The regulatory function of SPARC in vascular biology

Multi-author review

DOI: 10.1007/s00018-011-0781-8

Cite this article as:
Rivera, L.B., Bradshaw, A.D. & Brekken, R.A. Cell. Mol. Life Sci. (2011) 68: 3165. doi:10.1007/s00018-011-0781-8

Abstract

SPARC is a matricellular protein, able to modulate cell/ECM interactions and influence cell responses to growth factors, and therefore is particularly attuned to contribute to physiological processes involving changes in ECM and cell mobilization. Indeed, the list of biological processes affected by SPARC includes wound healing, tumor progression, bone formation, fibrosis, and angiogenesis. The process of angiogenesis is complex and involves a number of cellular processes such as endothelial cell proliferation, migration, ECM degradation, and synthesis, as well as pericyte recruitment to stabilize nascent vessels. In this review, we will summarize current results that explore the function of SPARC in the regulation of angiogenic events with a particular emphasis on the modulation of growth factor activity by SPARC in the context of blood vessel formation. The primary function of SPARC in angiogenesis remains unclear, as SPARC activity in some circumstances promotes angiogenesis and in others is more consistent with an anti-angiogenic activity. Undoubtedly, the mercurial nature of SPARC belies a redundancy of functional proteins in angiogenesis as well as cell-type-specific activities that alter signal transduction events in response to unique cellular milieus. Nonetheless, the investigation of cellular mechanisms that define functional activities of SPARC continue to contribute novel and exciting paradigms to vascular biology.

Keywords

SPARC/osteonectin TGF-β Angiogenesis Extracellular matrix 

Abbreviations

SPARC

Secreted protein acidic and rich in cysteine

ECM

Extracellular matrix

PDGF

Platelet-derived growth factor

VEGF

Vascular endothelial growth factor

VEGFR1

VEGF receptor 1

VEGFR2

VEGF receptor 2

FGF

Fibroblast growth factor

TGF-β

Transforming growth factor-beta

BMP

Bone morphogenic protein

αSMA

Alpha smooth muscle actin

ER

Endoplasmic reticulum

ILK

Integrin-linked kinase

SHP-1

Src homology region 2 domain-containing phosphatase-1

CNV

Choroidal neovascularization

Copyright information

© Springer Basel AG 2011

Authors and Affiliations

  1. 1.Departments of Surgery and Pharmacology and the Hamon Center for Therapeutic Oncology ResearchUT Southwestern Medical CenterDallasUSA
  2. 2.Department of Medicine, Gazes Cardiac Research InstituteMedical University of South CarolinaCharlestonUSA

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