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Related Concept Videos

Activation of Integrins01:15

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.
Integrins01:10

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,...
Intracellular Signaling Affects Focal Adhesions01:17

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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HUVEC cell affinity evaluation and integrin-mediated mechanism study on PHSRN-modified polymer.

Yuan Liu1, Wei Wang, Jun Wang

  • 1Key Laboratory of Functional Polymer Materials, Ministry of Education, Institute of Polymer Chemistry, Nankai University, Tianjin, China.

Colloids and Surfaces. B, Biointerfaces
|January 11, 2011
PubMed
Summary

The peptide Pro-His-Ser-Arg-Asn (PHSRN) effectively supports human umbilical vein endothelial cell adhesion and growth. PHSRN-modified polymers show potential as biocompatible materials for cell culture and tissue engineering.

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Area of Science:

  • Biomaterials Science
  • Cell Biology
  • Polymer Chemistry

Background:

  • Poly(D,L-lactide-co-beta-malic acid) (PLMA) is a versatile biomaterial.
  • Peptides like PHSRN and GRGDS play roles in cell interactions.
  • Understanding peptide-polymer interactions is crucial for biomaterial development.

Purpose of the Study:

  • To investigate the role of the peptide Pro-His-Ser-Arg-Asn (PHSRN) in cell adhesion and growth.
  • To synthesize and evaluate PHSRN-containing polymers for their biocompatibility.
  • To compare the efficacy of PHSRN-modified polymers with GRGDS-modified polymers.

Main Methods:

  • Synthesis of PHSRN- and GRGDS-containing polymers (P-PN5 and P-GS5) by modifying PLMA.
  • Evaluation of cell adhesion and proliferation using human umbilical vein endothelial cells (HUVECs).
  • Investigation of integrin-mediated cell-substrate interactions, including binding affinity and strength to α(5)β(1).

Main Results:

  • P-PN5 demonstrated comparable HUVEC adhesion and growth support to P-GS5.
  • PHSRN-modified polymers showed similar binding affinity and strength to α(5)β(1) as GRGDS-modified polymers.
  • PHSRN independently mediated HUVEC adhesion and growth.

Conclusions:

  • The peptide PHSRN is capable of mediating human umbilical vein endothelial cell adhesion and growth.
  • PHSRN-modified polymers exhibit potential as biologically compatible materials.
  • These findings support the use of PHSRN-functionalized biomaterials in regenerative medicine and tissue engineering.