementary Methods
09:04

Comprehensive Evaluation of the Effectiveness and Safety of Placenta-Targeted Drug Delivery Using Three Complementary Methods

Published on: September 10, 2018

Area of Science:

  • Biochemistry
  • Proteomics
  • Cell Biology

Background:

  • Cathepsin P belongs to placentally expressed cathepsins (PECs), closely related to the broad-specificity cathepsin L.
  • PECs offer a unique model to study proteolytic functions in the mammalian placenta.
  • Cathepsin P exhibits a restricted substrate preference for hydrophobic amino acids.

Purpose of the Study:

  • To identify and characterize substrates of Cathepsin P.
  • To investigate the role of Cathepsin P in the processing of endoplasmic reticulum (ER) proteins.
  • To explore the potential function of Cathepsin P in trophoblast giant cell differentiation.

Main Methods:

  • Proteomic techniques including 2D-difference gel electrophoresis, trypsin digestion, and MALDI MS/MS were employed.
  • Recombinant Cathepsin P was incubated with rat choriocarcinoma (Rcho-1) cell proteins.
  • Western blotting and immunohistochemistry were used to validate substrate processing and localization.

Main Results:

  • Two ER proteins, gp96 and calreticulin, were identified as potential substrates of Cathepsin P.
  • Cathepsin P was shown to process calreticulin and gp96 by removing their C-terminal KDEL ER retention signal.
  • Cathepsin P co-localizes with calreticulin in Rcho-1 cells, and extracellular calreticulin induces Rcho-1 cell differentiation.

Conclusions:

  • Cathepsin P plays a role in the post-translational modification of ER proteins, specifically calreticulin and gp96.
  • The processing of calreticulin by Cathepsin P may be involved in the secretion of calreticulin during trophoblast giant cell differentiation.
  • Cathepsin P's function in processing secreted proteins highlights its importance in placental biology.