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Related Concept Videos

Integrins

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...

Activation of Integrins

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.

Intracellular Signaling Affects Focal Adhesions

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...

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Related Experiment Video

Updated: May 31, 2026

Spatial and Temporal Control of Murine Melanoma Initiation from Mutant Melanocyte Stem Cells

Spatial and Temporal Control of Murine Melanoma Initiation from Mutant Melanocyte Stem Cells

Published on: June 7, 2019

Canine malignant melanoma alpha-3 integrin binding peptides.

Olulanu H Aina¹, Yoshiko Maeda, Matthew Harrison

¹Division of Hematology & Oncology, Department of Internal Medicine, UCD Cancer Center, University of California Davis, Sacramento, CA 95817, USA.

Veterinary Immunology and Immunopathology

|July 5, 2011

Summary

Novel peptide ligands targeting alpha-3 integrin show promise for melanoma imaging and therapy. These agents demonstrate rapid tumor uptake and high tumor-to-background ratios in canine models, aiding early detection and treatment.

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Area of Science:

Oncology
Molecular Imaging
Drug Delivery

Background:

Melanoma diagnosis and treatment require novel targeted agents.
Alpha-3 integrin is overexpressed in metastatic melanoma, presenting a potential therapeutic target.
Peptide ligands targeting alpha-3 integrin offer a strategy for diagnostic and therapeutic applications.

Purpose of the Study:

To evaluate alpha-3 integrin-binding peptides for melanoma imaging and therapeutic delivery.
To assess the binding affinity and tumor uptake of alpha-3 integrin ligands in canine melanoma models.

Main Methods:

Generated and validated five canine melanoma cell lines using melanoma markers.
Tested binding affinity of alpha-3 integrin-binding peptides (cdGXGXXc motif) to cell lines and primary tumors.
Utilized fluorescent conjugates of OA02 peptide for optical imaging of xenografts in nude mice.

Main Results:

All five canine melanoma cell lines expressed alpha-3 integrin.
Four cell lines and primary tumors showed affinity for alpha-3 integrin-binding peptides.
Optical imaging revealed rapid, strong tumor uptake of the tracer, persisting for approximately 48 hours with high tumor-to-background ratios.

Conclusions:

Alpha-3 integrin-binding ligands are effective for optical imaging of canine melanoma.
These ligands show potential as probes for melanoma imaging and delivery of cytotoxic agents.
Targeting alpha-3 integrin represents a promising strategy for melanoma management.