PMID- 21688302
OWN - NLM
STAT- MEDLINE
DCOM- 20120224
LR  - 20211020
IS  - 1097-4644 (Electronic)
IS  - 0730-2312 (Print)
IS  - 0730-2312 (Linking)
VI  - 112
IP  - 11
DP  - 2011 Nov
TI  - Proteolysis of the matricellular protein hevin by matrix metalloproteinase-3 
      produces a SPARC-like fragment (SLF) associated with neovasculature in a murine 
      glioma model.
PG  - 3093-102
LID - 10.1002/jcb.23235 [doi]
AB  - The matricellular SPARC-family member hevin (Sparc-like 1/SPARCL-1/SC1/Mast9) 
      contributes to neural development and alters tumor progression in a range of 
      mammalian models. Based on sequence similarity, we hypothesized that proteolytic 
      digestion of hevin would result in SPARC-like fragments (SLF) that affect the 
      activity and/or location of these proteins. Incubation of hevin with matrix 
      metalloproteinase-3 (MMP-3), a protease known to cleave SPARC, produced a limited 
      number of peptides. Sequencing revealed the major proteolytic products to be 
      SPARC-like in primary structure. In gliomas implanted into murine brain, a SLF 
      was associated with SPARC in the neovasculature but not with hevin, the latter 
      prominent in the astrocytes encompassed by infiltrating tumor. In this model of 
      invasive glioma that involves MMP-3 activity, host-derived SLF was not observed 
      in the extracellular matrix adjacent to tumor cells. In contrast, it occurred 
      with its homolog SPARC in the angiogenic response to the tumor. We conclude that 
      MMP-3-derived SLF is a marker of neovessels in glioma, where it could influence 
      the activity of SPARC.
CI  - Copyright (c) 2011 Wiley Periodicals, Inc.
FAU - Weaver, Matt
AU  - Weaver M
AD  - Benaroya Research Institute, 1201 Ninth Avenue, Seattle, Washington 98101, USA.
FAU - Workman, Gail
AU  - Workman G
FAU - Schultz, Chad R
AU  - Schultz CR
FAU - Lemke, Nancy
AU  - Lemke N
FAU - Rempel, Sandra A
AU  - Rempel SA
FAU - Sage, E Helene
AU  - Sage EH
LA  - eng
GR  - R01 GM040711-22/GM/NIGMS NIH HHS/United States
GR  - R01 GM040711/GM/NIGMS NIH HHS/United States
GR  - CA86997/CA/NCI NIH HHS/United States
GR  - R01 CA086997/CA/NCI NIH HHS/United States
GR  - GM40711/GM/NIGMS NIH HHS/United States
GR  - R01 CA086997-07/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - United States
TA  - J Cell Biochem
JT  - Journal of cellular biochemistry
JID - 8205768
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Extracellular Matrix Proteins)
RN  - 0 (Osteonectin)
RN  - 0 (Sparcl1 protein, mouse)
RN  - EC 3.4.24.17 (Matrix Metalloproteinase 3)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brain Neoplasms/blood supply/enzymology/*metabolism
MH  - CHO Cells
MH  - Calcium-Binding Proteins/*metabolism
MH  - Cell Line, Tumor
MH  - Cricetinae
MH  - Cricetulus
MH  - Disease Models, Animal
MH  - Extracellular Matrix Proteins/*metabolism
MH  - Glioma/blood supply/enzymology/*metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - Matrix Metalloproteinase 3/chemistry/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - *Neovascularization, Pathologic
MH  - Osteonectin/*metabolism
MH  - Proteolysis
MH  - Transplantation, Heterologous
PMC - PMC3188378
MID - NIHMS305974
EDAT- 2011/06/21 06:00
MHDA- 2012/03/01 06:00
PMCR- 2012/11/01
CRDT- 2011/06/21 06:00
PHST- 2011/06/21 06:00 [entrez]
PHST- 2011/06/21 06:00 [pubmed]
PHST- 2012/03/01 06:00 [medline]
PHST- 2012/11/01 00:00 [pmc-release]
AID - 10.1002/jcb.23235 [doi]
PST - ppublish
SO  - J Cell Biochem. 2011 Nov;112(11):3093-102. doi: 10.1002/jcb.23235.