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Title: Type I Collagen and Collagen Mimetics as Angiogenesis Promoting Superpolymers

Abstract

Angiogenesis, the development of blood vessels from the pre-existing vasculature, is a key component of embryogenesis and tissue regeneration. Angiogenesis also drives pathologies such as tumor growth and metastasis, and hemangioma development in newborns. On the other hand, promotion of angiogenesis is needed in tissues with vascular insufficiencies, and in bioengineering, to endow tissue substitutes with appropriate microvasculatures. Therefore, much research has focused on defining mechanisms of angiogenesis, and identifying pro- and anti-angiogenic molecules. Type I collagen, the most abundant protein in humans, potently stimulates angiogenesis in vitro and in vivo. Crucial to its angiogenic activity appears to be ligation and possibly clustering of endothelial cell (EC) surface {alpha}1{beta}1/{alpha}2{beta}1 integrin receptors by the GFPGER502-507 sequence of the collagen fibril. However, additional aspects of collagen structure and function that may modulate its angiogenic properties are discussed. Moreover, type I collagen and fibrin, another angiogenic polymer, share several structural features. These observations suggest strategies for creating 'angiogenic superpolymers', including: modifying type I collagen to influence its biological half-life, immunogenicity, and integrin binding capacity; genetically engineering fibrillar collagens to include additional integrin binding sites or angiogenic determinants, and remove unnecessary or deleterious sequences without compromising fibril integrity; and exploring the suitability of poly(orthomore » ester), PEG-lysine copolymer, tubulin, and cholesteric cuticle as collagen mimetics, and suggesting means of modifying them to display ideal angiogenic properties. The collagenous and collagen mimetic angiogenic superpolymers described here may someday prove useful for many applications in tissue engineering and human medicine.« less

Authors:
; ; ;  [1];  [2];  [2]
  1. (TJU)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1007649
Resource Type:
Journal Article
Resource Relation:
Journal Name: Curr. Pharm. Design; Journal Volume: 13; Journal Issue: 2007
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; ANGIOMAS; BIOLOGICAL HALF-LIFE; BLOOD VESSELS; CAPACITY; COLLAGEN; FIBRIN; IN VITRO; IN VIVO; MEDICINE; NEOPLASMS; PROTEINS; REGENERATION

Citation Formats

Twardowski, T., Fertala, A., Orgel, J.P.R.O., San Antonio, J.D., IIT), and Widener). Type I Collagen and Collagen Mimetics as Angiogenesis Promoting Superpolymers. United States: N. p., 2008. Web.
Twardowski, T., Fertala, A., Orgel, J.P.R.O., San Antonio, J.D., IIT), & Widener). Type I Collagen and Collagen Mimetics as Angiogenesis Promoting Superpolymers. United States.
Twardowski, T., Fertala, A., Orgel, J.P.R.O., San Antonio, J.D., IIT), and Widener). Fri . "Type I Collagen and Collagen Mimetics as Angiogenesis Promoting Superpolymers". United States.
@article{osti_1007649,
title = {Type I Collagen and Collagen Mimetics as Angiogenesis Promoting Superpolymers},
author = {Twardowski, T. and Fertala, A. and Orgel, J.P.R.O. and San Antonio, J.D. and IIT) and Widener)},
abstractNote = {Angiogenesis, the development of blood vessels from the pre-existing vasculature, is a key component of embryogenesis and tissue regeneration. Angiogenesis also drives pathologies such as tumor growth and metastasis, and hemangioma development in newborns. On the other hand, promotion of angiogenesis is needed in tissues with vascular insufficiencies, and in bioengineering, to endow tissue substitutes with appropriate microvasculatures. Therefore, much research has focused on defining mechanisms of angiogenesis, and identifying pro- and anti-angiogenic molecules. Type I collagen, the most abundant protein in humans, potently stimulates angiogenesis in vitro and in vivo. Crucial to its angiogenic activity appears to be ligation and possibly clustering of endothelial cell (EC) surface {alpha}1{beta}1/{alpha}2{beta}1 integrin receptors by the GFPGER502-507 sequence of the collagen fibril. However, additional aspects of collagen structure and function that may modulate its angiogenic properties are discussed. Moreover, type I collagen and fibrin, another angiogenic polymer, share several structural features. These observations suggest strategies for creating 'angiogenic superpolymers', including: modifying type I collagen to influence its biological half-life, immunogenicity, and integrin binding capacity; genetically engineering fibrillar collagens to include additional integrin binding sites or angiogenic determinants, and remove unnecessary or deleterious sequences without compromising fibril integrity; and exploring the suitability of poly(ortho ester), PEG-lysine copolymer, tubulin, and cholesteric cuticle as collagen mimetics, and suggesting means of modifying them to display ideal angiogenic properties. The collagenous and collagen mimetic angiogenic superpolymers described here may someday prove useful for many applications in tissue engineering and human medicine.},
doi = {},
journal = {Curr. Pharm. Design},
number = 2007,
volume = 13,
place = {United States},
year = {Fri Jul 18 00:00:00 EDT 2008},
month = {Fri Jul 18 00:00:00 EDT 2008}
}