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MMP-13 substrate specificity in cartilage breakdown

Mannaa, Atef LU (2012) KEMR16 20121
Department of Chemistry
Abstract
Abstract
MMP13 (Collagenase 3) is a member of the matrix metalloproteinase (MMP) family. In
pathology it is overexpressed in rheumatoid arthritis (RA), osteoarthritis (OA) and human
carcinomas. It is secreted in its inactive proforms from which it can be activated. The project
studies how MMP13 can degrade/digest the normal femoral head human articular cartilage.
Peptides were separated using reversed phase chromatography coupled on-line with various
mass spectrometry techniques including ion trap, quadropole Time-Of-Flight (Q-TOF) and
triple quadropole (QQQ) instruments. Guanidine hydrochloride (GuHCl) was used to extract
proteins from the cartilage tissue. Sodium dodecyl sulfate poly acrylamide gel electrophoresis
was used also... (More)
Abstract
MMP13 (Collagenase 3) is a member of the matrix metalloproteinase (MMP) family. In
pathology it is overexpressed in rheumatoid arthritis (RA), osteoarthritis (OA) and human
carcinomas. It is secreted in its inactive proforms from which it can be activated. The project
studies how MMP13 can degrade/digest the normal femoral head human articular cartilage.
Peptides were separated using reversed phase chromatography coupled on-line with various
mass spectrometry techniques including ion trap, quadropole Time-Of-Flight (Q-TOF) and
triple quadropole (QQQ) instruments. Guanidine hydrochloride (GuHCl) was used to extract
proteins from the cartilage tissue. Sodium dodecyl sulfate poly acrylamide gel electrophoresis
was used also to give visualize similarities and differences between the control and the
MMP13 treated sample. MMP13 showed an effect on both media (released proteins from the
cartilage tissue via the buffer solution) and a little effect on the cartilage tissue (pellet). The
main result showed that the tissue sample preparation was critical in order to obtain sufficient
release of proteins. The powderisation of tissue was much better in releasing proteins than
intact tissue plugs probably due to larger contact area and shorter diffusion distance. (Less)
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author
Mannaa, Atef LU
supervisor
organization
course
KEMR16 20121
year
type
H2 - Master's Degree (Two Years)
subject
keywords
Analytisk kemi
language
English
id
3053542
date added to LUP
2012-09-19 11:27:25
date last changed
2012-09-19 11:27:25
@misc{3053542,
  abstract     = {Abstract
MMP13 (Collagenase 3) is a member of the matrix metalloproteinase (MMP) family. In
pathology it is overexpressed in rheumatoid arthritis (RA), osteoarthritis (OA) and human
carcinomas. It is secreted in its inactive proforms from which it can be activated. The project
studies how MMP13 can degrade/digest the normal femoral head human articular cartilage.
Peptides were separated using reversed phase chromatography coupled on-line with various
mass spectrometry techniques including ion trap, quadropole Time-Of-Flight (Q-TOF) and
triple quadropole (QQQ) instruments. Guanidine hydrochloride (GuHCl) was used to extract
proteins from the cartilage tissue. Sodium dodecyl sulfate poly acrylamide gel electrophoresis
was used also to give visualize similarities and differences between the control and the
MMP13 treated sample. MMP13 showed an effect on both media (released proteins from the
cartilage tissue via the buffer solution) and a little effect on the cartilage tissue (pellet). The
main result showed that the tissue sample preparation was critical in order to obtain sufficient
release of proteins. The powderisation of tissue was much better in releasing proteins than
intact tissue plugs probably due to larger contact area and shorter diffusion distance.},
  author       = {Mannaa, Atef},
  keyword      = {Analytisk kemi},
  language     = {eng},
  note         = {Student Paper},
  title        = {MMP-13 substrate specificity in cartilage breakdown},
  year         = {2012},
}